{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T16:59:30Z","timestamp":1790182770625,"version":"4.1.0"},"publisher-location":"New York, NY","reference-count":161,"publisher":"Springer US","isbn-type":[{"value":"9781071654712","type":"print"},{"value":"9781071654729","type":"electronic"}],"license":[{"start":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T00:00:00Z","timestamp":1790208000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T00:00:00Z","timestamp":1790208000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2027]]},"DOI":"10.1007\/978-1-0716-5472-9_1","type":"book-chapter","created":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T15:59:40Z","timestamp":1790179180000},"page":"3-28","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Lipases: An Overview"],"prefix":"10.1007","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1815-0133","authenticated-orcid":false,"given":"David A.","family":"Torres-A\u00f1orve","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0003-5570-4048","authenticated-orcid":false,"given":"Elisa","family":"Gutierrez-Navarro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9105-0702","authenticated-orcid":false,"given":"Georgina","family":"Sandoval","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,9,24]]},"reference":[{"key":"1_CR1","doi-asserted-by":"publisher","unstructured":"Godoy CA, Pardo-Tamayo JS, Barbosa O (2022) Microbial lipases and their potential in the production of pharmaceutical building blocks. Int J Mol Sci 23(17):9933. https:\/\/doi.org\/10.3390\/ijms23179933","DOI":"10.3390\/ijms23179933"},{"issue":"1","key":"1_CR2","doi-asserted-by":"publisher","first-page":"169","DOI":"10.1186\/s12934-020-01428-8","volume":"19","author":"P Chandra","year":"2020","unstructured":"Chandra P, Singh R, Arora PK (2020) Microbial lipases and their industrial applications: a comprehensive review. Microb Cell Fact 19(1):169. https:\/\/doi.org\/10.1186\/s12934-020-01428-8","journal-title":"Microb Cell Fact"},{"issue":"1","key":"1_CR3","doi-asserted-by":"publisher","first-page":"45","DOI":"10.2174\/1872208312666181029093333","volume":"13","author":"N Patel","year":"2019","unstructured":"Patel N, Rai D, Shivam, Shahane S, Mishra U (2019) Lipases: sources, production, purification, and applications. Recent Pat Biotechnol 13(1):45\u201356. https:\/\/doi.org\/10.2174\/1872208312666181029093333","journal-title":"Recent Pat Biotechnol"},{"key":"1_CR4","doi-asserted-by":"publisher","unstructured":"Lai OM, Phuah ET, Lee YY, Akoh CC, Weete JD (2017) Microbial lipases. In: Akoh CC (ed) Food lipids: chemistry, nutrition, and biotechnology, 4th edn. CRC Press. pp 853\u2013898. https:\/\/doi.org\/10.1201\/9781315151854","DOI":"10.1201\/9781315151854"},{"key":"1_CR5","doi-asserted-by":"publisher","first-page":"358","DOI":"10.1016\/j.ijbiomac.2020.04.061","volume":"158","author":"L Silvestrini","year":"2020","unstructured":"Silvestrini L, Cianci M (2020) Principles of lipid-enzyme interactions in the limbus region of the catalytic site of Candida antarctica Lipase B. Int J Biol Macromol 158:358\u2013363. https:\/\/doi.org\/10.1016\/j.ijbiomac.2020.04.061","journal-title":"Int J Biol Macromol"},{"issue":"9","key":"1_CR6","doi-asserted-by":"publisher","first-page":"960","DOI":"10.3390\/catal12090960","volume":"12","author":"AL Reyes-Reyes","year":"2022","unstructured":"Reyes-Reyes AL, Valero Barranco F, Sandoval G (2022) Recent advances in lipases and their applications in the food and nutraceutical industry. Catalysts 12(9):960","journal-title":"Catalysts"},{"issue":"1","key":"1_CR7","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1002\/btpr.2581","volume":"34","author":"N Sarmah","year":"2018","unstructured":"Sarmah N, Revathi D, Sheelu G, Yamuna Rani K, Sridhar S, Mehtab V, Sumana C (2018) Recent advances on sources and industrial applications of lipases. Biotechnol Prog 34(1):5\u201328. https:\/\/doi.org\/10.1002\/btpr.2581","journal-title":"Biotechnol Prog"},{"issue":"9","key":"1_CR8","doi-asserted-by":"publisher","first-page":"20774","DOI":"10.3390\/ijms160920774","volume":"16","author":"GM Borrelli","year":"2015","unstructured":"Borrelli GM, Trono D (2015) Recombinant lipases and phospholipases and their use as biocatalysts for industrial applications. Int J Mol Sci 16(9):20774\u201320840. https:\/\/doi.org\/10.3390\/ijms160920774","journal-title":"Int J Mol Sci"},{"issue":"9","key":"1_CR9","doi-asserted-by":"publisher","first-page":"2441","DOI":"10.1002\/slct.201702954","volume":"3","author":"BP Dwivedee","year":"2018","unstructured":"Dwivedee BP, Soni S, Sharma M, Bhaumik J, Laha JK, Banerjee UC (2018) Promiscuity of lipase-catalyzed reactions for organic synthesis: a recent update. ChemistrySelect 3(9):2441\u20132466. https:\/\/doi.org\/10.1002\/slct.201702954","journal-title":"ChemistrySelect"},{"issue":"2","key":"1_CR10","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1080\/15422119.2018.1564328","volume":"49","author":"NB Melani","year":"2020","unstructured":"Melani NB, Tambourgi EB, Silveira E (2020) Lipases: from production to applications. Sep Purif Rev 49(2):143\u2013158. https:\/\/doi.org\/10.1080\/15422119.2018.1564328","journal-title":"Sep Purif Rev"},{"issue":"4","key":"1_CR11","doi-asserted-by":"publisher","DOI":"10.1051\/ocl\/2017031","volume":"24","author":"D Guerrand","year":"2017","unstructured":"Guerrand D (2017) Lipases industrial applications: focus on food and agroindustries. OCL 24(4), D403. https:\/\/doi.org\/10.1051\/ocl\/2017031","journal-title":"OCL"},{"issue":"10","key":"1_CR12","doi-asserted-by":"publisher","first-page":"2380","DOI":"10.1039\/c9cy00415g","volume":"9","author":"C Ortiz","year":"2019","unstructured":"Ortiz C, Ferreira ML, Barbosa O, Dos Santos JCS, Rodrigues RC, Berenguer-Murcia \u00c1, Briand LE, Fernandez-Lafuente R (2019) Novozym 435: the \u201cperfect\u201d lipase immobilized biocatalyst?. Catal Sci Technol 9(10):2380\u20132420. https:\/\/doi.org\/10.1039\/c9cy00415g","journal-title":"Catal Sci Technol"},{"key":"1_CR13","doi-asserted-by":"publisher","first-page":"70","DOI":"10.1016\/j.procbio.2017.01.027","volume":"55","author":"A Guti\u00e9rrez-Ortega","year":"2017","unstructured":"Guti\u00e9rrez-Ortega A, Rivera I, Cruz-Franco S, Guti\u00e9rrez-Mora A, Alpuche-Sol\u00eds \u00c1G, S\u00e1nchez-Hern\u00e1ndez C, Horchani H, Sandoval G (2017) Identification, cloning and expression of a new GDSL lipase from Carica papaya. Process Biochem 55:70\u201376. https:\/\/doi.org\/10.1016\/j.procbio.2017.01.027","journal-title":"Process Biochem"},{"issue":"5700","key":"1_CR14","doi-asserted-by":"publisher","first-page":"1383","DOI":"10.1126\/science.1100747","volume":"306","author":"R Zimmermann","year":"2004","unstructured":"Zimmermann R, Strauss JG, Haemmerle G, Schoiswohl G, Birner-Gruenberger R, Riederer M, Lass A, Neuberger G, Eisenhaber F, Hermetter A, Zechner R (2004) Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase. Science 306(5700):1383\u20131386. https:\/\/doi.org\/10.1126\/science.1100747","journal-title":"Science"},{"key":"1_CR15","doi-asserted-by":"publisher","first-page":"110314","DOI":"10.1016\/j.biopha.2020.110314","volume":"128","author":"T-T Liu","year":"2020","unstructured":"Liu T-T, Liu X-T, Chen Q-X, Shi Y (2020) Lipase Inhibitors for obesity: a review. Biomed Pharmacother 128:110314. https:\/\/doi.org\/10.1016\/j.biopha.2020.110314","journal-title":"Biomed Pharmacother"},{"key":"1_CR16","doi-asserted-by":"publisher","unstructured":"Barrero JJ, Casler JC, Valero F, Ferrer P, Glick BS (2018) An improved secretion signal enhances the secretion of model proteins from Pichia pastoris. Microb Cell Fact 17(1):161. https:\/\/doi.org\/10.1186\/s12934-018-1009-5","DOI":"10.1186\/s12934-018-1009-5"},{"issue":"2","key":"1_CR17","doi-asserted-by":"publisher","first-page":"117","DOI":"10.1016\/j.jbiotec.2011.06.035","volume":"156","author":"F Bordes","year":"2011","unstructured":"Bordes F, Tarquis L, Nicaud JM, Marty A (2011) Isolation of a thermostable variant of Lip2 lipase from Yarrowia lipolytica by directed evolution and deeper insight into the denaturation mechanisms involved. J Biotech 156(2):117\u2013124. https:\/\/doi.org\/10.1016\/j.jbiotec.2011.06.035","journal-title":"J Biotech"},{"issue":"2","key":"1_CR18","doi-asserted-by":"publisher","first-page":"345","DOI":"10.1007\/s00792-016-0907-x","volume":"21","author":"LJ Kang","year":"2017","unstructured":"Kang LJ, Meng ZT, Hu C, Zhang Y, Guo HL, Li Q, Li M (2017) Screening, purification, and characterization of a novel organic solvent-tolerant esterase, Lip2, from Monascus purpureus strain M7. Extremophiles 21(2):345\u2013355. https:\/\/doi.org\/10.1007\/s00792-016-0907-x","journal-title":"Extremophiles"},{"issue":"5","key":"1_CR19","doi-asserted-by":"publisher","first-page":"634","DOI":"10.1111\/j.1751-7915.2012.00354.x","volume":"5","author":"F Darvishi","year":"2012","unstructured":"Darvishi F (2012) Expression of native and mutant extracellular lipases from Yarrowia lipolytica in Saccharomyces cerevisiae. Microb Biotechnol 5(5):634\u2013641. https:\/\/doi.org\/10.1111\/j.1751-7915.2012.00354.x","journal-title":"Microb Biotechnol"},{"key":"1_CR20","doi-asserted-by":"publisher","first-page":"767","DOI":"10.1038\/343767a0","volume":"343","author":"L Brady","year":"1990","unstructured":"Brady L, Brzozowski AM, Derewenda ZS, Dodson E, Dodson G, Tolley S (1990) A serine protease triad forms the catalytic centre of a triacylglycerol lipase. Nature 343:767\u2013770. https:\/\/doi.org\/10.1038\/343767a0","journal-title":"Nature"},{"key":"1_CR21","doi-asserted-by":"publisher","first-page":"771","DOI":"10.1038\/343771a0","volume":"343","author":"FK Winkler","year":"1990","unstructured":"Winkler FK, D\u2019Arcy A, Hunziker W (1990) Structure of human pancreatic lipase. Nature 343:771\u2013774. https:\/\/doi.org\/10.1038\/343771a0","journal-title":"Nature"},{"key":"1_CR22","doi-asserted-by":"publisher","unstructured":"Casas-Godoy L, Duquesne S, Bordes F, Sandoval G, Marty A (2012) Lipases: an overview. Methods Mol Biol 861, https:\/\/doi.org\/10.1007\/978-1-61779-600-5_1","DOI":"10.1007\/978-1-61779-600-5_1"},{"issue":"7873","key":"1_CR23","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","volume":"596","author":"J Jumper","year":"2021","unstructured":"Jumper J, Evans R, Pritzel A, Green T, Figurnov M, Ronneberger O, Tunyasuvunakool K, Bates R, \u017d\u00eddek A, Potapenko A, Bridgland A, Meyer C, Kohl SAA, Ballard AJ, Cowie A, Romera-Paredes B, Nikolov S, Jain R, Adler J, Back T, Petersen S, Reiman D, Clancy E, Zielinski M, Steinegger M, Pacholska M, Berghammer T, Bodenstein S, Silver D, Vinyals O, Senior AW, Kavukcuoglu K, Kohli P, Hassabis D (2021) Highly accurate protein structure prediction with AlphaFold. Nature 596(7873):583\u2013589. https:\/\/doi.org\/10.1038\/s41586-021-03819-2","journal-title":"Nature"},{"issue":"D1","key":"1_CR24","doi-asserted-by":"publisher","first-page":"D439","DOI":"10.1093\/nar\/gkab1061","volume":"50","author":"M Varadi","year":"2021","unstructured":"Varadi M, Anyango S, Deshpande M, Nair S, Natassia C, Yordanova G, Yuan D, Stroe O, Wood G, Laydon A, \u017d\u00eddek A, Green T, Tunyasuvunakool K, Petersen S, Jumper J, Clancy E, Green R, Vora A, Lutfi M, Figurnov M, Cowie A, Hobbs N, Kohli P, Kleywegt G, Birney E, Hassabis D, Velankar S (2021) AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models. Nucleic Acids Res 50(D1):D439\u2013D444. https:\/\/doi.org\/10.1093\/nar\/gkab1061","journal-title":"Nucleic Acids Res"},{"issue":"6557","key":"1_CR25","doi-asserted-by":"publisher","first-page":"871","DOI":"10.1126\/science.abj8754","volume":"373","author":"M Baek","year":"2021","unstructured":"Baek M, DiMaio F, Anishchenko I, Dauparas J, Ovchinnikov S, Lee GR, Wang J, Cong Q, Kinch LN, Schaeffer RD, Mill\u00e1n C, Park H, Adams C, Glassman CR, DeGiovanni A, Pereira JH, Rodrigues AV, van Dijk AA, Ebrecht AC, Opperman DJ, Sagmeister T, Buhlheller C, Pavkov-Keller T, Rathinaswamy MK, Dalwadi U, Yip CK, Burke JE, Garcia KC, Grishin NV, Adams PD, Read RJ, Baker D (2021) Accurate prediction of protein structures and interactions using a three-track neural network. Science 373(6557):871\u2013876. https:\/\/doi.org\/10.1126\/science.abj8754","journal-title":"Science"},{"issue":"12","key":"1_CR26","doi-asserted-by":"publisher","first-page":"2366","DOI":"10.1111\/febs.14814","volume":"286","author":"W Huang","year":"2019","unstructured":"Huang W, Lan D, Popowicz GM, Zak KM, Zhao Z, Yuan H, Yang B, Wang Y (2019) Structure and characterization of Aspergillus fumigatus lipase B with a unique, oversized regulatory subdomain. FEBS J 286(12):2366\u20132380. https:\/\/doi.org\/10.1111\/febs.14814","journal-title":"FEBS J"},{"issue":"2","key":"1_CR27","doi-asserted-by":"publisher","first-page":"302","DOI":"10.1016\/j.bbapap.2007.10.012","volume":"1784","author":"E Rajakumara","year":"2008","unstructured":"Rajakumara E, Acharya P, Ahmad S, Sankaranaryanan R, Rao NM (2008) Structural basis for the remarkable stability of Bacillus subtilis lipase (Lip A) at low pH. Biochim Biophys Acta (BBA) 1784(2):302\u2013311. https:\/\/doi.org\/10.1016\/j.bbapap.2007.10.012","journal-title":"Biochim Biophys Acta (BBA)"},{"issue":"1","key":"1_CR28","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1002\/cbic.200500308","volume":"7","author":"MJ Dr\u00f6ge","year":"2006","unstructured":"Dr\u00f6ge MJ, Boersma YL, van Pouderoyen G, Vrenken TE, R\u00fcggeberg CJ, Reetz MT, Dijkstra BW, Quax WJ (2006) Directed evolution of Bacillus subtilis lipase A by use of enantiomeric phosphonate inhibitors: crystal structures and phage display selection. ChemBioChem 7(1):149\u2013157. https:\/\/doi.org\/10.1002\/cbic.200500308","journal-title":"ChemBioChem"},{"issue":"1","key":"1_CR29","doi-asserted-by":"publisher","first-page":"215","DOI":"10.1006\/jmbi.2001.4659","volume":"309","author":"G van Pouderoyen","year":"2001","unstructured":"van Pouderoyen G, Eggert T, Jaeger K-E, Dijkstra BW (2001) The crystal structure of Bacillus subtili lipase: a minimal \u03b1\/\u03b2 hydrolase fold enzyme. J Mol Biol 309(1):215\u2013226. https:\/\/doi.org\/10.1006\/jmbi.2001.4659","journal-title":"J Mol Biol"},{"key":"1_CR30","doi-asserted-by":"publisher","unstructured":"Kim KK, Song HK, Shin DH, Hwang KY, Suh SW (1997) The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor. Structure 5:173\u2013185. https:\/\/doi.org\/10.1016\/S0969-2126(97)00177-9","DOI":"10.1016\/S0969-2126(97)00177-9"},{"key":"1_CR31","doi-asserted-by":"publisher","unstructured":"Schrag JD, Li Y, Cygler M, Lang D, Burgdorf T, Hecht HJJ (1997) The open conformation of a Pseudomonas lipase. Structure 5:187\u2013202. https:\/\/doi.org\/10.1016\/S0969-2126(97)00178-0","DOI":"10.1016\/S0969-2126(97)00178-0"},{"key":"1_CR32","doi-asserted-by":"publisher","unstructured":"Lang DA, Mannesse ML, Haas GH, Verheij HM, Dijkstra BW (1998) Structural basis of the chiral selectivity of Pseudomonas cepacia lipase. Eur J Biochem 254:333\u2013340. https:\/\/doi.org\/10.1046\/j.1432-1327.1998.2540333.x","DOI":"10.1046\/j.1432-1327.1998.2540333.x"},{"issue":"14","key":"1_CR33","doi-asserted-by":"publisher","first-page":"3964","DOI":"10.1046\/j.1432-1327.2001.02303.x","volume":"268","author":"M Lui\u0107","year":"2001","unstructured":"Lui\u0107 M, Tomi\u0107 S, Le\u0161\u010di\u0107 I, Ljubovi\u0107 E, \u0160epac D, \u0160unji\u0107 V, Vitale L, Saenger W, Koji\u0107-Prodi\u0107 B (2001) Complex of Burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane. Eur J Biochem 268(14):3964\u20133973. https:\/\/doi.org\/10.1046\/j.1432-1327.2001.02303.x","journal-title":"Eur J Biochem"},{"key":"1_CR34","doi-asserted-by":"publisher","unstructured":"Mezzetti A, Schrag JD, Cheong CS, Kazlauskas RJ (2005) Mirror-image packing in enantiomer discrimination: molecular basis for the enantioselectivity of B. cepacia lipase toward 2-methyl-3-phenyl-1-propanol. Chem Biol 12:427\u2013437. https:\/\/doi.org\/10.1016\/j.chembiol.2005.01.016","DOI":"10.1016\/j.chembiol.2005.01.016"},{"key":"1_CR35","doi-asserted-by":"publisher","unstructured":"Lui\u0107 M, \u0160tefani\u0107 Z, Ceilinger I, Hodo\u0161\u010dek M, Jane\u017ei\u010d D, Lenac T (2008) Combined X-ray diffraction and QM\/MM study of the Burkholderia cepacia lipase-catalyzed secondary alcohol esterification. J Phys Chem B 112(16):4876\u20134883. https:\/\/doi.org\/10.1021\/jp077717u","DOI":"10.1021\/jp077717u"},{"key":"1_CR36","doi-asserted-by":"publisher","unstructured":"Grochulski P, Li Y, Schrag JD, Bouthillier F, Smith P, Harrison D (1993) Insights into interfacial activation from an open structure of Candida rugosa lipase. J Biol Chem 268(17):12843\u201312847. https:\/\/doi.org\/10.1016\/S0021-9258(18)31464-9","DOI":"10.1016\/S0021-9258(18)31464-9"},{"key":"1_CR37","doi-asserted-by":"publisher","unstructured":"Grochulski P, Li Y, Schrag JD, Cygler M (1994) Two conformational states of Candida rugosa lipase. Protein Sci 3:82\u201391. https:\/\/doi.org\/10.1002\/pro.5560030111","DOI":"10.1002\/pro.5560030111"},{"key":"1_CR38","doi-asserted-by":"publisher","unstructured":"Grochulski P, Bouthillier F, Kazlauskas RJ, Serreqi AN, Schrag JD, Ziomek E (1994) Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase. Biochemistry 33:3494\u20133500. https:\/\/doi.org\/10.1021\/bi00178a005","DOI":"10.1021\/bi00178a005"},{"key":"1_CR39","doi-asserted-by":"publisher","unstructured":"Cygler M, Grochulskui P, Kazlauskas R, Schrag JD, Bouthiller F, Rubin B (1994) A structural basis for the chiral preferences of lipases. J Am Chem Soc 116:3180\u20133186. https:\/\/doi.org\/10.1021\/ja00087a002","DOI":"10.1021\/ja00087a002"},{"key":"1_CR40","doi-asserted-by":"publisher","unstructured":"Manche\u00f1o JM, Pernas MA, Mart\u00ednez MJ, Ochoa B, R\u00faa ML, Hermoso JA (2003) Structural insights into the lipase\/esterase behavior in the Candida rugosa lipases family: crystal structure of the lipase 2 isoenzyme at 1.97A resolution. J Mol Biol 332:1059\u20131069. https:\/\/doi.org\/10.1016\/j.jmb.2003.08.005","DOI":"10.1016\/j.jmb.2003.08.005"},{"issue":"13","key":"1_CR41","doi-asserted-by":"publisher","first-page":"2529","DOI":"10.1002\/adsc.201100459","volume":"353","author":"IJ Colton","year":"2011","unstructured":"Colton IJ, Yin D, Grochulski P, Kazlauskas RJ (2011) Molecular basis of chiral acid recognition by Candida rugosa lipase: X-ray structure of transition state analog and modeling of the hydrolysis of methyl 2-methoxy-2-phenylacetate. Adv Synth Catal 353(13):2529\u20132544. https:\/\/doi.org\/10.1002\/adsc.201100459","journal-title":"Adv Synth Catal"},{"issue":"2","key":"1_CR42","doi-asserted-by":"publisher","first-page":"575","DOI":"10.1006\/jmbi.1993.1171","volume":"230","author":"JD Schrag","year":"1993","unstructured":"Schrag JD, Cygler M (1993) 1\u00b78 \u00c5 refined structure of the lipase from Geotrichum candidum. J Mol Biol 230(2):575\u2013591. https:\/\/doi.org\/10.1006\/jmbi.1993.1171","journal-title":"J Mol Biol"},{"key":"1_CR43","doi-asserted-by":"publisher","unstructured":"Tilbeurgh H, Sarda L, Verger R, Cambillau C (1992) Structure of the pancreatic lipase-procolipase complex. Nature 359:159\u2013162. https:\/\/doi.org\/10.1038\/359159a0","DOI":"10.1038\/359159a0"},{"key":"1_CR44","doi-asserted-by":"publisher","unstructured":"Eydoux C, Spinelli S, Davis TL, Walker JR, Seitova A, Dhe-Paganon S (2008) Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation. Biochemistry 47:9553\u20139564. https:\/\/doi.org\/10.1021\/bi8005576","DOI":"10.1021\/bi8005576"},{"key":"1_CR45","doi-asserted-by":"publisher","unstructured":"Uppenberg J, Hansen MT, Patkar S, Jones TA (1994) The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica. Structure 2:293\u2013308. https:\/\/doi.org\/10.1016\/S0969-2126(00)00031-9","DOI":"10.1016\/S0969-2126(00)00031-9"},{"key":"1_CR46","doi-asserted-by":"publisher","unstructured":"Uppenberg J, Ohrner N, Norin M, Hult K, Kleywegt GJ, Patkar S (1995) Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols. Biochemistry 34:16838\u201316851. https:\/\/doi.org\/10.1021\/bi00051a035","DOI":"10.1021\/bi00051a035"},{"key":"1_CR47","doi-asserted-by":"publisher","unstructured":"Qian Z, Horton JR, Cheng X, Lutz S (2009) Structural redesign of lipase B from Candida antarctica by circular permutation and incremental truncation. J Mol Biol 393:191\u2013201. https:\/\/doi.org\/10.1016\/j.jmb.2009.08.008","DOI":"10.1016\/j.jmb.2009.08.008"},{"key":"1_CR48","doi-asserted-by":"publisher","unstructured":"Xie Y, An J, Yang G, Wu G, Zhang Y, Cui L (2014) Enhanced enzyme kinetic stability by increasing rigidity within the active site. J Biol Chem 289(11):7994\u20138006. https:\/\/doi.org\/10.1074\/jbc.M113.536045","DOI":"10.1074\/jbc.M113.536045"},{"issue":"12","key":"1_CR49","doi-asserted-by":"publisher","first-page":"2348","DOI":"10.1194\/jlr.M063388","volume":"56","author":"B Stauch","year":"2015","unstructured":"Stauch B, Fisher SJ, Cianci M (2015) Open and closed states of Candida antarctica lipase B: protonation and the mechanism of interfacial activation. J Lipid Res 56(12):2348\u20132358. https:\/\/doi.org\/10.1194\/jlr.M063388","journal-title":"J Lipid Res"},{"key":"1_CR50","doi-asserted-by":"publisher","unstructured":"Strzelczyk P, Bujacz GD, Kie\u0142basi\u0144ski P, B\u0142aszczyk J (2016) Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica. Acta Biochim Pol 63(1):103\u2013109. https:\/\/doi.org\/10.18388\/abp.2015_1065","DOI":"10.18388\/abp.2015_1065"},{"key":"1_CR51","doi-asserted-by":"publisher","unstructured":"Brzozowski AM (1992) Structure and molecular model refinement of Rhizomucor miehei triacylglyceride lipase: a case study of the use of simulated annealing in partial model refinement. Acta Crystallogr 48:307\u2013319. https:\/\/doi.org\/10.1107\/S0108768191014647","DOI":"10.1107\/S0108768191014647"},{"key":"1_CR52","doi-asserted-by":"publisher","unstructured":"Derewenda U, Brzozowski AM, Lawson DM, Derewenda ZS (1992) Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase. Biochemistry 31:1532\u20131541. https:\/\/doi.org\/10.1021\/bi00120a034","DOI":"10.1021\/bi00120a034"},{"key":"1_CR53","doi-asserted-by":"publisher","unstructured":"Brzozowski AM, Derewenda U, Derewenda ZS, Dodson GG, Lawson DM, Turkenburg JP (1991) A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature 351:491\u2013494. https:\/\/doi.org\/10.1038\/351491a0","DOI":"10.1038\/351491a0"},{"key":"1_CR54","doi-asserted-by":"publisher","unstructured":"Derewenda U, Swenson L, Wei Y, Green R, Kobos PM, Joerger R (1994) Conformational lability of lipases observed in the absence of an oil-water interface: crystallographic studies of enzymes from the fungi Humicola lanuginosa and Rhizopus delemar. J Lipid Res 35(3):524\u2013534. https:\/\/doi.org\/10.1016\/S0022-2275(20)41203-9","DOI":"10.1016\/S0022-2275(20)41203-9"},{"key":"1_CR55","doi-asserted-by":"publisher","unstructured":"Thoms S, Hofhuis J, Th\u00f6ing C, G\u00e4rtner J, Niemann HH (2011) The unusual extended C-terminal helix of the peroxisomal \u03b1\/\u03b2-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization. J Struct Biol 175(3):362\u2013371. https:\/\/doi.org\/10.1016\/j.jsb.2011.06.008","DOI":"10.1016\/j.jsb.2011.06.008"},{"issue":"43","key":"1_CR56","doi-asserted-by":"publisher","first-page":"31477","DOI":"10.1074\/jbc.M704942200","volume":"282","author":"R Meier","year":"2007","unstructured":"Meier R, Drepper T, Svensson V, Jaeger K-E, Baumann U (2007) A calcium-gated lid and a large \u03b2-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens. J Biol Chem 282(43):31477\u201331483. https:\/\/doi.org\/10.1074\/jbc.M704942200","journal-title":"J Biol Chem"},{"key":"1_CR57","doi-asserted-by":"publisher","first-page":"87","DOI":"10.1016\/j.procbio.2021.02.009","volume":"103","author":"A Eddehech","year":"2021","unstructured":"Eddehech A, Rahier R, Smichi N, Arhab Y, Noiriel A, Abousalham A, Sayari A, Zarai Z (2021) Heterologous expression, kinetic characterization and molecular modeling of a new sn-1,3-regioselective triacylglycerol lipase from Serratia sp. W3. Process Biochem 103:87\u2013W97. https:\/\/doi.org\/10.1016\/j.procbio.2021.02.009","journal-title":"Process Biochem"},{"key":"1_CR58","doi-asserted-by":"publisher","unstructured":"Brzozowski AM, Savage H, Verma CS, Turkenburg JP, Lawson DM, Svendsen A (2000) Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase. Biochemistry 39:15071\u201315082. https:\/\/doi.org\/10.1021\/bi0013905","DOI":"10.1021\/bi0013905"},{"key":"1_CR59","doi-asserted-by":"publisher","unstructured":"Yapoudjian SS, Ivanova MG, Brzozowski AM, Patkar SA, Vind J, Svendsen A (2002) Binding of Thermomyces (Humicola) lanuginosa lipase to the mixed micelles of cis-parinaric acid\/NaTDC: fluorescence resonance energy transfer and crystallographic study. Eur J Biochem 269:1613\u20131621. https:\/\/doi.org\/10.1046\/j.1432-1327.2002.02786.x","DOI":"10.1046\/j.1432-1327.2002.02786.x"},{"key":"1_CR60","doi-asserted-by":"publisher","unstructured":"Kumar M, Mukherjee J, Sinha M, Kaur P, Sharma S, Gupta MN (2015) Enhancement of stability of a lipase by subjecting to three phase partitioning (TPP): structures of native and TPP-treated lipase from Thermomyces lanuginosa. Sustain Chem Processes 3:14. https:\/\/doi.org\/10.1186\/s40508-015-0042-5","DOI":"10.1186\/s40508-015-0042-5"},{"key":"1_CR61","doi-asserted-by":"publisher","unstructured":"Skjold-J\u00f8rgensen J, Vind J, Moroz OV, Blagova E, Bhatia VK, Svendsen A (2017) Controlled lid-opening in Thermomyces lanuginosus lipase\u2014an engineered switch for studying lipase function. Biochim Biophys Acta 1865(1):20\u201327. https:\/\/doi.org\/10.1016\/j.bbapap.2016.09.016","DOI":"10.1016\/j.bbapap.2016.09.016"},{"key":"1_CR62","doi-asserted-by":"publisher","unstructured":"Bordes F, Barbe S, Escalier P, Mourey L, Andr\u00e9 I, Marty A (2010) Exploring the conformational states and rearrangements of Yarrowia lipolytica lipase. Biophys J 99:2225\u20132234. https:\/\/doi.org\/10.1016\/j.bpj.2010.07.040","DOI":"10.1016\/j.bpj.2010.07.040"},{"key":"1_CR63","doi-asserted-by":"publisher","unstructured":"Lenfant N, Hotelier T, Velluet E, Bourne Y, Marchot P, Chatonnet A (2013) ESTHER, the database of the \u03b1\/\u03b2-hydrolase fold superfamily of proteins: tools to explore diversity of functions. Nucleic Acids Res 41(D1):D423\u2013D429. https:\/\/doi.org\/10.1093\/nar\/gks1154","DOI":"10.1093\/nar\/gks1154"},{"key":"1_CR64","doi-asserted-by":"publisher","unstructured":"Jaeger KE, Dijkstra BW, Reetz MT (1999) Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases. Annu Rev Microbiol 53:315\u2013351. https:\/\/doi.org\/10.1146\/annurev.micro.53.1.315","DOI":"10.1146\/annurev.micro.53.1.315"},{"issue":"1","key":"1_CR65","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1002\/cctc.201901369","volume":"12","author":"S Gihaz","year":"2020","unstructured":"Gihaz S, Bash Y, Rush I, Shahar A, Pazy Y, Fishman A (2020) Bridges to stability: engineering disulfide bonds towards enhanced lipase biodiesel synthesis. ChemCatChem 12(1):181\u2013192. https:\/\/doi.org\/10.1002\/cctc.201901369","journal-title":"ChemCatChem"},{"issue":"5-6","key":"1_CR66","doi-asserted-by":"publisher","first-page":"1673","DOI":"10.1007\/s00253-023-12396-5","volume":"107","author":"SH Hamdan","year":"2023","unstructured":"Hamdan SH, Maiangwa J, Nezhad NG, Ali MSM, Normi YM, Shariff FM, Rahman R, Leow TC (2023) Knotting terminal ends of mutant T1 lipase with disulfide bond improved structure rigidity and stability. Appl Microbiol Biotechnol 107(5-6):1673\u20131686. https:\/\/doi.org\/10.1007\/s00253-023-12396-5","journal-title":"Appl Microbiol Biotechnol"},{"key":"1_CR67","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1016\/j.enzmictec.2019.03.008","volume":"126","author":"L Li","year":"2019","unstructured":"Li L, Zhang S, Wu W, Guan W, Deng Z, Qiao H (2019) Enhancing thermostability of Yarrowia lipolytica lipase 2 through engineering multiple disulfide bonds and mitigating reduced lipase production associated with disulfide bonds. Enzyme Microb Technol 126:41\u201349. https:\/\/doi.org\/10.1016\/j.enzmictec.2019.03.008","journal-title":"Enzyme Microb Technol"},{"key":"1_CR68","doi-asserted-by":"publisher","unstructured":"Pouderoyen G, Eggert T, Jaeger KE, Dijkstra BW (2001) The crystal structure of Bacillus subtilis lipase: a minimal \u03b1\/\u03b2 hydrolase fold enzyme. J Mol Biol 309:215\u2013226. https:\/\/doi.org\/10.1006\/jmbi.2001.4659","DOI":"10.1006\/jmbi.2001.4659"},{"key":"1_CR69","doi-asserted-by":"publisher","unstructured":"Pleiss J, Fischer M, Schmid RD (1998) Anatomy of lipase binding sites: the scissile fatty acid binding site. Chem Phys Lipids 93:67\u201380. https:\/\/doi.org\/10.1016\/S0009-3084(98)00030-9","DOI":"10.1016\/S0009-3084(98)00030-9"},{"key":"1_CR70","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1007\/978-1-4939-8672-9","volume-title":"Lipases and phospholipases: methods and protocols","author":"L Casas-Godoy","year":"2018","unstructured":"Casas-Godoy L, Gasteazoro F, Duquesne S, Bordes F, Marty A, Sandoval G (2018) Lipases: an overview. In: Sandoval G (Ed.)Eds. Lipases and phospholipases: methods and protocols. Springer, New York, NY, 3\u201338 https:\/\/doi.org\/10.1007\/978-1-4939-8672-9"},{"key":"1_CR71","doi-asserted-by":"publisher","unstructured":"Anobom CD, Pinheiro AS, De-Andrade RA, Aguieiras ECG, Andrade GC, Moura MV (2014) From structure to catalysis: recent developments in the biotechnological applications of lipases. Biomed Res Int 2014:684506. https:\/\/doi.org\/10.1155\/2014\/684506","DOI":"10.1155\/2014\/684506"},{"key":"1_CR72","doi-asserted-by":"publisher","first-page":"16","DOI":"10.3389\/fbioe.2017.00016","volume":"5","author":"FI Khan","year":"2017","unstructured":"Khan FI, Lan D, Durrani R, Huan W, Zhao Z, Wang Y (2017) The lid domain in lipases: structural and functional determinant of enzymatic properties. Front Bioeng Biotechnol 5:16. https:\/\/doi.org\/10.3389\/fbioe.2017.00016","journal-title":"Front Bioeng Biotechnol"},{"key":"1_CR73","doi-asserted-by":"publisher","unstructured":"Kapoor M, Gupta MN (2012) Lipase promiscuity and its biochemical applications. Process Biochem 47(4):555\u2013569. https:\/\/doi.org\/10.1016\/j.procbio.2012.01.011","DOI":"10.1016\/j.procbio.2012.01.011"},{"key":"1_CR74","doi-asserted-by":"publisher","unstructured":"Gupta R, Kumari A, Syal P, Singh Y (2015) Molecular and functional diversity of yeast and fungal lipases: their role in biotechnology and cellular physiology. Prog Lipid Res 57:40\u201354. https:\/\/doi.org\/10.1016\/j.plipres.2014.12.001","DOI":"10.1016\/j.plipres.2014.12.001"},{"issue":"5","key":"1_CR75","doi-asserted-by":"publisher","first-page":"1035","DOI":"10.1111\/febs.15071","volume":"287","author":"TL Bauer","year":"2020","unstructured":"Bauer TL, Buchholz PCF, Pleiss J (2020) The modular structure of \u03b1\/\u03b2-hydrolases. FEBS J 287(5):1035\u20131053. https:\/\/doi.org\/10.1111\/febs.15071","journal-title":"FEBS J"},{"issue":"1","key":"1_CR76","doi-asserted-by":"publisher","first-page":"319","DOI":"10.1093\/nar\/gkg015","volume":"31","author":"M Fischer","year":"2003","unstructured":"Fischer M, Pleiss J (2003) The Lipase Engineering Database: a navigation and analysis tool for protein families. Nucleic Acids Res 31(1):319\u2013321. https:\/\/doi.org\/10.1093\/nar\/gkg015","journal-title":"Nucleic Acids Res"},{"issue":"6","key":"1_CR77","doi-asserted-by":"publisher","first-page":"1724","DOI":"10.1128\/aem.06332-11","volume":"78","author":"A Bassegoda","year":"2012","unstructured":"Bassegoda A, Pastor FI, Diaz P (2012) Rhodococcus sp. strain CR-53 LipR, the first member of a new bacterial lipase family (family X) displaying an unusual Y-type oxyanion hole, similar to the Candida antarctica lipase clan. Appl Environ Microbiol 78(6):1724\u20131732. https:\/\/doi.org\/10.1128\/aem.06332-11","journal-title":"Appl Environ Microbiol"},{"issue":"1","key":"1_CR78","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2105-7-495","volume":"7","author":"M Fischer","year":"2006","unstructured":"Fischer M, Thai QK, Grieb M, Pleiss J (2006) DWARF \u2013 a data warehouse system for analyzing protein families. BMC Bioinformatics 7(1):495. https:\/\/doi.org\/10.1186\/1471-2105-7-495","journal-title":"BMC Bioinformatics"},{"issue":"9","key":"1_CR79","doi-asserted-by":"publisher","first-page":"151","DOI":"10.1007\/s11738-019-2944-4","volume":"41","author":"L-N Ding","year":"2019","unstructured":"Ding L-N, Li M, Wang W-J, Cao J, Wang Z, Zhu K-M, Yang Y-H, Li Y-L, Tan X-L (2019) Advances in plant GDSL lipases: from sequences to functional mechanisms. Acta Physiol Plant 41(9):151. https:\/\/doi.org\/10.1007\/s11738-019-2944-4","journal-title":"Acta Physiol Plant"},{"key":"1_CR80","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1016\/j.bej.2015.12.019","volume":"109","author":"E Akil","year":"2016","unstructured":"Akil E, Carvalho T, B\u00e1rea B, Finotelli P, Lecomte J, Torres AG, Amaral P, Villeneuve P (2016) Accessing regio-and typo-selectivity of Yarrowia lipolytica lipase in its free form and immobilized onto magnetic nanoparticles. Biochem Eng J 109:101\u2013111. https:\/\/doi.org\/10.1016\/j.bej.2015.12.019","journal-title":"Biochem Eng J"},{"issue":"13","key":"1_CR81","doi-asserted-by":"publisher","first-page":"1608","DOI":"10.1016\/j.tetasy.2008.06.009","volume":"19","author":"M Cancino","year":"2008","unstructured":"Cancino M, Bauchart P, Sandoval G, Nicaud JM, Andr\u00e9 I, Dossat V, Marty A (2008) A variant of Yarrowia lipolytica lipase with improved activity and enantioselectivity for resolution of 2-bromo-arylacetic acid esters. Tetrahedron Asymmetry 19(13):1608\u20131612. https:\/\/doi.org\/10.1016\/j.tetasy.2008.06.009","journal-title":"Tetrahedron Asymmetry"},{"key":"1_CR82","doi-asserted-by":"publisher","unstructured":"Najm TA, Walsh MK, Park N (2024) Different substrate selectivity and product patterns of immobilized thermophilic lipases from Geobacillus stearothermophilus, Anoxybacillus flavithermus, and Thermomyces lanuginosus for glyceryl decanoate synthesis. ChemEngineering 8(1):12. https:\/\/doi.org\/10.3390\/chemengineering8010012","DOI":"10.3390\/chemengineering8010012"},{"issue":"3","key":"1_CR83","doi-asserted-by":"publisher","first-page":"511","DOI":"10.1007\/s43153-021-00132-3","volume":"38","author":"SMP Marcucci","year":"2021","unstructured":"Marcucci SMP, Araki CA, da Silva LS, Zanin GM, Arroyo PA (2021) Influence of the chain length of the fatty acids present in different oils and the pore diameter of the support on the catalytic activity of immobilized lipase for ethyl ester production. Braz J Chem Eng 38(3):511\u2013522. https:\/\/doi.org\/10.1007\/s43153-021-00132-3","journal-title":"Braz J Chem Eng"},{"key":"1_CR84","doi-asserted-by":"publisher","unstructured":"Rivero-Pino F, Padial-Dominguez M, Guadix EM, Morales-Medina R (2020) Novozyme 435 and Lipozyme RM IM preferably esterify polyunsaturated fatty acids at the sn-2 position. Eur J Lipid Sci Technol 122(10):e2000115. https:\/\/doi.org\/10.1002\/ejlt.202000115","DOI":"10.1002\/ejlt.202000115"},{"key":"1_CR85","doi-asserted-by":"publisher","unstructured":"Ghattas N, Abidi F, Galai S, Marzouki MN, Salah AB (2014) Monoolein production by triglycerides hydrolysis using immobilized Rhizopus oryzae lipase. Int J Biol Macromol 68:1\u20136. https:\/\/doi.org\/10.1016\/j.ijbiomac.2014.04.017","DOI":"10.1016\/j.ijbiomac.2014.04.017"},{"key":"1_CR86","doi-asserted-by":"publisher","unstructured":"Soumanou MM, P\u00e9rignon M, Villeneuve P (2013) Lipase-catalyzed interesterification reactions for human milk fat substitutes production: a review. Eur J Lipid Sci Technol 115:270\u2013285. https:\/\/doi.org\/10.1002\/ejlt.201200084","DOI":"10.1002\/ejlt.201200084"},{"key":"1_CR87","doi-asserted-by":"publisher","unstructured":"Yan Q, Duan X, Liu Y, Jiang Z, Yang S (2016) Expression and characterization of a novel 1,3-regioselective cold-adapted lipase from Rhizomucor endophyticus suitable for biodiesel synthesis. Biotechnol Biofuels 9:86. https:\/\/doi.org\/10.1186\/s13068-016-0501-6","DOI":"10.1186\/s13068-016-0501-6"},{"key":"1_CR88","doi-asserted-by":"publisher","unstructured":"\u0160inkuniene D, Adlercreutz P (2014) Effects of regioselectivity and lipid class specificity of lipases on transesterification, exemplified by biodiesel production. J Am Oil Chem Soc 91:1283\u20131290. https:\/\/doi.org\/10.1007\/s11746-014-2465-7","DOI":"10.1007\/s11746-014-2465-7"},{"key":"1_CR89","doi-asserted-by":"publisher","unstructured":"Bueso F, Moreno L, Cede\u00f1o M, Manzanarez K (2015) Lipase-catalyzed biodiesel production and quality with Jatropha curcas oil: exploring its potential for Central America. J Biol Eng 9:12. https:\/\/doi.org\/10.1186\/s13036-015-0009-9","DOI":"10.1186\/s13036-015-0009-9"},{"key":"1_CR90","doi-asserted-by":"publisher","unstructured":"Br\u00edgida AIS, Amaral PFF, Coelho MAZ, Gon\u00e7alves LRB (2014) Lipase from Yarrowia lipolytica: production, characterization and application as an industrial biocatalyst. J Mol Catal B Enzym 101:148\u2013158. https:\/\/doi.org\/10.1016\/j.molcatb.2013.11.016","DOI":"10.1016\/j.molcatb.2013.11.016"},{"key":"1_CR91","doi-asserted-by":"publisher","unstructured":"Watanabe Y, Sato S, Sera S, Sato C, Yoshinaga K, Nagai T (2014) Enzymatic analysis of positional distribution of fatty acids in solid fat by 1,3-selective transesterification with Candida antarctica lipase B. J Am Oil Chem Soc 91:1323\u20131330. https:\/\/doi.org\/10.1007\/s11746-014-2481-7","DOI":"10.1007\/s11746-014-2481-7"},{"key":"1_CR92","doi-asserted-by":"publisher","unstructured":"Horchani H, Aissa I, Ouertani S, Zarai Z, Gargouri Y, Sayari A (2012) Staphylococcal lipases: biotechnological applications. J Mol Catal B Enzym 76:125\u2013132. https:\/\/doi.org\/10.1016\/j.molcatb.2011.11.018","DOI":"10.1016\/j.molcatb.2011.11.018"},{"key":"1_CR93","doi-asserted-by":"publisher","unstructured":"Ota Y, Sawamoto T, Hasuo M (2000) Tributyrin specifically induces a lipase with a preference for the sn-2 position of triglyceride in Geotrichum sp. FO401B. Biosci Biotechnol Biochem 64:2497\u20132499. https:\/\/doi.org\/10.1271\/bbb.64.2497","DOI":"10.1271\/bbb.64.2497"},{"key":"1_CR94","doi-asserted-by":"publisher","unstructured":"Barriuso J, Vaquero ME, Prieto A, Mart\u00ednez MJ (2016) Structural traits and catalytic versatility of the lipases from the Candida rugosa-like family: a review. Biotechnol Adv 34(5):874\u2013885. https:\/\/doi.org\/10.1016\/j.biotechadv.2016.05.004","DOI":"10.1016\/j.biotechadv.2016.05.004"},{"key":"1_CR95","doi-asserted-by":"publisher","unstructured":"Sarkar P, Yamasaki S, Basak S, Bera A, Bag PK (2012) Purification and characterization of a new alkali-thermostable lipase from Staphylococcus aureus isolated from Arachis hypogaea rhizosphere. Process Biochem 47:858\u2013866. https:\/\/doi.org\/10.1016\/j.procbio.2012.02.023","DOI":"10.1016\/j.procbio.2012.02.023"},{"key":"1_CR96","doi-asserted-by":"publisher","unstructured":"Kasprzyk-Hordern B, Baker DR (2012) Enantiomeric profiling of chiral drugs in wastewater and receiving waters. Environ Sci Technol 46(3):1681\u20131691. https:\/\/doi.org\/10.1021\/es203113y","DOI":"10.1021\/es203113y"},{"key":"1_CR97","doi-asserted-by":"publisher","unstructured":"Kazlauskas R, Weissefloch A, Rappaport AT, Cuccia LA (1991) A rule to predict which enantiomer of a secondary alcohol react faster in reactions catalyzed by cholesterol esterase, lipase from Pseudomonas cepacia, and lipase from Candida rugosa. J Organomet Chem 56:2656\u20132665. https:\/\/doi.org\/10.1021\/jo00008a016","DOI":"10.1021\/jo00008a016"},{"key":"1_CR98","doi-asserted-by":"publisher","unstructured":"Weissefloch A, Kazlauskas RJ (1995) Enantiopreference of lipase from Pseudomonas cepacia toward primary alcohols. J Organomet Chem 60(21):6959\u20136969. https:\/\/doi.org\/10.1021\/jo00126a056","DOI":"10.1021\/jo00126a056"},{"key":"1_CR99","doi-asserted-by":"publisher","unstructured":"Bordes F, Cambon E, Dossat-l\u00f8tisse V, Andr\u00f8 I, Croux C, Nicaud JM (2009) Improvement of Yarrowia lipolytica lipase enantioselectivity by using mutagenesis targeted to the substrate binding site. Chembiochem 10(10):1705\u20131713. https:\/\/doi.org\/10.1002\/cbic.200900215","DOI":"10.1002\/cbic.200900215"},{"key":"1_CR100","doi-asserted-by":"publisher","unstructured":"Li J, Yue L, Li C, Pan Y, Yang L (2015) Enantioselectivity and catalysis improvements of Pseudomonas cepacia lipase with Tyr and Asp modification. Cat Sci Technol 5:2681\u20132687. https:\/\/doi.org\/10.1039\/C5CY00110B","DOI":"10.1039\/C5CY00110B"},{"key":"1_CR101","doi-asserted-by":"publisher","first-page":"5451","DOI":"10.1016\/j.csbj.2023.10.049","volume":"21","author":"HD Tjornelund","year":"2023","unstructured":"Tjornelund HD, Vind J, Brask J, Woodley JM, Peters GHJ (2023) Candida antarctica lipase B performance in organic solvent at varying water activities studied by molecular dynamics simulations. Comput Struct Biotechnol J 21:5451\u20135462. https:\/\/doi.org\/10.1016\/j.csbj.2023.10.049","journal-title":"Comput Struct Biotechnol J"},{"issue":"3","key":"1_CR102","doi-asserted-by":"publisher","first-page":"1669","DOI":"10.1021\/acs.joc.1c01136","volume":"87","author":"KN Ingenbosch","year":"2022","unstructured":"Ingenbosch KN, Vieyto-Nu\u00f1ez JC, Ruiz-Blanco YB, Mayer C, Hoffmann-Jacobsen K, Sanchez-Garcia E (2022) Effect of organic solvents on the structure and activity of a minimal lipase. J Org Chem 87(3):1669\u20131678. https:\/\/doi.org\/10.1021\/acs.joc.1c01136","journal-title":"J Org Chem"},{"issue":"10","key":"1_CR103","doi-asserted-by":"publisher","first-page":"1139","DOI":"10.1007\/s10529-022-03284-5","volume":"44","author":"P Priyanka","year":"2022","unstructured":"Priyanka P, Kinsella GK, Henehan GT, Ryan BJ (2022) Listeria monocytogenes is a solvent tolerant organism secreting a solvent stable lipase: potential biotechnological applications. Biotechnol Lett 44(10):1139\u20131147. https:\/\/doi.org\/10.1007\/s10529-022-03284-5","journal-title":"Biotechnol Lett"},{"key":"1_CR104","doi-asserted-by":"publisher","first-page":"96","DOI":"10.1016\/j.molcatb.2013.11.011","volume":"99","author":"M Li","year":"2014","unstructured":"Li M, Yang LR, Xu G, Wu JP (2014) Identification of organic solvent-tolerant lipases from organic solvent-sensitive microorganisms. J Mol Catal B Enzym 99:96\u2013101. https:\/\/doi.org\/10.1016\/j.molcatb.2013.11.011","journal-title":"J Mol Catal B Enzym"},{"issue":"2","key":"1_CR105","doi-asserted-by":"publisher","first-page":"203","DOI":"10.1007\/s10529-018-02633-7","volume":"41","author":"P Priyanka","year":"2019","unstructured":"Priyanka P, Tan YQ, Kinsella GK, Henehan GT, Ryan BJ (2019) Solvent stable microbial lipases: current understanding and biotechnological applications. Biotechnol Lett 41(2):203\u2013220. https:\/\/doi.org\/10.1007\/s10529-018-02633-7","journal-title":"Biotechnol Lett"},{"issue":"1","key":"1_CR106","doi-asserted-by":"publisher","first-page":"86","DOI":"10.1016\/j.procbio.2014.10.019","volume":"50","author":"A Salihu","year":"2015","unstructured":"Salihu A, Alam MZ (2015) Solvent tolerant lipases: a review. Process Biochem 50(1):86\u201396. https:\/\/doi.org\/10.1016\/j.procbio.2014.10.019","journal-title":"Process Biochem"},{"key":"1_CR107","unstructured":"Precedence Research (2025) Enzymes market size, share, growth, trends, report 2023 to 2032. Report code 1806. https:\/\/www.precedenceresearch.com\/enzymes-market"},{"key":"1_CR108","unstructured":"Precedence Research (2025) Industrial enzymes market (by product: carbohydrases, proteases, lipases, polymerases & nucleases, others; by source: plants, animals, microorganisms; by application: food & beverages, detergents, animal feed, biofuels, nutraceutical, wastewater, others)\u2014global industry analysis, size, share, growth, trends, regional outlook, and forecast 2021\u20132030. Report code 1382. https:\/\/www.precedenceresearch.com\/industrial-enzymes-market."},{"key":"1_CR109","unstructured":"Future Market Insights (2026) Lipase market outlook (2023 to 2033). Report no. REP-GB-5619, 342 pp. https:\/\/www.futuremarketinsights.com\/reports\/lipase-market."},{"key":"1_CR110","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/1475-2859-13-1","volume":"13","author":"Q Peng","year":"2014","unstructured":"Peng Q, Wang X, Shang M, Huang J, Guan G, Li Y (2014) Isolation of a novel alkaline-stable lipase from a metagenomic library and its specific application for milkfat flavor production. Microb Cell Fact 13:1. https:\/\/doi.org\/10.1186\/1475-2859-13-1","journal-title":"Microb Cell Fact"},{"key":"1_CR111","unstructured":"Chaurasia SP, Bhandari K, Sharma A, Dalai AK (2016) A review on lipase catalysed synthesis of DHA rich glyceride from fish oils. Int J Res Sci Innov 3(1A):9\u201319. https:\/\/rsisinternational.org\/Issue23\/09-19.pdf"},{"key":"1_CR112","doi-asserted-by":"publisher","unstructured":"Ferreira-Dias S SG, Plou F, Valero F (2013) The potential use of lipases in the production of fatty acid derivatives for the food and nutraceutical industries. Electron J Biotechnol 16(3):1\u201338. https:\/\/doi.org\/10.2225\/vol16-issue3-fulltext-5","DOI":"10.2225\/vol16-issue3-fulltext-5"},{"issue":"4","key":"1_CR113","doi-asserted-by":"publisher","first-page":"607","DOI":"10.1002\/bab.1761","volume":"66","author":"A Carpen","year":"2019","unstructured":"Carpen A, Bonomi F, Iametti S, Marengo M (2019) Effects of starch addition on the activity and specificity of food-grade lipases. Biotechnol Appl Biochem 66(4):607\u2013616. https:\/\/doi.org\/10.1002\/bab.1761","journal-title":"Biotechnol Appl Biochem"},{"issue":"2","key":"1_CR114","doi-asserted-by":"publisher","first-page":"208","DOI":"10.1007\/s42995-022-00128-z","volume":"4","author":"Q Liang","year":"2022","unstructured":"Liang Q, Yuan M, Xu L, Lio E, Zhang F, Mou H, Secundo F (2022) Application of enzymes as a feed additive in aquaculture. Mar Life Sci Technol 4(2):208\u2013221. https:\/\/doi.org\/10.1007\/s42995-022-00128-z","journal-title":"Mar Life Sci Technol"},{"key":"1_CR115","doi-asserted-by":"publisher","unstructured":"Li XL, Zhang WH, Wang YD, Dai YJ, Zhang HT, Wang Y (2014) A high-detergent-performance, cold-adapted lipase from Pseudomonas stutzeri PS59 suitable for detergent formulation. J Mol Catal B Enzym 102:16\u201324. https:\/\/doi.org\/10.1016\/j.molcatb.2014.01.006","DOI":"10.1016\/j.molcatb.2014.01.006"},{"key":"1_CR116","doi-asserted-by":"publisher","unstructured":"Lailaja VP, Chandrasekaran M (2013) Detergent compatible alkaline lipase produced by marine Bacillus smithii BTMS 11. World J Microbiol Biotechnol 29(8):1349\u20131360. https:\/\/doi.org\/10.1007\/s11274-013-1298-0","DOI":"10.1007\/s11274-013-1298-0"},{"key":"1_CR117","doi-asserted-by":"publisher","unstructured":"G\u00e9rard D, Gu\u00e9roult M, Casas-Godoy L, Condoret J-S, Andr\u00e9 I, Marty A et al (2017) Efficient resolution of profen ethyl ester racemates by engineered Yarrowia lipolytica Lip2p lipase. Tetrahedron Asymmetry 28:433\u2013441. https:\/\/doi.org\/10.1016\/j.tetasy.2017.01.014.","DOI":"10.1016\/j.tetasy.2017.01.014."},{"key":"1_CR118","doi-asserted-by":"publisher","unstructured":"Tian X, Zhang G, L\u00fc X, Zhang A, Lin J, Zheng L (2012) Resolution of N-(2-ethyl-6-methylphenyl) alanine by using microgel beads containing Pseudomonas cepacia lipase. Biocatal Biotransform 30(4):391\u2013398. https:\/\/doi.org\/10.3109\/10242422.2012.702109","DOI":"10.3109\/10242422.2012.702109"},{"key":"1_CR119","doi-asserted-by":"publisher","unstructured":"Bora L, Gohain D, Das R (2013) Recent advances in production and biotechnological applications of thermostable and alkaline bacterial lipases. J Chem Technol Biotechnol 88:1959\u20131970. https:\/\/doi.org\/10.1002\/jctb.4170","DOI":"10.1002\/jctb.4170"},{"key":"1_CR120","doi-asserted-by":"publisher","unstructured":"Khan NR, Rathod VK (2015) Enzyme catalyzed synthesis of cosmetic esters and its intensification: a review. Process Biochem 50(11):1793\u20131806. https:\/\/doi.org\/10.1016\/j.procbio.2015.07.014","DOI":"10.1016\/j.procbio.2015.07.014"},{"key":"1_CR121","doi-asserted-by":"publisher","unstructured":"Sharma S, Kanwar SS (2014) Organic solvent tolerant lipases and applications. Sci World J 2014:625258. https:\/\/doi.org\/10.1155\/2014\/625258","DOI":"10.1155\/2014\/625258"},{"key":"1_CR122","doi-asserted-by":"publisher","unstructured":"Aarthy M, Saravanan P, Gowthaman MK, Rose C, Kamini NR (2014) Enzymatic transesterification for production of biodiesel using yeast lipases: an overview. Chem Eng Res Design 92(8):1591\u20131601. https:\/\/doi.org\/10.1016\/j.cherd.2014.04.008","DOI":"10.1016\/j.cherd.2014.04.008"},{"key":"1_CR123","doi-asserted-by":"publisher","unstructured":"Norjannah B, Ong HC, Masjuki HH, Juan JC, Chong WT, Ashnani MHM (2016) Enzymatic transesterification for biodiesel production: a comprehensive review. RSC Adv 6:60034\u201360055. https:\/\/doi.org\/10.1039\/C6RA08062F","DOI":"10.1039\/C6RA08062F"},{"key":"1_CR124","doi-asserted-by":"publisher","unstructured":"Sandoval G, Casas-Godoy L, Bonet-Ragel K, Rodrigues J, Ferreira-Dias S, Valero F (2017) Enzyme-catalyzed production of biodiesel as alternative to chemical-catalyzed processes: advantages and constraints. Curr Biochem Eng 4(2):109\u2013141. https:\/\/doi.org\/10.2174\/2212711904666170615123640","DOI":"10.2174\/2212711904666170615123640"},{"key":"1_CR125","doi-asserted-by":"publisher","unstructured":"Tao Y, Chen B, Liu L, Tan T (2012) Synthesis of trimethylolpropane esters with immobilized lipase from Candida sp. 99\u2013125. J Mol Catal B Enzym 74(3\u20134):151\u2013155. https:\/\/doi.org\/10.1016\/j.molcatb.2011.07.017","DOI":"10.1016\/j.molcatb.2011.07.017"},{"key":"1_CR126","doi-asserted-by":"publisher","unstructured":"Matsumoto KI, Taguchi S (2013) Enzyme and metabolic engineering for the production of novel biopolymers: crossover of biological and chemical processes. Curr Opin Biotechnol 24(6):1054\u20131060. https:\/\/doi.org\/10.1016\/j.copbio.2013.02.021","DOI":"10.1016\/j.copbio.2013.02.021"},{"key":"1_CR127","doi-asserted-by":"publisher","unstructured":"Hwang HT, Qi F, Yuan C, Zhao X, Ramkrishna D, Liu D (2014) Lipase-catalyzed process for biodiesel production: protein engineering and lipase production. Biotechnol Bioeng 111(4):639\u2013653. https:\/\/doi.org\/10.1002\/bit.25162","DOI":"10.1002\/bit.25162"},{"key":"1_CR128","doi-asserted-by":"publisher","unstructured":"Singh AK, Mukhopadhyay M (2012) Overview of fungal lipase: a review. Appl Biochem Biotechnol 166:486\u2013520. https:\/\/doi.org\/10.1007\/s12010-011-9444-3","DOI":"10.1007\/s12010-011-9444-3"},{"issue":"4","key":"1_CR129","doi-asserted-by":"publisher","first-page":"1562","DOI":"10.1016\/j.foodchem.2011.02.018","volume":"127","author":"I Kurtovic","year":"2011","unstructured":"Kurtovic I, Marshall SN, Miller MR, Zhao X (2011) Flavour development in dairy cream using fish digestive lipases from Chinook salmon (Oncorhynchus tshawytscha) and New Zealand hoki (Macruronus novaezealandiae). Food Chem 127(4):1562\u20131568. https:\/\/doi.org\/10.1016\/j.foodchem.2011.02.018","journal-title":"Food Chem"},{"key":"1_CR130","doi-asserted-by":"publisher","unstructured":"Chen X, Wang J, Stevenson RJ, Ang X, Peng Y, Quek SY (2021) Lipase-catalyzed modification of milk fat: a promising way to alter flavor notes of goat milk products. LWT 145:111286. https:\/\/doi.org\/10.1016\/j.lwt.2021.111286","DOI":"10.1016\/j.lwt.2021.111286"},{"issue":"10","key":"1_CR131","doi-asserted-by":"publisher","first-page":"1299","DOI":"10.5650\/jos.ess18078","volume":"67","author":"P Kosiyanant","year":"2018","unstructured":"Kosiyanant P, Pande G, Tungjaroenchai W, Akoh CC (2018) Lipase - catalyzed modification of rice bran oil solid fat fraction. J Oleo Sci 67(10):1299\u20131306. https:\/\/doi.org\/10.5650\/jos.ess18078","journal-title":"J Oleo Sci"},{"issue":"1","key":"1_CR132","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s11746-007-1155-0","volume":"85","author":"JH Lee","year":"2008","unstructured":"Lee JH, Akoh CC, Lee KT (2008) Physical properties of trans-free bakery shortening produced by lipase-catalyzed interesterification.  J Am Oil Chem Soc 85(1):1\u201311. https:\/\/doi.org\/10.1007\/s11746-007-1155-0","journal-title":"J Am Oil Chem Soc"},{"issue":"8","key":"1_CR133","doi-asserted-by":"publisher","first-page":"669","DOI":"10.1007\/s10295-006-0100-9","volume":"33","author":"N Saisubramanian","year":"2006","unstructured":"Saisubramanian N, Edwinoliver NG, Nandakumar N, Kamini NR, Puvanakrishnan R (2006) Efficacy of lipase from Aspergillus niger as an additive in detergent formulations: a statistical approach. J Ind Microbiol Biotechnol 33(8):669\u2013676. https:\/\/doi.org\/10.1007\/s10295-006-0100-9","journal-title":"J Ind Microbiol Biotechnol"},{"key":"1_CR134","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1016\/j.ijbiomac.2021.03.111","volume":"181","author":"D Abol-Fotouh","year":"2021","unstructured":"Abol-Fotouh D, AlHagar OEA, Hassan MA (2021) Optimization, purification, and biochemical characterization of thermoalkaliphilic lipase from a novel Geobacillus stearothermophilus FMR12 for detergent formulations. Int J Biiol Macromol 181:125\u2013135. https:\/\/doi.org\/10.1016\/j.ijbiomac.2021.03.111","journal-title":"Int J Biiol Macromol"},{"key":"1_CR135","doi-asserted-by":"publisher","unstructured":"Gurkok S, Ozdal M (2021) Purification and characterization of a novel extracellular, alkaline, thermoactive, and detergent-compatible lipase from Aeromonas caviae LipT51 for application in detergent industry. Protein Expr Purif 180:105819. https:\/\/doi.org\/10.1016\/j.pep.2021.105819","DOI":"10.1016\/j.pep.2021.105819"},{"issue":"6","key":"1_CR136","doi-asserted-by":"publisher","first-page":"442","DOI":"10.1515\/tsd-2021-2378","volume":"58","author":"A Mehta","year":"2021","unstructured":"Mehta A, Gupta A, Bhardwaj KK, Gupta R (2021) A purified alkaline and detergent-tolerant lipase from Aspergillus fumigatus with potential application in removal of mustard oil stains from cotton fabric. Tenside Surf Det 58(6):442\u2013451. https:\/\/doi.org\/10.1515\/tsd-2021-2378","journal-title":"Tenside Surf Det"},{"issue":"20","key":"1_CR137","doi-asserted-by":"publisher","first-page":"4085","DOI":"10.1016\/s0040-4020(02)00258-2","volume":"58","author":"SM Swaleh","year":"2002","unstructured":"Swaleh SM, Hungerhoff B, Sonnenschein H, Theil F (2002) Separation of enantiomers by lipase-catalyzed fluorous-phase delabeling. Tetrahedron 58(20):4085\u20134089. https:\/\/doi.org\/10.1016\/s0040-4020(02)00258-2","journal-title":"Tetrahedron"},{"key":"1_CR138","doi-asserted-by":"publisher","unstructured":"Horino S, Nishio T, Kawanishi S, Oki S, Nishihara K, Ikawa T, Kanomata K, Wagner K, Gr\u00f6ger H, Akai S (2022) Enantiodivergent chemoenzymatic dynamic kinetic resolution: conversion of racemic propargyl alcohols into both enantiomers. Chem-A Eur J 28(60):e202202437. https:\/\/doi.org\/10.1002\/chem.202202437","DOI":"10.1002\/chem.202202437"},{"issue":"8","key":"1_CR139","doi-asserted-by":"publisher","first-page":"2352","DOI":"10.1007\/s10562-022-04157-2","volume":"153","author":"BH Jiang","year":"2023","unstructured":"Jiang BH, Xie R, Tang KW (2023) Resolution of (R, S)-4-BrMA catalyzed by Pseudomonas cepacia lipase in an organic phase. Catal Lett 153(8):2352\u20132358. https:\/\/doi.org\/10.1007\/s10562-022-04157-2","journal-title":"Catal Lett"},{"key":"1_CR140","doi-asserted-by":"publisher","unstructured":"Estrada-Valenzuela D, Ramos-Sanchez VH, Zaragoza-Galan G, Espinoza-Hicks JC, Bugarin A, Chavez-Flores D (2021) Lipase assisted (S)-ketoprofen resolution from commercially available racemic mixture. Pharmaceuticals 14(10):996. https:\/\/doi.org\/10.3390\/ph14100996","DOI":"10.3390\/ph14100996"},{"key":"1_CR141","doi-asserted-by":"publisher","unstructured":"Cipolatti EP, Rios NS, Sousa JS, Robert JD, da Silva AAT, Pinto MCC, Simas ABC, Vilarrasa-Garcia E, Fernandez-Lafuente R, Goncalves LRB, Freire DMG, Manoel EA (2021) Synthesis of lipase\/silica biocatalysts through the immobilization of CALB on porous SBA-15 and their application on the resolution of pharmaceutical derivatives and on nutraceutical enrichment of natural oil. Mol Catal 505:111529. https:\/\/doi.org\/10.1016\/j.mcat.2021.111529","DOI":"10.1016\/j.mcat.2021.111529"},{"issue":"2","key":"1_CR142","doi-asserted-by":"publisher","first-page":"239","DOI":"10.2298\/hemind120522079s","volume":"67","author":"MM Stojanovic","year":"2013","unstructured":"Stojanovic MM, Carevic MB, Mihailovic MD, Knezevic-Jugovic ZD, Petrovic SD, Bezbradica DI (2013) Enzymatic synthesis and application of fatty acid ascorbyl esters. Hem Ind 67(2):239\u2013247. https:\/\/doi.org\/10.2298\/hemind120522079s","journal-title":"Hem Ind"},{"issue":"4","key":"1_CR143","first-page":"3508","volume":"16","author":"MO Al-limoun","year":"2019","unstructured":"Al-limoun MO (2019) Potential bioremediation of waste corn oil by extracellular lipase enzyme from Monascus purpureus W7. Biosci Res 16(4):3508\u20133522","journal-title":"Biosci Res"},{"issue":"13","key":"1_CR144","doi-asserted-by":"publisher","first-page":"35517","DOI":"10.1007\/s11356-022-24669-z","volume":"30","author":"JDD Dickel","year":"2023","unstructured":"Dickel JDD, Carvalho JK, Silveira MAD, dos Santos PM, Rodrigues MLF, Fagundes-Klen MR, Rosa CA, Johann S, Buzanello CV, de Lucca RAD, Santos ARD, da Rosa MF (2023) Aspergillus sclerotiorum lipolytic activity and its application in bioremediation of high-fat dairy wastewater environments. Environ Sci Pollut Res 30(13):35517\u201335527. https:\/\/doi.org\/10.1007\/s11356-022-24669-z","journal-title":"Environ Sci Pollut Res"},{"issue":"4","key":"1_CR145","doi-asserted-by":"publisher","first-page":"1984","DOI":"10.1039\/d0nj05175f","volume":"45","author":"C Isik","year":"2021","unstructured":"Isik C, Sara\u00e7 N, Teke M, Ugur A (2021) A new bioremediation method for removal of wastewater containing oils with high oleic acid composition: Acinetobacter haemolyticus lipase immobilized on eggshell membrane with improved stabilities. New J Chem 45(4):1984\u20131992. https:\/\/doi.org\/10.1039\/d0nj05175f","journal-title":"New J Chem"},{"key":"1_CR146","doi-asserted-by":"publisher","unstructured":"Guti\u00e9rrez-Navarro E, Daniel Padilla-de la Rosa J, Mac\u00edas A, Sol\u00eds J, Sandoval G (2024) Enzymatically acylated naringin with gut modulation potential. Electron J Biotechnol https:\/\/doi.org\/10.1016\/j.ejbt.2023.12.003","DOI":"10.1016\/j.ejbt.2023.12.003"},{"issue":"20","key":"1_CR147","doi-asserted-by":"publisher","first-page":"10886","DOI":"10.1021\/jf102871g","volume":"58","author":"HJ You","year":"2010","unstructured":"You HJ, Ahn HJ, Ji GE (2010) Transformation of Rutin to antiproliferative quercetin-3-glucoside by Aspergillus niger. J Agric Food Chem 58(20):10886\u201310892. https:\/\/doi.org\/10.1021\/jf102871g","journal-title":"J Agric Food Chem"},{"issue":"2","key":"1_CR148","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1080\/10242422.2021.1952192","volume":"40","author":"AR Campos-Valdez","year":"2022","unstructured":"Campos-Valdez AR, Casas-Godoy L, Sandoval G, Hern\u00e1ndez L, Sassaki GL, Alencar de Menezes LR, Campos-Ter\u00e1n J, Reyes-Duarte D, Arrizon J (2022) Regioselective synthesis of 6\u2033-O-lauroyl-1-kestose and 6\u2033-O-lauroylnystose by sequential enzymatic reactions of transfructosylation and acylation. Biocatal Biotransform 40(2):133\u2013143. https:\/\/doi.org\/10.1080\/10242422.2021.1952192","journal-title":"Biocatal Biotransform"},{"issue":"3","key":"1_CR149","doi-asserted-by":"publisher","first-page":"1041","DOI":"10.1007\/s11756-024-01610-y","volume":"79","author":"H Kattatheyil","year":"2024","unstructured":"Kattatheyil H, Sajeela V, Kabeer SS, Ezhuthanikkunnel AP, Padinchati KK, Ammanamveetil MH (2024) Screening, optimization, and molecular characterization of cold-active lipase producing Bacillus cereus I13 from Arctic sediments. Biologia 79(3):1041\u20131055. https:\/\/doi.org\/10.1007\/s11756-024-01610-y","journal-title":"Biologia"},{"issue":"11","key":"1_CR150","doi-asserted-by":"publisher","first-page":"96","DOI":"10.25303\/1811rjbt0960105","volume":"18","author":"M Kaur","year":"2023","unstructured":"Kaur M, Sharma D, Gupta R (2023) Isolation of lipase producing thermotolerant Bacillus subtilis TTP-06 from hot spring of Himachal Pradesh. Res J Biotechnol 18(11):96\u2013105. https:\/\/doi.org\/10.25303\/1811rjbt0960105","journal-title":"Res J Biotechnol"},{"issue":"6","key":"1_CR151","doi-asserted-by":"publisher","first-page":"3240","DOI":"10.26538\/tjnpr\/v7i6.27","volume":"7","author":"AO Ogunniran","year":"2023","unstructured":"Ogunniran AO, Odeleye BO, Femi-Ola TO (2023) Optimization of culture conditions for lipase production by Pseudomonas aeruginosa ECS3. Trop J Nat Prod Res 7(6):3240\u20133245. https:\/\/doi.org\/10.26538\/tjnpr\/v7i6.27","journal-title":"Trop J Nat Prod Res"},{"issue":"1","key":"1_CR152","doi-asserted-by":"publisher","first-page":"84","DOI":"10.4014\/jmb.1107.07060","volume":"22","author":"W Xie","year":"2012","unstructured":"Xie W, Khosasih V, Suwanto A, Kim HK (2012) Characterization of lipases from Staphylococcus aureus and Staphylococcus epidermidis isolated from human facial sebaceous skin. J Microbiol Biotechnol 22(1):84\u201391. https:\/\/doi.org\/10.4014\/jmb.1107.07060","journal-title":"J Microbiol Biotechnol"},{"issue":"3","key":"1_CR153","doi-asserted-by":"publisher","first-page":"327","DOI":"10.1007\/s00253-005-0065-z","volume":"70","author":"Z Jiang","year":"2006","unstructured":"Jiang Z, Wang H, Ma Y, Wei D (2006) Characterization of two novel lipase genes isolated directly from environmental sample. Appl Microbiol Biotechnol 70(3):327\u2013332. https:\/\/doi.org\/10.1007\/s00253-005-0065-z","journal-title":"Appl Microbiol Biotechnol"},{"issue":"9","key":"1_CR154","doi-asserted-by":"publisher","first-page":"1017","DOI":"10.1007\/s11745-000-0613-z","volume":"35","author":"X Galan","year":"2000","unstructured":"Galan X, Robert MQ, Llobera M, Ramirez I (2000) Secretion of hepatic lipase by perfused liver and isolated hepatocytes. Lipids 35(9):1017\u20131026. https:\/\/doi.org\/10.1007\/s11745-000-0613-z","journal-title":"Lipids"},{"issue":"1","key":"1_CR155","doi-asserted-by":"publisher","first-page":"71","DOI":"10.48022\/mbl.2109.09006","volume":"50","author":"SWM Hassan","year":"2022","unstructured":"Hassan SWM, Abd El Latif HH, Beltagy EA (2022) Purification, characterization and application of a cold active lipase from marine Bacillus cereus HSS. Microbiol Biotechnol Lett 50(1):71\u201380. https:\/\/doi.org\/10.48022\/mbl.2109.09006","journal-title":"Microbiol Biotechnol Lett"},{"issue":"3","key":"1_CR156","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1016\/j.bej.2009.05.018","volume":"46","author":"P Ferrer","year":"2009","unstructured":"Ferrer P, Alarc\u00f3n M, Ram\u00f3n R, Dolors Benaiges M, Valero F (2009) Recombinant Candida rugosa LIP2 expression in Pichia pastoris under the control of the AOX1 promoter. Biochem Eng J 46(3):271\u2013277. https:\/\/doi.org\/10.1016\/j.bej.2009.05.018","journal-title":"Biochem Eng J"},{"key":"1_CR157","doi-asserted-by":"publisher","unstructured":"Theron CW, Vandermies M, Telek S, Steels S, Fickers P (2020) Comprehensive comparison of Yarrowia lipolytica and Pichia pastoris for production of Candida antarctica lipase B. Sci Rep 10(1). https:\/\/doi.org\/10.1038\/s41598-020-58683-3","DOI":"10.1038\/s41598-020-58683-3"},{"issue":"3","key":"1_CR158","doi-asserted-by":"publisher","first-page":"344","DOI":"10.1007\/s11130-015-0501-x","volume":"70","author":"D Sosnowska","year":"2015","unstructured":"Sosnowska D, Pods\u0119dek A, Redzynia M, \u017by\u017celewicz D (2015) Effects of fruit extracts on pancreatic lipase activity in lipid emulsions. Plant Foods Hum Nutr 70(3):344\u2013350. https:\/\/doi.org\/10.1007\/s11130-015-0501-x","journal-title":"Plant Foods Hum Nutr"},{"issue":"5","key":"1_CR159","doi-asserted-by":"publisher","first-page":"3973","DOI":"10.1007\/s00289-023-05009-8","volume":"81","author":"S Sharma","year":"2024","unstructured":"Sharma S, Sahney R, Dahiya P (2024) Preparation and characterization of stable biopolymer-based nanogel for studying its application in immobilization of Candida rugosa lipase. Polym Bull 81(5):3973\u20133994. https:\/\/doi.org\/10.1007\/s00289-023-05009-8","journal-title":"Polym Bull"},{"issue":"8","key":"1_CR160","doi-asserted-by":"publisher","first-page":"1151","DOI":"10.1007\/s11746-013-2256-6","volume":"90","author":"M P\u00e9rignon","year":"2013","unstructured":"P\u00e9rignon M, Lecomte J, Pina M, Renault A, Simonneau-Deve C, Villeneuve P (2013) Activity of immobilized Thermomyces lanuginosus and Candida antarctica B lipases in interesterification reactions: effect of the aqueous microenvironment.. J Am Oil Chem Soc 90(8):1151\u20131156. https:\/\/doi.org\/10.1007\/s11746-013-2256-6","journal-title":"J Am Oil Chem Soc"},{"issue":"1-4","key":"1_CR161","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1016\/S1381-1177(96)00052-5","volume":"3","author":"B Al-Duri","year":"1997","unstructured":"Al-Duri B, Yong YP (1997) Characterisation of the equilibrium behaviour of lipase PS (from Pseudomonas) and lipolase 100L (from Humicola) onto Accurel EP100. J Mol Catal B Enzym 3(1-4):177\u2013188. https:\/\/doi.org\/10.1016\/S1381-1177(96)00052-5","journal-title":"J Mol Catal B Enzym"}],"container-title":["Methods in Molecular Biology","Lipases and Phospholipases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/978-1-0716-5472-9_1","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T15:59:42Z","timestamp":1790179182000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/978-1-0716-5472-9_1"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,24]]},"ISBN":["9781071654712","9781071654729"],"references-count":161,"URL":"https:\/\/doi.org\/10.1007\/978-1-0716-5472-9_1","relation":{},"ISSN":["1064-3745","1940-6029"],"issn-type":[{"value":"1064-3745","type":"print"},{"value":"1940-6029","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,24]]},"assertion":[{"value":"24 September 2026","order":1,"name":"first_online","label":"First Online","group":{"name":"ChapterHistory","label":"Chapter History"}},{"value":"The authors have no conflicts of interest to declare that are relevant to the content of this chapter.","order":1,"name":"Ethics","label":"Conflict of Interest","group":{"name":"EthicsHeading","label":"Ethics"}}]}}