{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,16]],"date-time":"2026-01-16T05:21:14Z","timestamp":1768540874635,"version":"3.49.0"},"reference-count":31,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2022,1,29]],"date-time":"2022-01-29T00:00:00Z","timestamp":1643414400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2022,1,29]],"date-time":"2022-01-29T00:00:00Z","timestamp":1643414400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"funder":[{"DOI":"10.13039\/501100004883","name":"shahrekord university","doi-asserted-by":"publisher","award":["shahrekord university"],"award-info":[{"award-number":["shahrekord university"]}],"id":[{"id":"10.13039\/501100004883","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Protein J"],"published-print":{"date-parts":[[2022,2]]},"DOI":"10.1007\/s10930-021-10033-6","type":"journal-article","created":{"date-parts":[[2022,1,29]],"date-time":"2022-01-29T00:02:43Z","timestamp":1643414563000},"page":"157-165","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Comparison of Periplasmic and Cytoplasmic Expression of Bovine Enterokinase Light Chain in E. coli"],"prefix":"10.1007","volume":"41","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5699-3994","authenticated-orcid":false,"given":"Hoda","family":"Ayat","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1494-0901","authenticated-orcid":false,"given":"Omid","family":"Darvishi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7046-1812","authenticated-orcid":false,"given":"Elham","family":"Moazeni","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9934-0640","authenticated-orcid":false,"given":"Asiye","family":"Momeni Bidezard","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2022,1,29]]},"reference":[{"key":"10033_CR1","first-page":"187","volume":"81","author":"EN Kosobokova","year":"2016","unstructured":"Kosobokova EN, Skrypnik KA, Kosorukov VS (2016) Overview of fusion tags for recombinant proteins. Biochemistry 81:187\u2013200","journal-title":"Biochemistry"},{"key":"10033_CR2","doi-asserted-by":"publisher","first-page":"620","DOI":"10.1002\/biot.201100155","volume":"7","author":"CL Young","year":"2012","unstructured":"Young CL, Britton ZT, Robinson AS (2012) Recombinant protein expression and purification: a comprehensive review of affinity tags and microbial applications. Biotechnol J 7:620\u2013634","journal-title":"Biotechnol J"},{"key":"10033_CR3","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.pep.2005.12.002","volume":"48","author":"J Arnau","year":"2006","unstructured":"Arnau J, Lauritzen C, Petersen GE, Pedersen J (2006) Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. Protein Exp Purif 48:1\u201313","journal-title":"Protein Exp Purif"},{"key":"10033_CR4","doi-asserted-by":"publisher","first-page":"283","DOI":"10.1016\/j.pep.2011.08.005","volume":"80","author":"DS Waugh","year":"2011","unstructured":"Waugh DS (2011) An overview of enzymatic reagents for the removal of affinity tags. Pro Expr Purif 80:283\u2013293. https:\/\/doi.org\/10.1016\/j.pep.2011.08.005","journal-title":"Pro Expr Purif"},{"key":"10033_CR5","first-page":"242","volume":"1","author":"XL Zheng","year":"2009","unstructured":"Zheng XL, Kitamoto Y, Sadler JE (2009) Enteropeptidase, a type II transmembrane serine protease. Front Biosci 1:242\u2013249","journal-title":"Front Biosci"},{"key":"10033_CR6","first-page":"655","volume":"34","author":"E Eggermont","year":"1971","unstructured":"Eggermont E, Molla AM, Tytgat G, Rutgeerts L (1971) Distribution of enterokinase activity in the human intestine. Acta Gastroent Belg 34:655\u2013662","journal-title":"Acta Gastroent Belg"},{"key":"10033_CR7","first-page":"113","volume":"71","author":"ME Gasparian","year":"2006","unstructured":"Gasparian ME, Ostapchenko VG, Dolgikh DA, Kirpichnikov MP (2006) Biochemical characterization of human enteropeptidase light chain. Biochemistry 71:113\u2013119","journal-title":"Biochemistry"},{"key":"10033_CR8","doi-asserted-by":"publisher","first-page":"226","DOI":"10.1016\/S0014-5793(98)01656-1","volume":"442","author":"AG Mikhailova","year":"1999","unstructured":"Mikhailova AG, Rumsh LD (1999) Autolysis of bovine enteropeptidase heavy chain: evidence of fragment 118-465 involvement in trypsinogen activation. FEBS Lett 442:226\u2013230","journal-title":"FEBS Lett"},{"key":"10033_CR9","first-page":"216","volume":"2","author":"L Niu","year":"2015","unstructured":"Niu L, Li J, Ji X, Yang B (2015) Efficient expression and purification of recombinant human enteropeptidase light chain in Escherichia coli. Braz Arch Biotechnol 2:216\u2013221","journal-title":"Braz Arch Biotechnol"},{"issue":"1","key":"10033_CR10","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1016\/S1046-5928(03)00159-1","volume":"31","author":"ME Gasparian","year":"2003","unstructured":"Gasparian ME, Ostapchenko VG, Schulga AA, Dolgikh DA, Kirpichnikov MP (2003) Expression, purification, and characterization of human enteropeptidase catalytic subunit in Escherichia coli. Prot Exp Purif 31(1):133\u2013139","journal-title":"Prot Exp Purif"},{"key":"10033_CR11","doi-asserted-by":"publisher","first-page":"982","DOI":"10.1038\/nbt0995-982","volume":"13","author":"LA Collins-Racie","year":"1995","unstructured":"Collins-Racie LA, McColgan JM, Grant KL (1995) Production of recombinant bovine enterokinase catalytic subunit in Escherichia coli using the novel secretory fusion partner DsbA. J Biotechnol 13:982\u2013987. https:\/\/doi.org\/10.1038\/nbt0995-982","journal-title":"J Biotechnol"},{"key":"10033_CR12","first-page":"1","volume":"5","author":"GL Rosano","year":"2014","unstructured":"Rosano GL, Ceccarelli EA (2014) Recombinant protein expression in Escherichia coli: advances and challenges. Front Microbiol 5:1\u201317","journal-title":"Front Microbiol"},{"issue":"2","key":"10033_CR13","first-page":"169","volume":"34","author":"L Rezaei","year":"2021","unstructured":"Rezaei L, Ayat H, Ahadi AM (2021) Design and construction of pET32b(+) Rh expression vector based on pET system to facilitate purification. J Cell Mol Res 34(2):169\u2013181","journal-title":"J Cell Mol Res"},{"issue":"63","key":"10033_CR14","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3389\/fmicb.2014.00063","volume":"5","author":"S Costa","year":"2014","unstructured":"Costa S, Almeida A, Castro A, Domingues L (2014) Fusion tags for protein solubility, purification, and immunogenicity in Escherichia coli: the novel Fh8 system. Front Microbiol 5(63):1\u201320. https:\/\/doi.org\/10.3389\/fmicb.2014.00063","journal-title":"Front Microbiol"},{"issue":"26","key":"10033_CR15","first-page":"1","volume":"8","author":"A Marco","year":"2009","unstructured":"Marco A (2009). Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli, Microbial Cell Factories, 8(26): 1\u201318.","journal-title":"Microbial Cell Factories"},{"key":"10033_CR16","doi-asserted-by":"publisher","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","volume":"72","author":"MM Bradford","year":"1976","unstructured":"Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248\u2013524","journal-title":"Anal Biochem"},{"key":"10033_CR17","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1016\/j.pep.2007.07.006","volume":"56","author":"H Tan","year":"2007","unstructured":"Tan H, Wang J, Zhao Z (2007) Purification and refolding optimization of recombinant bovine enterokinase light chain overexpressed in Escherichia coli. Prot Exp Purif 56:40\u201347","journal-title":"Prot Exp Purif"},{"issue":"3","key":"10033_CR18","doi-asserted-by":"publisher","first-page":"261","DOI":"10.1093\/protein\/gzq104","volume":"24","author":"P Simeonov","year":"2011","unstructured":"Simeonov P, Berger-Hoffmann R, Hoffmann R, Stra\u00a8ter N, Zuchner T (2011) Surface supercharged human enteropeptidase light chain shows improved solubility and refolding yield. Protein Eng Des Sel 24(3):261\u2013268","journal-title":"Protein Eng Des Sel"},{"issue":"7","key":"10033_CR19","doi-asserted-by":"publisher","first-page":"513","DOI":"10.1093\/abbs\/36.7.513","volume":"36","author":"L Fang","year":"2004","unstructured":"Fang L, Sun Q, Hua Z (2004) Expression of recombinant Chinese bovine enterokinase catalytic subunit in P. pastoris and its purification and characterization. Acta Biochim Biophys Sinica 36(7):513\u2013517. https:\/\/doi.org\/10.1093\/abbs\/36.7.513","journal-title":"Acta Biochim Biophys Sinica"},{"key":"10033_CR20","doi-asserted-by":"publisher","first-page":"717","DOI":"10.1016\/j.procbio.2004.01.055","volume":"40","author":"HJ Kim","year":"2005","unstructured":"Kim HJ, Kim YH, Roh YH, Seong BL, Shin CS (2005) Optimization of enterokinase fermentation using a recombinant Saccharomyces cerevisiae. Process Biochem 40:717\u2013722","journal-title":"Process Biochem"},{"key":"10033_CR21","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1016\/S0168-1656(99)00191-1","volume":"76","author":"M Svetina","year":"2000","unstructured":"Svetina M, Krasevec N, Gaberc-Porekar V, Komel R (2000) Expression of catalytic subunit of bovine enterokinase in the filamentous fungus Aspergillus niger. J Biotechnol 76:245\u2013251","journal-title":"J Biotechnol"},{"issue":"1","key":"10033_CR22","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1016\/j.jbiotec.2011.08.017","volume":"156","author":"S Pepeliaev","year":"2011","unstructured":"Pepeliaev S, Krahulec J, Cern\u00fd Z, J\u00edlkov\u00e1 J, Tlust\u00e1 M, Dost\u00e1lov\u00e1 J (2011) High level expression of human enteropeptidase light chain in Pichia pastoris. J Biotechnol 156(1):67\u201375. https:\/\/doi.org\/10.1016\/j.jbiotec.2011.08.017","journal-title":"J Biotechnol"},{"key":"10033_CR23","doi-asserted-by":"publisher","first-page":"1927","DOI":"10.1007\/s00253-016-7960-3P10","volume":"101","author":"K Melicherov\u00e1","year":"2017","unstructured":"Melicherov\u00e1 K, Krahulec J, \u0160afr\u00e1nek M et al (2017) Optimization of the fermentation and downstream processes for human enterokinase production in Pichia pastoris. Appl Microbiol Biotechnol 101:1927\u20131934. https:\/\/doi.org\/10.1007\/s00253-016-7960-3P10","journal-title":"Appl Microbiol Biotechnol"},{"key":"10033_CR24","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3389\/fbioe.2019.00420","volume":"7","author":"N Tripathi","year":"2019","unstructured":"Tripathi N, Shrivastava A (2019) Recent developments in bioprocessing of recombinant proteins: expression hosts and process development. Front Bioeng Biotechnol 7:1\u201335. https:\/\/doi.org\/10.3389\/fbioe.2019.00420","journal-title":"Front Bioeng Biotechnol"},{"key":"10033_CR25","doi-asserted-by":"publisher","first-page":"205","DOI":"10.1080\/10826060701386695","volume":"37","author":"L Huang","year":"2007","unstructured":"Huang L, Ruan H, Gu W, Xu Z, Cen P, Fan L (2007) Functional expression and purification of bovine enterokinase light chain in recombinant Escherichia coli. Prep Biochem Biotechnol 37:205\u2013217","journal-title":"Prep Biochem Biotechnol"},{"key":"10033_CR26","doi-asserted-by":"publisher","first-page":"300","DOI":"10.1016\/S1046-5928(02)00012-8","volume":"25","author":"L Yuan","year":"2002","unstructured":"Yuan L, Hua Z (2002) Expression, purification, and characterization of a biologically active bovine enterokinase catalytic subunit in Escherichia coli. Prot Expr Purif 25:300\u2013304","journal-title":"Prot Expr Purif"},{"issue":"6324","key":"10033_CR27","first-page":"1","volume":"21","author":"A Sandomenico","year":"2020","unstructured":"Sandomenico A, Sivaccumar JP, Ruvo M (2020) Evolution of Escherichia coli expression system in producing antibody recombinant fragments. Int J Mol Sci 21(6324):1\u201339","journal-title":"Int J Mol Sci"},{"issue":"3","key":"10033_CR28","first-page":"206","volume":"19","author":"Z Dehghan","year":"2020","unstructured":"Dehghan Z, Ayat H, Ahadi AM (2020) Expression, purification and docking studies on IMe-AGAP, the first antitumor-analgesic like peptide from Iranian Scorpion Mesobuthus eupeus. Iran J Pharm Sci 19(3):206\u2013216","journal-title":"Iran J Pharm Sci"},{"key":"10033_CR29","doi-asserted-by":"publisher","first-page":"1085","DOI":"10.1007\/s10529-013-1180-z","volume":"35","author":"A Abbas","year":"2013","unstructured":"Abbas A, Plattner S, Hussain Shah K, Bohlmann H (2013) Comparison of periplasmic and intracellular expression of Arabidopsis thionin proproteins in E. coli. Biotechnol Lett 35:1085\u20131091","journal-title":"Biotechnol Lett"},{"key":"10033_CR30","doi-asserted-by":"publisher","first-page":"23311","DOI":"10.1016\/S0021-9258(19)49464-7","volume":"31","author":"ER LaVallie","year":"1993","unstructured":"LaVallie ER, Rehemtulla A, Racie LA, DiBlasio EA, Ferenz C, Grant KL, Light A, McCoy JM (1993) Cloning and functional expression of a cDNA encoding the catalytic subunit of bovine Enterokinase. J Biol Chem 31:23311\u201323317. https:\/\/doi.org\/10.1016\/S0021-9258(19)49464-7","journal-title":"J Biol Chem"},{"key":"10033_CR31","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1006\/abbi.2001.2737","volume":"400","author":"HW Song","year":"2002","unstructured":"Song HW, Choi S, Seong BL (2002) Engineered recombinant enteropeptidase catalytic subunit: effect of N-terminal modification. Biochim Biophys Acta 400:1\u20136. https:\/\/doi.org\/10.1006\/abbi.2001.2737","journal-title":"Biochim Biophys Acta"}],"container-title":["The Protein Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s10930-021-10033-6.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s10930-021-10033-6\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s10930-021-10033-6.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,11,4]],"date-time":"2022-11-04T00:35:05Z","timestamp":1667522105000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s10930-021-10033-6"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,1,29]]},"references-count":31,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2022,2]]}},"alternative-id":["10033"],"URL":"https:\/\/doi.org\/10.1007\/s10930-021-10033-6","relation":{},"ISSN":["1572-3887","1875-8355"],"issn-type":[{"value":"1572-3887","type":"print"},{"value":"1875-8355","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,1,29]]},"assertion":[{"value":"26 November 2021","order":1,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"29 January 2022","order":2,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}}]}}