{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,9]],"date-time":"2026-09-09T19:42:36Z","timestamp":1788982956152,"version":"build-2803163510"},"reference-count":36,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,9,1]],"date-time":"2022-09-01T00:00:00Z","timestamp":1661990400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,9,1]],"date-time":"2022-09-01T00:00:00Z","timestamp":1661990400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,9,1]],"date-time":"2022-09-01T00:00:00Z","timestamp":1661990400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,9,1]],"date-time":"2022-09-01T00:00:00Z","timestamp":1661990400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,9,1]],"date-time":"2022-09-01T00:00:00Z","timestamp":1661990400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,9,1]],"date-time":"2022-09-01T00:00:00Z","timestamp":1661990400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,9,1]],"date-time":"2022-09-01T00:00:00Z","timestamp":1661990400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100012964","name":"Minist\u00e8re de l\u2019Enseignement Sup\u00e9rieur et de la Recherche Scientifique","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100012964","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Toxicon"],"published-print":{"date-parts":[[2022,9]]},"DOI":"10.1016\/j.toxicon.2022.05.046","type":"journal-article","created":{"date-parts":[[2022,6,2]],"date-time":"2022-06-02T12:00:04Z","timestamp":1654171204000},"page":"1-10","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":6,"special_numbering":"C","title":["Efficient heterologous expression in Pichia pastoris, immobilization and functional characterization of a scorpion venom secreted phospholipase A2"],"prefix":"10.1016","volume":"216","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6008-8361","authenticated-orcid":false,"given":"Najeh","family":"Krayem","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rim","family":"Sidhoum","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Slim","family":"Cherif","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aida","family":"Karray","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.toxicon.2022.05.046_bib1","doi-asserted-by":"crossref","first-page":"5301","DOI":"10.1007\/s00253-014-5732-5","article-title":"Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production","volume":"98","author":"Ahmad","year":"2014","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.toxicon.2022.05.046_bib2","doi-asserted-by":"crossref","first-page":"6319","DOI":"10.1007\/s00253-018-9122-2","article-title":"Microbial production of toxins from the scorpion venom: properties and applications","volume":"102","author":"Amorim","year":"2018","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.toxicon.2022.05.046_bib3","first-page":"254","article-title":"Enzyme immobilization and its applications in food processing: a review","volume":"8","author":"Bashir","year":"2020","journal-title":"Int. J. Commun. Syst."},{"key":"10.1016\/j.toxicon.2022.05.046_bib4","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.toxicon.2022.05.046_bib5","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1385\/MB:16:1:23","article-title":"Recombinant protein expression in Pichia pastoris","volume":"16","author":"Cregg","year":"2000","journal-title":"Mol. Biotechnol."},{"key":"10.1016\/j.toxicon.2022.05.046_bib6","series-title":"Transformation, Pichia Protocols","first-page":"27","author":"Cregg","year":"1998"},{"key":"10.1016\/j.toxicon.2022.05.046_bib7","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s13205-012-0071-7","article-title":"Enzyme immobilization: an overview on techniques and support materials","volume":"3","author":"Datta","year":"2013","journal-title":"3 Biotech"},{"key":"10.1016\/j.toxicon.2022.05.046_bib8","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/0005-2736(75)90045-0","article-title":"Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayers","volume":"406","author":"Demel","year":"1975","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.toxicon.2022.05.046_bib9","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/j.bej.2009.09.009","article-title":"Organic solvent-tolerant enzymes","volume":"48","author":"Doukyu","year":"2010","journal-title":"Biochem. Eng. J."},{"key":"10.1016\/j.toxicon.2022.05.046_bib10","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1042\/bj3030527","article-title":"A study on the functional subunits of phospholipases A2 by enzyme immobilization","volume":"303","author":"Ferreira","year":"1994","journal-title":"Biochem. J."},{"key":"10.1016\/j.toxicon.2022.05.046_bib11","doi-asserted-by":"crossref","first-page":"8098","DOI":"10.1021\/bi00083a007","article-title":"Influence of chemistry in immobilization of cobra venom phospholipase A2: implications as to mechanism","volume":"32","author":"Ferreira","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2022.05.046_bib12","first-page":"5.24. 21","article-title":"Strategies to optimize protein expression in E. coli","volume":"61","author":"Francis","year":"2010","journal-title":"Curr. Proto. Prot. Sci."},{"key":"10.1016\/j.toxicon.2022.05.046_bib13","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1016\/j.toxicon.2009.05.024","article-title":"Functions, structures and Triton X-100 effect for the catalytic subunits of heterodimeric phospholipases A2 from Vipera nikolskii venom","volume":"54","author":"Gao","year":"2009","journal-title":"Toxicon : Off. J. Int. Soc. Toxicol."},{"key":"10.1016\/j.toxicon.2022.05.046_bib14","doi-asserted-by":"crossref","first-page":"2159","DOI":"10.1016\/S0021-9258(18)69185-9","article-title":"Human gastric lipase: a sulfhydryl enzyme","volume":"263","author":"Gargouri","year":"1988","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2022.05.046_bib15","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1016\/j.enzmictec.2004.06.002","article-title":"1-Butyl oleate synthesis by immobilized lipase from Rhizopus oryzae: a comparative study between n-hexane and solvent-free system","volume":"35","author":"Ghamgui","year":"2004","journal-title":"Enzym. Microb. Technol."},{"key":"10.1016\/j.toxicon.2022.05.046_bib16","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1016\/j.ijbiomac.2011.01.004","article-title":"Structural analysis of a group III Glu62-phospholipase A2 from the scorpion, Mesobuthus tamulus: targeting and reversible inhibition by native peptides","volume":"48","author":"Hariprasad","year":"2011","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.toxicon.2022.05.046_bib17","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1016\/j.toxicon.2011.01.002","article-title":"Arthropod venoms and cancer","volume":"57","author":"Heinen","year":"2011","journal-title":"Toxicon : Off. J. Int. Soc. Toxicol."},{"key":"10.1016\/j.toxicon.2022.05.046_bib18","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.colsurfb.2017.12.002","article-title":"Interactions between surfactants and hydrolytic enzymes","volume":"168","author":"Holmberg","year":"2018","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"10.1016\/j.toxicon.2022.05.046_bib19","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1016\/j.procbio.2008.06.004","article-title":"Enzyme stability and stabilization\u2014aqueous and non-aqueous environment","volume":"43","author":"Iyer","year":"2008","journal-title":"Process Biochem."},{"key":"10.1016\/j.toxicon.2022.05.046_bib20","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1007\/s10068-014-0165-6","article-title":"Effects of organic solvents on transesterification of phospholipids using phospholipase A 2 and lipase","volume":"23","author":"Kim","year":"2014","journal-title":"Food Sci. Biotechnol."},{"key":"10.1016\/j.toxicon.2022.05.046_bib21","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.toxicon.2020.05.020","article-title":"Scorpion venom phospholipases A2: a minireview","volume":"184","author":"Krayem","year":"2020","journal-title":"Toxicon : Off. J. Int. Soc. Toxicol."},{"key":"10.1016\/j.toxicon.2022.05.046_bib22","doi-asserted-by":"crossref","first-page":"1247","DOI":"10.1016\/j.bbagen.2018.02.004","article-title":"Functional characterization and FTIR-based 3D modeling of full length and truncated forms of Scorpio maurus venom phospholipase A2","volume":"1862","author":"Krayem","year":"2018","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"10.1016\/j.toxicon.2022.05.046_bib23","doi-asserted-by":"crossref","first-page":"14174","DOI":"10.1021\/bi991432t","article-title":"Expression of group IA phospholipase A2 in Pichia pastoris: identification of a phosphatidylcholine activator site using site-directed mutagenesis","volume":"38","author":"Lefkowitz","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2022.05.046_bib24","doi-asserted-by":"crossref","first-page":"1663","DOI":"10.1016\/S0960-894X(01)00277-3","article-title":"A simple method to obtain a covalent immobilized phospholipase A2","volume":"11","author":"Madoery","year":"2001","journal-title":"Bioorg. Med. Chem. Lett"},{"key":"10.1016\/j.toxicon.2022.05.046_bib25","doi-asserted-by":"crossref","first-page":"599","DOI":"10.5650\/jos.ess13231","article-title":"Characterization and catalytic properties of free and silica-bound lipase: a comparative study","volume":"63","author":"Narwal","year":"2014","journal-title":"J. Oleo Sci."},{"key":"10.1016\/j.toxicon.2022.05.046_bib26","doi-asserted-by":"crossref","first-page":"157","DOI":"10.5757\/ASCT.2017.26.6.157","article-title":"An overview of techniques in enzyme immobilization","volume":"26","author":"Nguyen","year":"2017","journal-title":"Appl. Sci. Converg. Technol."},{"key":"10.1016\/j.toxicon.2022.05.046_bib27","first-page":"148","article-title":"A review on methods, application and properties of immobilized enzyme","volume":"1","author":"Nisha","year":"2012","journal-title":"Chem. Sci. Rev. Lett."},{"key":"10.1016\/j.toxicon.2022.05.046_bib28","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1016\/j.jmb.2007.03.034","article-title":"Structural basis for bile salt inhibition of pancreatic phospholipase A2","volume":"369","author":"Pan","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.toxicon.2022.05.046_bib29","doi-asserted-by":"crossref","first-page":"2691","DOI":"10.1021\/bi00580a001","article-title":"Regulation of phospholipase A2 activity by the lipid-water interface: a monolayer approach","volume":"18","author":"Pattus","year":"1979","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2022.05.046_bib30","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S1388-1981(00)00105-0","article-title":"The expanding superfamily of phospholipase A 2 enzymes: classification and characterization","volume":"1488","author":"Six","year":"2000","journal-title":"Biochim. Biophys. Acta Mol. Cell Biol. Lipids"},{"key":"10.1016\/j.toxicon.2022.05.046_bib31","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1007\/s00253-006-0465-8","article-title":"Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems","volume":"72","author":"Terpe","year":"2006","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.toxicon.2022.05.046_bib32","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.molcatb.2006.06.009","article-title":"Application of binary immobilized Candida rugosa lipase for hydrolysis of soybean oil","volume":"42","author":"Ting","year":"2006","journal-title":"J. Mol. Catal. B Enzym."},{"key":"10.1016\/j.toxicon.2022.05.046_bib33","doi-asserted-by":"crossref","first-page":"4753","DOI":"10.1111\/j.1432-1033.2004.04439.x","article-title":"Phaiodotoxin, a novel structural class of insect-toxin isolated from the venom of the Mexican scorpion Anuroctonus phaiodactylus","volume":"271","author":"Valdez-Cruz","year":"2004","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.toxicon.2022.05.046_bib34","doi-asserted-by":"crossref","first-page":"31195","DOI":"10.1074\/jbc.274.44.31195","article-title":"On the diversity of secreted phospholipases A2 cloning, tissue distribution, and functional expression of two novel mouse group II enzymes","volume":"274","author":"Valentin","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2022.05.046_bib35","doi-asserted-by":"crossref","first-page":"4962","DOI":"10.1021\/bi00069a035","article-title":"Conformational changes in oxidized phospholipids and their preferential hydrolysis by phospholipase A2: a monolayer study","volume":"32","author":"van den Berg","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2022.05.046_bib36","doi-asserted-by":"crossref","first-page":"15307","DOI":"10.1021\/bi00046a040","article-title":"Phospholipase A2 engineering. The roles of disulfide bonds in structure, conformational stability, and catalytic function","volume":"34","author":"Zhu","year":"1995","journal-title":"Biochemistry"}],"container-title":["Toxicon"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010122001763?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010122001763?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,22]],"date-time":"2025-09-22T21:20:46Z","timestamp":1758576046000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0041010122001763"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,9]]},"references-count":36,"alternative-id":["S0041010122001763"],"URL":"https:\/\/doi.org\/10.1016\/j.toxicon.2022.05.046","relation":{},"ISSN":["0041-0101"],"issn-type":[{"value":"0041-0101","type":"print"}],"subject":[],"published":{"date-parts":[[2022,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Efficient heterologous expression in Pichia pastoris, immobilization and functional characterization of a scorpion venom secreted phospholipase A2","name":"articletitle","label":"Article Title"},{"value":"Toxicon","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.toxicon.2022.05.046","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}