{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,6]],"date-time":"2026-09-06T10:26:45Z","timestamp":1788690405187,"version":"build-2803163510"},"reference-count":43,"publisher":"American Dairy Science Association","issue":"11","license":[{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,8,18]],"date-time":"2025-08-18T00:00:00Z","timestamp":1755475200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100008994","name":"Universidade de Bras\u00edlia","doi-asserted-by":"publisher","award":["001\/2025 DPI\/BCE\/UnB"],"award-info":[{"award-number":["001\/2025 DPI\/BCE\/UnB"]}],"id":[{"id":"10.13039\/100008994","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["INCT \\u2212406375\/2022-4"],"award-info":[{"award-number":["INCT \\u2212406375\/2022-4"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journalofdairyscience.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Dairy Science"],"published-print":{"date-parts":[[2025,11]]},"DOI":"10.3168\/jds.2025-26935","type":"journal-article","created":{"date-parts":[[2025,8,21]],"date-time":"2025-08-21T00:41:52Z","timestamp":1755736912000},"page":"12096-12107","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":3,"title":["A comparison of different constitutive expression systems for the production of bovine chymosin in Komagataella phaffii"],"prefix":"10.3168","volume":"108","author":[{"given":"Roberta F.","family":"Barros","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Janice L.","family":"De Marco","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luiza C.","family":"Piva","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cintia M.","family":"Coelho","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lidia Maria P.","family":"de Moraes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fernando A.G.","family":"Torres","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1747","reference":[{"key":"10.3168\/jds.2025-26935_bib1","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1007\/s00253-006-0698-6","article-title":"Translation elongation factor 1-\u03b1 gene from Pichia pastoris: Molecular cloning, sequence, and use of its promoter","volume":"74","author":"Ahn","year":"2007","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.3168\/jds.2025-26935_bib2","doi-asserted-by":"crossref","DOI":"10.1016\/j.heliyon.2021.e07137","article-title":"Constitutive expression of Camelus bactrianus prochymosin B in Pichia pastoris.","volume":"7","author":"Akishev","year":"2021","journal-title":"Heliyon"},{"key":"10.3168\/jds.2025-26935_bib3","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1007\/s10529-015-2002-2","article-title":"A constitutive expression system for Pichia pastoris based on the PGK1 promoter","volume":"38","author":"Arruda","year":"2016","journal-title":"Biotechnol. Lett."},{"key":"10.3168\/jds.2025-26935_bib4","doi-asserted-by":"crossref","first-page":"1542","DOI":"10.1002\/bit.25916","article-title":"Droplet digital PCR-aided screening and characterization of Pichia pastoris multiple gene copy strains","volume":"113","author":"C\u00e1mara","year":"2016","journal-title":"Biotechnol. Bioeng."},{"key":"10.3168\/jds.2025-26935_bib5","doi-asserted-by":"crossref","first-page":"2962","DOI":"10.1002\/bit.26846","article-title":"Process development for the continuous production of heterologous proteins by the industrial yeast, Komagataella phaffii.","volume":"115","author":"Cankorur-Cetinkaya","year":"2018","journal-title":"Biotechnol. Bioeng."},{"key":"10.3168\/jds.2025-26935_bib6","doi-asserted-by":"crossref","first-page":"8245","DOI":"10.1093\/nar\/16.17.8245","article-title":"The UAS of the yeast PGK gene is composed of multiple functional elements","volume":"16","author":"Chambers","year":"1988","journal-title":"Nucleic Acids Res."},{"key":"10.3168\/jds.2025-26935_bib7","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1002\/yea.1243","article-title":"Molecular characterization of the 3-phosphoglycerate kinase gene (PGK1) from the methylotrophic yeast Pichia pastoris.","volume":"22","author":"de Almeida","year":"2005","journal-title":"Yeast"},{"key":"10.3168\/jds.2025-26935_bib8","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.bej.2019.03.027","article-title":"Continuous operation, a realistic alternative to fed-batch fermentation for the production of recombinant lipase B from Candida antarctica under the constitutive promoter PGK in Pichia pastoris.","volume":"147","author":"de Macedo Robert","year":"2019","journal-title":"Biochem. Eng. J."},{"key":"10.3168\/jds.2025-26935_bib9","doi-asserted-by":"crossref","first-page":"2664","DOI":"10.1021\/acs.jafc.1c07908","article-title":"Efficient bioproduction of human milk alpha-lactalbumin in Komagataella phaffii.","volume":"70","author":"Deng","year":"2022","journal-title":"J. Agric. Food Chem."},{"key":"10.3168\/jds.2025-26935_bib10","doi-asserted-by":"crossref","first-page":"1380","DOI":"10.1021\/pr8007623","article-title":"The effect of temperature on the proteome of recombinant Pichia pastoris.","volume":"8","author":"Dragosits","year":"2009","journal-title":"J. Proteome Res."},{"key":"10.3168\/jds.2025-26935_bib11","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.34595","article-title":"Estimating the protein burden limit of yeast cells by measuring the expression limits of glycolytic proteins","volume":"7","author":"Eguchi","year":"2018","journal-title":"eLife"},{"key":"10.3168\/jds.2025-26935_bib12","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1134\/S0003683820060058","article-title":"Optimization of the production method for recombinant chymosin in the methylotrophic yeast Komagataella phaffii.","volume":"56","author":"Filkin","year":"2020","journal-title":"Appl. Biochem. Microbiol."},{"issue":"sup210","key":"10.3168\/jds.2025-26935_bib13","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1080\/00365519209104656","article-title":"Chymosin: A short review on foetal and neonatal gastric proteases","volume":"52","author":"Foltmann","year":"1992","journal-title":"Scand. J. Clin. Lab. Invest."},{"key":"10.3168\/jds.2025-26935_bib14","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1016\/j.procbio.2016.02.018","article-title":"A step forward to improve recombinant protein production in Pichia pastoris: From specific growth rate effect on protein secretion to carbon-starving conditions as advanced strategy","volume":"51","author":"Garcia-Ortega","year":"2016","journal-title":"Process Biochem."},{"key":"10.3168\/jds.2025-26935_bib15","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1186\/1471-2164-8-179","article-title":"Monitoring of transcriptional regulation in Pichia pastoris under protein production conditions","volume":"8","author":"Gasser","year":"2007","journal-title":"BMC Genomics"},{"key":"10.3168\/jds.2025-26935_bib16","doi-asserted-by":"crossref","DOI":"10.3389\/fbioe.2022.818434","article-title":"Innovative bioprocess strategies combining physiological control and strain engineering of Pichia pastoris to improve recombinant protein production","volume":"10","author":"Gasset","year":"2022","journal-title":"Front. Bioeng. Biotechnol."},{"key":"10.3168\/jds.2025-26935_bib17","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/0734-9750(95)00004-A","article-title":"Metabolic load and heterologous gene expression","volume":"13","author":"Glick","year":"1995","journal-title":"Biotechnol. Adv."},{"key":"10.3168\/jds.2025-26935_bib18","doi-asserted-by":"crossref","first-page":"118","DOI":"10.3389\/fbioe.2020.00118","article-title":"A combinational strategy for effective heterologous production of functional human lysozyme in Pichia pastoris.","volume":"8","author":"He","year":"2020","journal-title":"Front. Bioeng. Biotechnol."},{"key":"10.3168\/jds.2025-26935_bib19","doi-asserted-by":"crossref","first-page":"E11025","DOI":"10.1073\/pnas.1809921115","article-title":"Engineering the protein secretory pathway of Saccharomyces cerevisiae enables improved protein production","volume":"115","author":"Huang","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.3168\/jds.2025-26935_bib20","series-title":"IDF standard 157. Determination of the total clotting activity of bovine rennets","author":"IDF (International Dairy Federation)","year":"2007"},{"key":"10.3168\/jds.2025-26935_bib21","doi-asserted-by":"crossref","first-page":"2087","DOI":"10.1007\/s11274-012-1012-7","article-title":"Constitutive expression, purification and characterization of bovine prochymosin in Pichia pastoris GS115","volume":"28","author":"Jiang","year":"2012","journal-title":"World J. Microbiol. Biotechnol."},{"key":"10.3168\/jds.2025-26935_bib22","doi-asserted-by":"crossref","first-page":"1174","DOI":"10.3168\/jds.S0022-0302(06)72186-5","article-title":"Major technological advances and trends in cheese","volume":"89","author":"Johnson","year":"2006","journal-title":"J. Dairy Sci."},{"key":"10.3168\/jds.2025-26935_bib23","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1186\/s13068-021-02013-w","article-title":"Oxidative stress tolerance contributes to heterologous protein production in Pichia pastoris.","volume":"14","author":"Lin","year":"2021","journal-title":"Biotechnol. Biofuels"},{"key":"10.3168\/jds.2025-26935_bib24","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodres.2021.110704","article-title":"Advances in research on calf rennet substitutes and their effects on cheese quality","volume":"149","author":"Liu","year":"2021","journal-title":"Food Res. Int."},{"key":"10.3168\/jds.2025-26935_bib25","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.jbiotec.2004.04.035","article-title":"Stress in recombinant protein producing yeasts","volume":"113","author":"Mattanovich","year":"2004","journal-title":"J. Biotechnol."},{"key":"10.3168\/jds.2025-26935_bib26","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.jbiotec.2014.08.035","article-title":"Synergistic modular promoter and gene optimization to push cellulase secretion by Pichia pastoris beyond existing benchmarks","volume":"191","author":"Mellitzer","year":"2014","journal-title":"J. Biotechnol."},{"key":"10.3168\/jds.2025-26935_bib27","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1186\/1475-2859-11-61","article-title":"Expression of lignocellulolytic enzymes in Pichia pastoris.","volume":"11","author":"Mellitzer","year":"2012","journal-title":"Microb. Cell Fact."},{"key":"10.3168\/jds.2025-26935_bib28","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1111\/1751-7915.13498","article-title":"Rationale-based selection of optimal operating strategies and gene dosage impact on recombinant protein production in Komagataella phaffii (Pichia pastoris)","volume":"13","author":"Nieto-Taype","year":"2020","journal-title":"Microb. Biotechnol."},{"key":"10.3168\/jds.2025-26935_bib29","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.pep.2014.09.014","article-title":"Bioprocess and downstream optimization of recombinant bovine chymosin B in Pichia (Komagataella) pastoris under methanol-inducible AOXI promoter","volume":"104","author":"Noseda","year":"2014","journal-title":"Protein Expr. Purif."},{"key":"10.3168\/jds.2025-26935_bib30","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.pep.2016.03.008","article-title":"Production in stirred-tank bioreactor of recombinant bovine chymosin B by a high-level expression transformant clone of Pichia pastoris.","volume":"123","author":"Noseda","year":"2016","journal-title":"Protein Expr. Purif."},{"key":"10.3168\/jds.2025-26935_bib31","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1016\/j.molcel.2018.07.017","article-title":"Emerging principles of gene expression programs and their regulation","volume":"71","author":"Pope","year":"2018","journal-title":"Mol. Cell"},{"key":"10.3168\/jds.2025-26935_bib32","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1007\/BF00986958","article-title":"Peptide-chain elongation in eukaryotes","volume":"19","author":"Proud","year":"1994","journal-title":"Mol. Biol. Rep."},{"key":"10.3168\/jds.2025-26935_bib33","series-title":"Molecular Cloning: A Laboratory Manual","author":"Sambrook","year":"2001"},{"key":"10.3168\/jds.2025-26935_bib34","doi-asserted-by":"crossref","first-page":"3211","DOI":"10.1007\/s00253-021-11195-0","article-title":"Identification of a novel promoter for driving antibiotic-resistant genes to reduce the metabolic burden during protein expression and effectively select multiple integrations in Pichia pastoris.","volume":"105","author":"Shen","year":"2021","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.3168\/jds.2025-26935_bib35","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.jbiotec.2010.09.957","article-title":"Identification and characterization of novel Pichia pastoris promoters for heterologous protein production","volume":"150","author":"Stadlmayr","year":"2010","journal-title":"J. Biotechnol."},{"key":"10.3168\/jds.2025-26935_bib36","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1186\/1741-7007-10-16","article-title":"Imbalance of heterologous protein folding and disulfide bond formation rates yields runaway oxidative stress","volume":"10","author":"Tyo","year":"2012","journal-title":"BMC Biol."},{"key":"10.3168\/jds.2025-26935_bib37","doi-asserted-by":"crossref","first-page":"609","DOI":"10.3168\/jds.2011-4445","article-title":"Short communication: A comparative analysis of recombinant chymosins","volume":"95","author":"Vallejo","year":"2012","journal-title":"J. Dairy Sci."},{"key":"10.3168\/jds.2025-26935_bib38","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1016\/j.jbiotec.2006.02.024","article-title":"Increased production of chymosin by glycosylation","volume":"125","author":"van den Brink","year":"2006","journal-title":"J. Biotechnol."},{"key":"10.3168\/jds.2025-26935_bib39","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/j.nbt.2012.11.010","article-title":"Regulation of Pichia pastoris promoters and its consequences for protein production","volume":"30","author":"Vogl","year":"2013","journal-title":"N. Biotechnol."},{"key":"10.3168\/jds.2025-26935_bib40","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1186\/s12934-022-01904-3","article-title":"The introduction of an N-glycosylation site into prochymosin greatly enhances its production and secretion by Pichia pastoris.","volume":"21","author":"Wang","year":"2022","journal-title":"Microb. Cell Fact."},{"key":"10.3168\/jds.2025-26935_bib41","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/S0378-1119(96)00675-0","article-title":"Isolation of the Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase gene and regulation and use of its promoter","volume":"186","author":"Waterham","year":"1997","journal-title":"Gene"},{"key":"10.3168\/jds.2025-26935_bib42","doi-asserted-by":"crossref","DOI":"10.1016\/j.enzmictec.2020.109671","article-title":"High-level production of glucose oxidase in Pichia pastoris: Effects of Hac1p overexpression on cell physiology and enzyme expression","volume":"141","author":"Yu","year":"2020","journal-title":"Enzyme Microb. Technol."},{"key":"10.3168\/jds.2025-26935_bib43","doi-asserted-by":"crossref","first-page":"10235","DOI":"10.1021\/acs.jafc.1c04124","article-title":"Efficient secretory expression and purification of food-grade porcine myoglobin in Komagataella phaffii.","volume":"69","author":"Zhang","year":"2021","journal-title":"J. Agric. Food Chem."}],"container-title":["Journal of Dairy Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022030225006915?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022030225006915?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T23:00:07Z","timestamp":1778626807000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022030225006915"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,11]]},"references-count":43,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2025,11]]}},"alternative-id":["S0022030225006915"],"URL":"https:\/\/doi.org\/10.3168\/jds.2025-26935","relation":{},"ISSN":["0022-0302"],"issn-type":[{"value":"0022-0302","type":"print"}],"subject":[],"published":{"date-parts":[[2025,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"A comparison of different constitutive expression systems for the production of bovine chymosin in Komagataella phaffii","name":"articletitle","label":"Article Title"},{"value":"Journal of Dairy Science","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.3168\/jds.2025-26935","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Author(s).","name":"copyright","label":"Copyright"}]}}