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Here, an integrated engineering strategy combining signal peptide optimization, transcription factor overexpression, and gene dosage amplification was established to enhance recombinant EGF production in Komagataella phaffii. Truncation of amino acids 57\u201370 in the \u03b1-factor signal peptide increased EGF secretion efficiency from 69.8% to 95.3% and yield from 21.86 to 36.07 mg\/L. Mit1 overexpression increased the yield to 42.44 mg\/L, while sequential gene dosage amplification enhanced EGF yield to 280.42 mg\/L in shake-flask culture, representing a 12.8-fold increase. The engineered strain was evaluated in a 5 L bioreactor, achieving 370.05 mg\/L EGF. Purified recombinant EGF exhibited biological activity by promoting porcine skeletal muscle satellite cell proliferation under low-serum conditions. This study provides an efficient strategy for recombinant EGF production in K. phaffii and supports its application in cultured meat development.<\/jats:p>","DOI":"10.1021\/acs.jafc.6c11610","type":"journal-article","created":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T08:01:43Z","timestamp":1791360103000},"page":"32448-32457","source":"Crossref","is-referenced-by-count":0,"title":["Efficient Expression\nof Epidermal Growth Factor in\n                    <i>Komagataella phaffii<\/i>\n                    and Its Bioactivity Evaluation\nin Cell Culture"],"prefix":"10.1021","volume":"74","author":[{"given":"Yihan","family":"Shen","sequence":"first","affiliation":[{"name":"Ocean University of China , , ,","place":["Qingdao, P. R. China, 266404"]},{"name":"Qingdao Institute of Marine Bio-Manufacturing Industry , , ,","place":["Qingdao, P. R. China, 266071"]},{"name":"China National Light Industry , , ,","place":["Qingdao, P. R. China, 266404"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yan","family":"Li","sequence":"additional","affiliation":[{"name":"Ocean University of China , , ,","place":["Qingdao, P. R. China, 266404"]},{"name":"Qingdao Institute of Marine Bio-Manufacturing Industry , , ,","place":["Qingdao, P. R. China, 266071"]},{"name":"China National Light Industry , , ,","place":["Qingdao, P. R. China, 266404"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suxue","family":"Chen","sequence":"additional","affiliation":[{"name":"Ocean University of China , , ,","place":["Qingdao, P. R. China, 266404"]},{"name":"Qingdao Institute of Marine Bio-Manufacturing Industry , , ,","place":["Qingdao, P. R. China, 266071"]},{"name":"China National Light Industry , , ,","place":["Qingdao, P. R. China, 266404"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haipeng","family":"Su","sequence":"additional","affiliation":[{"name":"Ocean University of China , , ,","place":["Qingdao, P. R. China, 266404"]},{"name":"Qingdao Institute of Marine Bio-Manufacturing Industry , , ,","place":["Qingdao, P. R. China, 266071"]},{"name":"China National Light Industry , , ,","place":["Qingdao, P. R. China, 266404"]},{"name":"Ocean University of China , , ,","place":["Sanya, China, 572025"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohamed A.","family":"Balah","sequence":"additional","affiliation":[{"name":"Desert Research Center , , ,","place":["Cairo, Egypt, 11753"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6976-2906","authenticated-orcid":true,"given":"Changhu","family":"Xue","sequence":"additional","affiliation":[{"name":"Ocean University of China , , ,","place":["Qingdao, P. R. China, 266404"]},{"name":"Qingdao Institute of Marine Bio-Manufacturing Industry , , ,","place":["Qingdao, P. R. China, 266071"]},{"name":"China National Light Industry , , ,","place":["Qingdao, P. R. China, 266404"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2939-2514","authenticated-orcid":true,"given":"Hong","family":"Jiang","sequence":"additional","affiliation":[{"name":"Ocean University of China , , ,","place":["Qingdao, P. R. China, 266404"]},{"name":"Qingdao Institute of Marine Bio-Manufacturing Industry , , ,","place":["Qingdao, P. R. China, 266071"]},{"name":"China National Light Industry , , ,","place":["Qingdao, P. R. China, 266404"]},{"name":"Ocean University of China , , ,","place":["Sanya, China, 572025"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6315-1338","authenticated-orcid":true,"given":"Xiangzhao","family":"Mao","sequence":"additional","affiliation":[{"name":"Ocean University of China , , ,","place":["Qingdao, P. R. China, 266404"]},{"name":"Qingdao Institute of Marine Bio-Manufacturing Industry , , ,","place":["Qingdao, P. R. China, 266071"]},{"name":"China National Light Industry , , ,","place":["Qingdao, P. R. China, 266404"]},{"name":"Ocean University of China , , ,","place":["Sanya, China, 572025"]},{"name":"Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology , ,","place":["Qingdao, P. R. China, 266237"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,10,7]]},"reference":[{"key":"2026102109082994200_cit1","doi-asserted-by":"publisher","DOI":"10.1016\/j.foodchem.2024.140696","article-title":"A Rich-Nutritious\nCultured Meat via Bovine Myocytes and Adipocytes Co-Culture: Novel\nProspect for Cultured Meat Production Techniques","volume":"460","author":"Wang","year":"2024","journal-title":"Food Chem."},{"issue":"28","key":"2026102109082994200_cit2","doi-asserted-by":"publisher","first-page":"17909","DOI":"10.1021\/acs.jafc.5c03314","article-title":"Biocompatibility, Physicochemical\nProperties, and Allergenicity Evaluation of Fish Gelatin Hydrogels\nas Cell-Cultured Meat Scaffold Material","volume":"73","author":"Wang","year":"2025","journal-title":"J.\nAgric. Food Chem."},{"issue":"11","key":"2026102109082994200_cit3","doi-asserted-by":"publisher","first-page":"6981","DOI":"10.1021\/acs.jafc.4c12089","article-title":"Preparation\nof Cell-Cultured Fish Fat via Adipogenic Transdifferentiation of Larimichthys crocea Muscle Satellite Cells","volume":"73","author":"Wei","year":"2025","journal-title":"J. Agric. Food Chem."},{"issue":"9","key":"2026102109082994200_cit4","doi-asserted-by":"publisher","DOI":"10.26599\/FSHW.2024.9250222","article-title":"Research on Organized\nMethod and Regulatory Mechanism of Cell Cultured\nMeat Based on Modified Silk","volume":"14","author":"Yang","year":"2025","journal-title":"Food Sci. Hum.\nWellness"},{"issue":"6","key":"2026102109082994200_cit5","doi-asserted-by":"publisher","first-page":"721","DOI":"10.1016\/j.tibtech.2021.11.004","article-title":"Bioprocessing\nTechnology\nof Muscle Stem Cells: Implications for Cultured Meat","volume":"40","author":"Guan","year":"2022","journal-title":"Trends Biotechnol."},{"issue":"1","key":"2026102109082994200_cit6","doi-asserted-by":"publisher","first-page":"74","DOI":"10.1038\/s43016-021-00419-1","article-title":"A Serum-Free\nMedia Formulation for Cultured Meat Production Supports Bovine Satellite\nCell Differentiation in the Absence of Serum Starvation","volume":"3","author":"Messmer","year":"2022","journal-title":"Nat. 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Int."},{"issue":"11","key":"2026102109082994200_cit10","doi-asserted-by":"publisher","first-page":"6064","DOI":"10.1021\/acs.jafc.4c00624","article-title":"Integrated\nOmics Approach: Revealing the Mechanism of Auxenochlorella pyrenoidosa Protein Extract Replacing Fetal Bovine\nSerum for Fish Muscle Cell Culture","volume":"72","author":"Dong","year":"2024","journal-title":"J. Agric.\nFood Chem."},{"issue":"5","key":"2026102109082994200_cit11","doi-asserted-by":"publisher","first-page":"775","DOI":"10.5851\/kosfa.2022.e46","article-title":"Review of the Current\nResearch on\nFetal Bovine Serum and the Development of Cultured Meat","volume":"42","author":"Lee","year":"2022","journal-title":"Food Sci. Anim. Resour."},{"key":"2026102109082994200_cit12","doi-asserted-by":"publisher","DOI":"10.1016\/j.fbio.2022.101571","article-title":"An effective cytokine\ncombination for ex vivo expansion of porcine muscle stem cells","volume":"46","author":"Lei","year":"2022","journal-title":"Food Biosci."},{"issue":"1","key":"2026102109082994200_cit13","doi-asserted-by":"publisher","DOI":"10.1038\/s42003-024-07400-1","article-title":"A Spontaneously Immortalized Muscle Stem Cell Line\n(EfMS) from Brown-Marbled Grouper for Cell-Cultured Fish Meat Production","volume":"7","author":"Xue","year":"2024","journal-title":"Commun. Biol."},{"issue":"18","key":"2026102109082994200_cit14","doi-asserted-by":"publisher","first-page":"5705","DOI":"10.1021\/bi9602268","article-title":"Activation of Epidermal Growth Factor\nReceptor by Epidermal Growth\nFactor","volume":"35","author":"Sherrill","year":"1996","journal-title":"Biochemistry"},{"issue":"12","key":"2026102109082994200_cit15","doi-asserted-by":"publisher","first-page":"9293","DOI":"10.1021\/acs.analchem.5c08113","article-title":"Dose-Dependent Inhibition\nof Protein Glycosylation\nReveals Crosstalk between Glycosylation and Phosphorylation in EGF\nSignaling Pathways","volume":"98","author":"Liu","year":"2026","journal-title":"Anal. Chem."},{"key":"2026102109082994200_cit16","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1016\/j.semcdb.2014.01.011","article-title":"Epidermal Growth Factor, from Gene Organization to\nBedside","volume":"28","author":"Zeng","year":"2014","journal-title":"Semin. Cell Dev. Biol."},{"issue":"7457","key":"2026102109082994200_cit17","doi-asserted-by":"publisher","first-page":"166","DOI":"10.1038\/nature12308","article-title":"Temporal Regulation\nof EGF Signalling Networks by the Scaffold Protein Shc1","volume":"499","author":"Zheng","year":"2013","journal-title":"Nature"},{"key":"2026102109082994200_cit18","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1016\/j.procbio.2024.07.022","article-title":"Production\nof Recombinant Human Epidermal\nGrowth Factor in Escherichia coli:\nStrategic Upstream and Downstream Considerations for High Protein\nYield","volume":"146","author":"Wong","year":"2024","journal-title":"Process Biochem."},{"key":"2026102109082994200_cit19","doi-asserted-by":"publisher","DOI":"10.1016\/j.pep.2025.106827","article-title":"Secretory\nExpression and Fermentation Optimization of Recombinant Porcine Epidermal\nGrowth Factor in Saccharomyces cerevisiae","volume":"237","author":"Liu","year":"2026","journal-title":"Protein Expression Purif."},{"issue":"3","key":"2026102109082994200_cit20","doi-asserted-by":"publisher","first-page":"758","DOI":"10.1002\/btpr.2086","article-title":"A pH-induced,\nIntein-mediated\nExpression and Purification of Recombinant Human Epidermal Growth\nFactor in Escherichia coli","volume":"31","author":"Zhang","year":"2015","journal-title":"Biotechnol. Prog."},{"issue":"1","key":"2026102109082994200_cit21","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-022-09060-9","article-title":"A Toolkit for Recombinant Production of Seven Human\nEGF Family Growth Factors in Active Conformation","volume":"12","author":"Ferreira","year":"2022","journal-title":"Sci. Rep."},{"key":"2026102109082994200_cit22","doi-asserted-by":"publisher","DOI":"10.1016\/j.foodres.2023.113017","article-title":"Efficient\nExpression\nof a Cytokine Combination in Saccharomyces cerevisiae for Cultured Meat Production","volume":"170","author":"Lei","year":"2023","journal-title":"Food Res. Int."},{"issue":"12","key":"2026102109082994200_cit23","doi-asserted-by":"publisher","DOI":"10.3390\/fermentation10120661","article-title":"Biofilm-Based Immobilization Fermentation\nfor Continuous hEGF Production in Saccharomyces cerevisiae","volume":"10","author":"Zhi","year":"2024","journal-title":"Fermentation"},{"issue":"2","key":"2026102109082994200_cit24","doi-asserted-by":"publisher","first-page":"286","DOI":"10.1016\/j.bjm.2016.10.017","article-title":"Production of Recombinant\nHuman Epidermal Growth Factor\nin Pichia pastoris","volume":"48","author":"Eissazadeh","year":"2017","journal-title":"Braz. J. Microbiol."},{"issue":"14","key":"2026102109082994200_cit25","doi-asserted-by":"publisher","first-page":"8555","DOI":"10.1021\/acs.jafc.5c00598","article-title":"Engineering Pichia pastoris for Efficient de novo Synthesis of 2\u2032-Fucosyllactose","volume":"73","author":"Fang","year":"2025","journal-title":"J.\nAgric. Food Chem."},{"issue":"6","key":"2026102109082994200_cit26","doi-asserted-by":"publisher","first-page":"561","DOI":"10.1038\/nbt.1544","article-title":"Genome Sequence of the Recombinant\nProtein Production Host Pichia pastoris","volume":"27","author":"De Schutter","year":"2009","journal-title":"Nat. Biotechnol."},{"issue":"21","key":"2026102109082994200_cit27","doi-asserted-by":"publisher","first-page":"15971","DOI":"10.1021\/acs.jafc.5c17284","article-title":"Metabolic Engineering of Microbial\nCell Factories for Efficient Heme\nBiosynthesis: Advances, Challenges, and Future Perspectives","volume":"74","author":"Cao","year":"2026","journal-title":"J. Agric. Food Chem."},{"issue":"1","key":"2026102109082994200_cit28","doi-asserted-by":"publisher","DOI":"10.1186\/s13068-022-02234-7","article-title":"Second Generation Pichia pastoris Strain and Bioprocess Designs","volume":"15","author":"Ergu\u0308n","year":"2022","journal-title":"Biotechnol. Biofuels Bioprod."},{"issue":"7","key":"2026102109082994200_cit29","doi-asserted-by":"publisher","DOI":"10.1093\/femsyr\/foab057","article-title":"Recombinant Protein\nProduction in Pichia pastoris: From\nTranscriptionally Redesigned Strains to Bioprocess Optimization and\nMetabolic Modelling","volume":"21","author":"Ergu\u0308n","year":"2021","journal-title":"FEMS Yeast Res."},{"issue":"3","key":"2026102109082994200_cit30","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1007\/s10930-021-09968-7","article-title":"Production of Industrial Enzymes via Pichia pastoris as a Cell Factory in Bioreactor: Current Status and Future Aspects","volume":"40","author":"Duman-O\u0308zdamar","year":"2021","journal-title":"Protein J."},{"key":"2026102109082994200_cit31","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2025.144270","article-title":"High-Level Secretory\nExpression of\nRecombinant Type III Human-like Collagen a1 in Pichia pastoris via Multilevel Systematic Optimization","volume":"313","author":"Wang","year":"2025","journal-title":"Int. J. Biol. Macromol."},{"issue":"1","key":"2026102109082994200_cit32","doi-asserted-by":"publisher","DOI":"10.1186\/s13068-022-02243-6","article-title":"The \u03b1-Mating\nFactor Secretion Signals and Endogenous Signal\nPeptides for Recombinant Protein Secretion in Komagataella phaffii","volume":"15","author":"Zou","year":"2022","journal-title":"Biotechnol. Biofuels\nBioprod."},{"issue":"15","key":"2026102109082994200_cit33","doi-asserted-by":"publisher","first-page":"9246","DOI":"10.1021\/acs.jafc.5c01338","article-title":"Ethanol-Inducible Bioproduction of\nHuman \u03b1-Lactalbumin in Komagataella phaffii","volume":"73","author":"Wang","year":"2025","journal-title":"J. Agric.\nFood Chem."},{"key":"2026102109082994200_cit34","doi-asserted-by":"publisher","DOI":"10.3389\/fcell.2025.1680263","article-title":"A Novel Proliferation Synergy Factor Cocktail Maintains Proliferation\nand Improves Transfection Efficiency in Muscle Cells and Fibroblasts\nunder Low-Serum Conditions","volume":"13","author":"Li","year":"2025","journal-title":"Front. Cell Dev.\nBiol."},{"issue":"1","key":"2026102109082994200_cit35","doi-asserted-by":"publisher","DOI":"10.1186\/1475-2859-7-11","article-title":"Protein Folding and Conformational\nStress in Microbial\nCells Producing Recombinant Proteins: A Host Comparative Overview","volume":"7","author":"Gasser","year":"2008","journal-title":"Microb. Cell Factories"},{"issue":"2","key":"2026102109082994200_cit36","doi-asserted-by":"publisher","first-page":"311","DOI":"10.1016\/j.gene.2013.01.062","article-title":"The Effect\nof \u03b1-Mating Factor Secretion Signal\nMutations on Recombinant Protein Expression in Pichia pastoris","volume":"519","author":"Lin-Cereghino","year":"2013","journal-title":"Gene"},{"issue":"9","key":"2026102109082994200_cit37","doi-asserted-by":"publisher","DOI":"10.1128\/aem.00296-22","article-title":"Potential of the Signal Peptide Derived from the PAS_chr3_0030 Gene Product for Secretory Expression of Valuable\nEnzymes in Pichia pastoris","volume":"88","author":"Shen","year":"2022","journal-title":"Appl. Environ. Microbiol."},{"issue":"1","key":"2026102109082994200_cit38","doi-asserted-by":"publisher","DOI":"10.1186\/s12934-020-01460-8","article-title":"Differential Role of Segments of\n\u03b1-Mating Factor\nSecretion Signal in Pichia pastoris towards Granulocyte Colony-Stimulating Factor Emerging from a Wild\nType or Codon Optimized Copy of the Gene","volume":"19","author":"Aggarwal","year":"2020","journal-title":"Microb.\nCell Factories"},{"issue":"1","key":"2026102109082994200_cit39","doi-asserted-by":"publisher","DOI":"10.1186\/s43141-023-00521-w","article-title":"Full-Length\nversus Truncated \u03b1-Factor Secretory\nSignal Sequences for Expression of Recombinant Human Insulin Precursor\nin Yeast Pichia pastoris: A Comparison","volume":"21","author":"Utami","year":"2023","journal-title":"J. Genet. Eng. Biotechnol."},{"key":"2026102109082994200_cit40","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.jbiotec.2024.04.008","article-title":"Optimizing Pichia pastoris protein secretion: Role of N-linked glycosylation\non the \u03b1-mating factor secretion signal leader","volume":"391","author":"Dai","year":"2024","journal-title":"J. Biotechnol."},{"issue":"1","key":"2026102109082994200_cit41","doi-asserted-by":"publisher","DOI":"10.1186\/s12934-018-1009-5","article-title":"An Improved\nSecretion Signal Enhances the Secretion of Model Proteins from Pichia pastoris","volume":"17","author":"Barrero","year":"2018","journal-title":"Microb. Cell\nFact."},{"key":"2026102109082994200_cit42","doi-asserted-by":"publisher","first-page":"50","DOI":"10.1016\/j.gene.2016.10.040","article-title":"Structural Characterization of the\n\u03b1-Mating Factor Prepro-Peptide for Secretion of Recombinant\nProteins in Pichia pastoris","volume":"598","author":"Chahal","year":"2017","journal-title":"Gene"},{"issue":"3","key":"2026102109082994200_cit43","doi-asserted-by":"publisher","first-page":"414","DOI":"10.1089\/ars.2014.5844","article-title":"Engineering of Protein\nFolding and Secretion\u2500Strategies to Overcome Bottlenecks for\nEfficient Production of Recombinant Proteins","volume":"21","author":"Delic","year":"2014","journal-title":"Antioxid. 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