Authors
Yihan Shen, Yan Li, Suxue Chen, Haipeng Su, Mohamed A Balah, Changhu Xue, Hong Jiang, Xiangzhao Mao
Published in
Journal of agricultural and food chemistry. Volume 74. Issue 41. Pages 32448-32457. Oct 21, 2026.
Abstract
Epidermal growth factor (EGF) is an important growth factor for low-serum cultured meat production, yet efficient recombinant expression remains challenging. 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 57-70 in the α-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.
PMID:
42904972
Bibliographic data and abstract were imported from PubMed on 23 Oct 2026.
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