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Expression of the hybrid antimicrobial peptide lactoferrin–lysozyme in Pichia pastoris
Author(s) -
Sun Jie,
Jiang Jie,
Liu Lifeng,
Wang Zhao,
Wei Chun
Publication year - 2018
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1002/bab.1705
Subject(s) - pichia pastoris , lactoferrin , lysozyme , antimicrobial , peptide , antimicrobial peptides , antibacterial activity , escherichia coli , microbiology and biotechnology , biochemistry , biology , chemistry , bacteria , recombinant dna , gene , genetics
The use of lactoferrin antimicrobial peptides and lysozymes as traditional antibiotic alternatives is suitable for solving drug residue and pathogen resistance. In this study, bovine lactoferrin (LfcinB) and human lysozyme (hLY) were combined through fusion expression in Pichia pastoris GS115 driven by constitutive GAP promoter. For neutralizing the toxic property of the antimicrobial peptide, anion antioxidant peptides from porcine myofibrillar protein and enzymatically hydrolyzed chicken egg white were fused to the hybrid antimicrobial peptide LfcinB–hLY. The 72‐H culture supernatant of the strain GS–LfcinB–hLY exhibited antibacterial activity toward both Escherichia coli K88 and Staphylococcus aureus (ATCC 25923). The LfcinB–hLY yield was 15.7 mg/L, and approximately 1.8 mg of pure LfcinB–hLY was obtained from 500 mL of cell culture after purification via ion exchange and reversed‐phase chromatography. The LfcinB–hLY fusion peptide demonstrates good antibacterial activity toward both Gram‐positive and Gram‐negative bacteria. This recombination protein with good stability demonstrates a potential use as animal feed additive to partly replace antibiotics.