Hydrophobin HFBI promoting active expression of pediocin PA-1 in Pichia pastoris and extending its application in emulsion
作者单位：The Key Laboratory of Molecular Microbiology and TechnologyMinistry of EducationCollege of Life SciencesNankai University
会议名称：《中国生物化学与分子生物学会第十二届全国会员代表大会暨2...》
会议日期：2018年
学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 07[理学] 08[工学] 0822[工学-轻工技术与工程] 082203[工学-发酵工程]
关 键 词：PA-1 Hydrophobin Fusion protein Antibacterial activity Emulsion
摘 要：Pediocin PA-1,originating from Pediococcus acidilactici,is regarded as a broad-spectrum bacteriocin in lactic acid bacteria.It was reported that PA-1 could highly expressed in Pichia pastoris but without bioactivity,resulting from covalent binding by collagen-like materials presented in the supernatant.In this study,P.pastoris was used as the host for expression of fusion protein PA-1-linker-HFBI(PB),and Ultra-filtration and aqueous two-phase system(ATPs) extraction were employed to purify the recombinant protein PB.Antibacterial activity assays showed the fusion protein PB retained the biological properties of native PA-1,indicated HFBI can overcome the unfunctional expression of PA-1 in P.pastoris.In addition,Water contact angle,oil emulsion antibacterial activity assay indicated PB also retained the biological properties of HFBI.The method of active expression of PA-1 in P.pastoris and the applications of PA-1 in food emulsion and antiseptic explored a novel technology to be used for other bacteriocins with the same feature of pediocin PA-1 molecule.