EXPRESSION OF RECOMBINANT BOVINE LACTOFERRIN IN PICHIA PASTORIS AND ANTIMICROBIAL ACTIVITY OF ITS HYDROLYSATE
Published: 18 Sep 2021
Abstract: The bovine lactoferrin (bLf) has been well-characterized as a multifunctional glycoprotein, which belongs to the transferrin family exhibiting multifunctional immunoregulation of antibacterial, antioxidant, anti-tumour and antiviral activities. In this study, the structure of pPICZαA::bLfopt was transformed into Pichia pastoris KM71H for heterologous production of lactoferrin under the control of the AOX1 promoter. The antimicrobial activity of the full rbLF and the pepsin-hydrolyzed rbLf against some pathogens were tested. The results showed that the optimized bLf gene encoding bovine lactoferrin was successfully transferred and expressed in Pichia pastoris KM71H. The expression of recombinant bovine lactoferrin was detected by SDS PAGE analysis and confirmed by Western blot. The recombinant bovine lactoferrin digested by Pepsin showed a higher percentage of inhibition than the whole molecular for three strains Candida albicans ATCC 10231, Staphylococcus aureus ATCC 6538P and Escherichia coli ATCC 11303 with the highest proportion of 50.71%; 56.76% and 21.11%, respectively. The successful expression of the rbLfopt genes in Pichia pastoris KM71H opens a prospect for developing research in natural antimicrobial agents.
Keywords: bovine lactoferrin, expression, pichia pastoris km71h, antibacterial activity, hydrolyzed rblf
Cite this article: Thuy T.T. Trinh, Trang T. Nguyen, Thuy T. Nguyen, Phong Q. Truong. EXPRESSION OF RECOMBINANT BOVINE LACTOFERRIN IN PICHIA PASTORIS AND ANTIMICROBIAL ACTIVITY OF ITS HYDROLYSATE. Journal of International Scientific Publications: Agriculture & Food 9, 274-283 (2021). https://www.scientific-publications.net/en/article/1002166/
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