Heterologous expression of a novel linoleic acid isomerase BBI, and effect of fusion tags on its performance.

ABSTRACT: Functional proteins with the ability to isomerise free linoleic acid (LA) to conjugated linoleic acid (CLA) are termed linoleic acid isomerases (LAI). BBI is a novel LAI from Bifidobacterium breve with unique advantages in the production of a single CLA isomer; however, its complex membrane-bound form hampers over-expression of the protein in its natural host. To overcome this challenge, heterologous expression of BBI in Pichia pastoris was studied. Further, to investigate the influence of His-tags on the heterologous expression of BBI, three P. pastoris recombinant strains carrying either a C-terminal His-tag, an N-terminal His-tag, or none were constructed. The expression of recombinant proteins was analysed by dot and western blotting, and the enzyme activity was de

SUBMITTER: Mei Y 

PROVIDER: S-EPMC9636412 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature