Multistep metabolic engineering of Pichia pastoris for biosynthesis of N‑acetylneuraminic acid.

ABSTRACT: Free or protein-conjugated N-Acetylneuraminic acid (Neu5Ac) is widely distributed in organisms and possesses diverse biological functions, and for example lactoferrin with Neu5Ac-mediated sialylation exhibits significantly enhanced functional activity compared with non-sialylated lactoferrin. Pichia pastoris serves as an excellent host for lactoferrin; however, efficient biosynthesis of Neu5Ac is essential for efficiently expressing lactoferrin with Neu5Ac-mediated sialylation. In this study, P. pastoris was engineered into a high-yield Neu5Ac host for expressing highly active lactoferrin with Neu5Ac modification. Heterologous Neu5Ac biosynthesis genes (gfa1, gna1, yqaB, age, and neuB) were first introduced into a P. pastoris strain in which pfk1 and zwf attenuation combined with pfk2 dele

SUBMITTER: Zhao X 

PROVIDER: S-EPMC12935738 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature