Improvement of the Stability and Activity of an LPMO Through Rational Disulfide Bonds Design.

ABSTRACT: Lytic polysaccharide monooxygenases (LPMOs) oxidatively break down the glycosidic bonds of crystalline polysaccharides, significantly improving the saccharification efficiency of recalcitrant biomass, and have broad application prospects in industry. To meet the needs of industrial applications, enzyme engineering is needed to improve the catalytic performance of LPMOs such as enzyme activity and stability. In this study, we engineered the chitin-active CjLPMO10A from Cellvibrio japonicus through a rational disulfide bonds design. Compared with the wild-type, the variant M1 (N78C/H116C) exhibited a 3-fold increase in half-life at 60°C, a 3.5°C higher T ₅₀ ¹⁵ , and a 7°C rise in the apparent Tm. Furthermore, the resistance of M1 to ch

SUBMITTER: Zhou X 

PROVIDER: S-EPMC8801915 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature