Expanding the application range of the κ‑carrageenase OUC-FaKC16A when preparing oligosaccharides from κ-carrageenan and furcellaran.

ABSTRACT: Carrageenan oligosaccharides are important products that have demonstrated numerous bioactivities useful in the food, medicine, and cosmetics industries. However, the specific structure-function relationships of carrageenan oligosaccharides are not clearly described due to the deficiency of high specific carrageenases. Here, a truncated mutant OUC-FaKC16Q based on the reported κ-neocarratetrose (Nκ4)-producing κ-carrageenase OUC-FaKC16A from Flavobacterium algicola was constructed and further studied. After truncating the C-terminal Por_Secre_tail (PorS) domain (responsible for substrate binding), the catalytic efficiency and temperature stability decreased to a certain extent. Surprisingly, this truncation also enabled OUC-FaKC16Q to hydrolyze Nκ4 into <

SUBMITTER: Jiang C 

PROVIDER: S-EPMC10449746 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature