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Article Abstract
Unlabelled: 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 -neocarratetrose (N4)-producing -carrageenase OUC-FaKC16A from 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 N4 into -neocarrabiose (N2). The offset of Arg residue in OUC-FaKC16Q may explain this change. Moreover, the high catalytic abilities, the main products, and the degradation modes of OUC-FaKC16A and OUC-FaKC16Q toward furcellaran were also demonstrated. Data suggested OUC-FaKC16A and OUC-FaKC16Q could hydrolyze furcellaran to produce mainly the desulfated oligosaccharides DA-G-(DA-G4S) and DA-G-DA-G4S, respectively. As a result, the spectrum of products of -carrageenase OUC-FaKC16A has been fully expanded in this study, indicating its promising potential for application in the biomanufacturing of carrageenan oligosaccharides with specific structures.
Supplementary Information: The online version contains supplementary material available at 10.1007/s42995-023-00181-2.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10449746 | PMC |
| http://dx.doi.org/10.1007/s42995-023-00181-2 | DOI Listing |
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