Expanding the application range of theκ‑carrageenase OUC‑FaKC16A when preparing oligosaccharides fromκ‑carrageenan and furcellaran

作     者：Chengcheng Jiang Francesco Secundo Xiangzhao Mao 

作者机构：College of Food Science and EngineeringOcean University of ChinaQingdao 266003China Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and TechnologyQingdao 266237China Key Laboratory for Biological Processing of Aquatic ProductsChina National Light IndustryQingdao 266237China Istituto di Scienze e Tecnologie Chimiche“Giulio Natta”Consiglio Nazionale delle RicercheVia Mario Bianco 920131 MilanItaly 

出 版 物：《Marine Life Science & Technology》 (海洋生命科学与技术（英文）)

年 卷 期：2023年第5卷第3期

页      面：387-399页

核心收录：

学科分类：0710[理学-生物学] 070703[理学-海洋生物学] 07[理学] 0707[理学-海洋科学] 

基　　金：This work was supported by the National Key Research and Development Program of China(2022YFF1100202) Natural Science Foundation of Shandong Province(ZR2020JQ15) Taishan Scholar Project of Shandong Province(tsqn201812020) Fundamental Research Funds for the Central Universities(201941002) 

主　　题：Carrageenan oligosaccharides κ-Carrageenase Expression Degradation mode Desulfated oligosaccharides 

摘      要：Carrageenan oligosaccharides are important products that have demonstrated numerous bioactivities useful in the food,medicine,and cosmetics ***,the specifc structure–function relationships of carrageenan oligosaccharides are not clearly described due to the defciency of high specifc ***,a truncated mutant OUC-FaKC16Q based on the reportedκ-neocarratetrose(Nκ4)-producingκ-carrageenase OUC-FaKC16A from Flavobacterium algicola was constructed and further *** truncating the C-terminal Por_Secre_tail(PorS)domain(responsible for substrate binding),the catalytic efciency and temperature stability decreased to a certain ***,this truncation also enabled OUC-FaKC16Q to hydrolyze Nκ4 intoκ-neocarrabiose(Nκ2).The ofset of Arg265 residue in OUC-FaKC16Q may explain this ***,the high catalytic abilities,the main products,and the degradation modes of OUC-FaKC16A and OUC-FaKC16Q toward furcellaran were also *** suggested OUC-FaKC16A and OUC-FaKC16Q could hydrolyze furcellaran to produce mainly the desulfated oligosaccharides DA-G-(DA-G4S)2 and DA-G-DA-G4S,*** a result,the spectrum of products ofκ-carrageenase OUC-FaKC16A has been fully expanded in this study,indicating its promising potential for application in the biomanufacturing of carrageenan oligosaccharides with specifc structures.