Expression and characterization of a novel GH128 laminarinase OUC-Bs Lam26 harboring both hydrolyzing and transferring activities  

作　　者：Yueyang Dong Yongyi Quan Hong Jiang Hamed I.Hamouda Zewei Lu Yimiao Chen Chengqiang Li Xiangzhao Mao 

机构地区：[1]State Key Laboratory of Marine Food Processing and Safety Control,College of Food Science and Engineering,Ocean University of China,Qingdao 266404,China [2]Qingdao Key Laboratory of Food Biotechnology,Qingdao 266404,China [3]Key Laboratory of Biological Processing of Aquatic Products,China National Light Industry,Qingdao 266404,China [4]Sanya Ocean Research Institute,Ocean University of China,Sanya 572025,China [5]Processes Design and Development Department,Egyptian Petroleum Research Institute,Cairo 11727,Egypt [6]Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology,Qingdao 266237,China

出　　处：《Food Science and Human Wellness》2025年第1期134-143,共10页食品科学与人类健康(英文)

基　　金：supported by the National Natural Science Foundation of China(32072159);Natural Science Foundation of Hainan Province(322QN338);Young Talent of Lifting Engineering for Science and Technology in Shandong,China(SDAST2021qt18);Qingdao Science and Technology Plan Key Research and Development Project(22-3-3-hygg-28-hy);Fundamental Research Funds for the Central Universities(202262003);Taishan Scholar Project of Shandong Province(tsqn202312099);Support Program for Youth Innovation Technology in Colleges and Universities of Shandong Province(2023KJ041)。

摘　　要：Laminarin oligosaccharides(LOSs)with a specific degree of polymerization prepared through the laminarin degradation via laminarinase present more significant nutritional functions and application values.Human intestinal bacteria are promising potential producers of novel carbohydrate-active enzymes with unique properties.Here,a novel glycoside hydrolase family 128(GH128)laminarinase OUC-BsLam26 from the intestinal bacterium Bacteroides sp.CBA7301 was heterologously expressed and characterized.The recombinant OUC-BsLam26 with a molecular mass of 49.86 kDa exhibits highest activity(6.60 U/mg)at 45℃ and pH 6.0,which shows noticeable temperature and pH stability.The purified OUC-BsLam26 could degrade laminarin via an endo-type mode with the generation of laminaripentaose,laminaritetraose,laminaritriose,and laminaribiose,among them,laminaritetraose is the principal product,which accounts for 45.25% of the total products,which is significantly different from the reported GH128 laminarinases.The minimum recognition substrate of OUC-BsLam26 is laminarihexaose.Furthermore,OUC-BsLam26 also could catalyze the transglycosylation process with the production of some novel glycosides.Altogether,the intestinal bacterium Bacteroides sp.CBA7301 contains laminarinase with unique product composition and OUC-BsLam26 is a hopeful bio-catalyst with the potential to produce laminaritetraose and some novel glycosides.

关 键 词：Laminarinase EXPRESSION Laminarin oligosaccharides Hydrolytic pattern Novel glycosides 

分 类 号：TS201.25[轻工技术与工程—食品科学]