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 intestin...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.展开更多
基金supported by the National Natural Science Foundation of China(32072159)Natural Science Foundation of Hainan Province(322QN338)+4 种基金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)。
文摘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.
