@article{Dong2025, 
author = {Yueyang Dong and Yongyi Quan and Hong Jiang and Hamed I. Hamouda and Zewei Lu and Yimiao Chen and Chengqiang Li and Xiangzhao Mao},
title = {Expression and characterization of a novel GH128 laminarinase OUC-BsLam26 harboring both hydrolyzing and transferring activities},
year = {2025},
journal = {Food Science and Human Wellness},
volume = {14},
number = {1},
pages = {9250008},
keywords = {Laminarinase, Expression, Laminarin oligosaccharides, Hydrolytic pattern, Novel glycosides},
url = {https://www.sciopen.com/article/10.26599/FSHW.2024.9250008},
doi = {10.26599/FSHW.2024.9250008},
abstract = {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.}
}