Premium
Characterisation of a novel laminarinase from Microbulbifer sp. ALW1 and the antioxidant activity of its hydrolysates
Author(s) -
Hu Qingsong,
Yin Xiaoqian,
Li Hebin,
Wang Xinghua,
Jiang Zedong,
Li Lijun,
Ni Hui,
Li Qingbiao,
Zhu Yanbing
Publication year - 2021
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.15041
Subject(s) - laminarin , biochemistry , pichia pastoris , chemistry , hydrolysate , bacteria , recombinant dna , hydrolysis , biology , microbiology and biotechnology , genetics , gene
Laminarin and its derived oligosaccharides have diverse bioactivities. The β‐1,3‐glucanase in marine bacteria can be employed as a tool to digest laminarin in the cell wall of brown algae. Here, we cloned, expressed and characterised a β‐1,3‐glucanase (laminarinase), MaLamNA, from the previously characterised marine bacterium Microbulbifer sp. ALW1, phylogenetically distinct from the glycoside hydrolase families of characterised laminarinases. The recombinant laminarinase was heterologously expressed and purified from Pichia pastoris GS115 cells with a molecular mass of 57.3 kDa. MaLamNA exerted its hydrolytic activity specifically against laminarin, with the highest activity at 45 °C and pH 4.5–5.5, respectively, and demonstrated high stability against extreme acidic and alkaline pH exposure. The addition of reducing agent dithiothreitol could significantly enhance the activity of MaLamNA. The hydrolytic products of laminarin by MaLamNA exhibited more effective antioxidant activities than the undigested laminarin. These characteristics of MaLamNA provide clues to its industrial application for laminarin bioresource development.