Biochemical Characterization of a Novel Endo-1,3-β-Glucanase from the Scallop Chlamys farreri

• Published in: Marine drugs 2020-09, Vol.18 (9), p.466
• Main Authors: Li, Zhijian, Liu, Weizhi, Lyu, Qianqian
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Cloning, Molecular; endo-1,3-β-glucanases; Glucan Endo-1,3-beta-D-Glucosidase - chemistry; Glucan Endo-1,3-beta-D-Glucosidase - genetics; Glucan Endo-1,3-beta-D-Glucosidase - isolation & purification; Glucan Endo-1,3-beta-D-Glucosidase - metabolism; Glucans - metabolism; Glycosylation; Hydrolysis; laminarin; marine mollusk; Oligosaccharides - metabolism; Pectinidae - enzymology; Pectinidae - genetics; Recombinant Proteins - metabolism; Structure-Activity Relationship; Substrate Specificity; transglycosylation
• ISSN: 1660-3397; 1660-3397
• DOI: 10.3390/md18090466

Endo-1,3-β-glucanases derived from marine mollusks have attracted much attention in recent years because of their unique transglycosylation activity. In this study, a novel endo-1,3-β-glucanase from the scallop , named L , was biochemically characterized. Unlike in earlier studies on marine mollusk endo-1,3-β-glucanases, L was expressed in vitro first. Enzymatic analysis demonstrated that L preferred to hydrolyze laminarihexaose than to hydrolyze laminarin. Furthermore, L was capable of catalyzing transglycosylation reactions with different kinds of glycosyl acceptors. More interestingly, the transglycosylation specificity of L was different from that of other marine mollusk endo-1,3-β-glucanases, although they share a high sequence identity. This study enhanced our understanding of the diverse enzymatic specificities of marine mollusk endo-1,3-β-glucanases, which facilitated development of a unique endo-1,3-β-glucanase tool in the synthesis of novel glycosides.