ArticleApplied biochemistry and biotechnology2026
Identification and Biochemical Characterization of a Novel β-1, 3-glucanase for Efficient Preparation of Laminarin Oligosaccharides.
Article in Applied biochemistry and biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Endo-β-1, 3-glucanase, also called laminarinase, is a key enzyme tool for laminarin biomass biorefinery and pretreatment in industry by hydrolyzing the laminarin polysaccharide into oligosaccharides. Cel2C, a novel kind of endo-β-1, 3-glucanase, was identified and characterized in this study. The name of Cel2C originates from the genus abbreviation of its source strain, Cellulophaga lytica (Cel), combined with an internal sequence identifier (2 C). It consisted of three domains formed by 507 amino acids, namely the N-terminal helix domain, the uncharacterized region and the TIM-like catalytic domain. Cel2C exhibited degrading activities to laminarin, β-glucan and sodium carboxymethyl cellulose (CMC-Na). Notably, it exhibited maximal activity (1.062 × 10
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