TL;DR
Local enrichment of acidic residues on the PlGH3 surface could generate a negative electrostatic potential, which enables adaptation to high-salt and alkaline environments, thereby sustaining the enzyme's catalytic activity under such extreme conditions.
This study presents the first characterization of a GH3 β-glucosidase from L. buchneri and reveals a non-classical stabilizing effect of EDTA, offering valuable insights for enzyme engineering and biocatalytic applications.
According to amino acid motifs, AFBGL belongs to family 1 of glycosylhydrolase and 4/7 super family, as the amino acid sequence contained a GH1 specific domain, and is a member of GH1, as the amino acid sequence contained a GH1 specific domain.
BSEG2 is highly thermostable, tolerant of high salt and ionic liquids, and notably resistant to cellobiose inhibition up to 200 mM, suggesting potential to reduce freshwater demand in biomass processing and a strong candidate for simplified, cost-effective enzyme formulations for glucose production from lignocellulosic...
Recombinant WcEG394 efficiently hydrolyzed carboxymethyl cellulose, microcrystalline cellulose, and filter paper, and demonstrated broad substrate specificity toward xylans, pectin, chitin, agarose and agricultural residues such as corn cob and sugarcane bagasse.
High catalytic efficiency in hydrolyzing glycosidic bonds and substantial increases in the yields of bioactive daidzein and genistein are highlighted, highlighting ChaBGL's significant potential for diverse industrial applications, particularly in the nutritional, veterinary, and pharmaceutical sectors.
Overall, this study demonstrates the feasibility of producing a thermostable hemicellulolytic secretome from low-cost agro-industrial residues and identifies Parageobacillus sp.
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