Bioinformatics analysis of extracellular glycosyl hydrolases mined from the genome of Halophilic Meridianimaribacter sp. CL38.
TL;DR
Insights are provided into putative glycosyl hydrolase candidates for efficient lignocellulosic waste pre-treatment and significant predicted halophilic and thermostable properties are revealed, suggesting these putative enzymes may endure industrial conditions.
Abstract
Biological pre-treatment of lignocellulosic waste is crucial for efficient fermentation in second-generation biofuel production. Halophilic bacteria produce glycosyl hydrolases with enhanced stability for industrial application. This study aimed to characterise putative glycosyl hydrolases (cellulases and hemicellulases) encoded in the genome of the halophilic bacterium Meridianimaribacter sp. CL38 using bioinformatic approaches, in order to address the scarcity of structural information for this genus. Four putative glycosyl hydrolases (GH9, GH3, GH144 and GH16) were analysed, focusing on their functional domains and structural properties. Phylogenetic analysis indicated a close relationship with other members of the Flavobacteriaceae family. Structural analyses revealed significant predicted halophilic and thermostable properties, suggesting these putative enzymes may endure industrial conditions. This study provides insights into putative glycosyl hydrolase candidates for efficient lignocellulosic waste pre-treatment.