Abstract
Beta-glucanases have prominent applications in the brewing industry as well as the feed enzyme industry. Streptomyces origin beta-glucanases have more demand due to the broad substrate specificity, high catalytic activity, and stability in wide ranges of pH and temperatures. Many industrially valuable beta-glucanase are identified from novel actinomycetes strains. One of the strategies for the identification of novel glucanohydrolase includes the prediction of the enzymatic function of the uncharacterized gene sequence using in silico approaches. The gene sequence and corresponding protein structure of a particular enzyme contain all the specificity of the enzyme. The theoretical overview of predicted proteins and their coding genes provides a basic concept of the protein domain architecture that is likely to regulate their function, stability and their interaction with substrates. The in silico study of structure–function relationships exclusively reveals the absolute potential of beta-glucanase enzymes. The insights provided by in silico tools on protein structure and function can be channelized for increased enzyme production and stability towards industrial applications.
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Edison, L.K., Nandu, T.G., Pradeep, N.S. (2022). Structural Characterization of Beta-Glucanase from Actinobacteria. In: Pradeep, N., Edison, L.K. (eds) Microbial Beta Glucanases. Interdisciplinary Biotechnological Advances. Springer, Singapore. https://doi.org/10.1007/978-981-19-6466-4_9
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