Abstract
β-glucan rich cereals such as barley and oats serve as a raw material in breweries and also used as an animal feed. Digestion of β-glucan is often a major hurdle, thus providing exogenous enzyme β-glucanase serves as an option. The present study takes an effort for the expression and over production of β-glucanase genes from Streptomyces sp in E. coli. The exo-β-1,4-glucanase and endo-β-1,3-glucanase encoding genes were isolated and codon optimized and significant-high expression levels were obtained in E. coli strain. The expressed enzymes showed broad pH stability, good thermostability, and better affinity towards the barley β-glucan substrate. The study implies that heterologous expression with codon optimization strategy enhances the production of Streptomyces origin beta-glucanase enzymes with prominent physio-chemical properties for efficient beta-glucan degradation.
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