Abstract

Direct conversion of crystalline chitin to N-acetylglucosamine and the related chitooligomers through enzymatic approaches is gaining importance owing to their various biological applications. Here we report the crystalline chitin degradation ability of chitinolytic cocktail produced by the isolate Paenibacillus sp. LS1. Growth studies of the isolate in presence of different chitin substrates revealed preference for β-chitin and colloidal chitin. FE-SEM micrographs showed formation of visible perforations on the crystalline chitin particles by the isolate. Further, zymogram analysis revealed the presence of six potential chitinase isozymes. The enzyme-cocktail produced by the isolate was optimally active at 50 °C in 50 mM sodium acetate, pH-4.0. Time-course hydrolysis of crystalline α- and β-chitin with the Paenibacillus sp. LS1 enzyme-cocktail produced N-acetylglucosamine and N,N'-diacetylchitobiose as the predominant products. Taken together, our results confirm that the Paenibacillus sp. LS1 enzyme-cocktail would have potential application in eco-friendly enzymatic approaches for efficient saccharification of crystalline chitin.

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