Abstract
Xylanases are industrial enzymes with multiple applications in the food, pharmaceuticals, bio-bleaching, and textiles industries. The present study explores a putative novel bacterium Paenibacillus sp. PCH8 shows xylanolytic activity from Himalayan glacial soil. Genome sequencing and analysis revealed multiple genes encoding xylanases, cellulases, and other lignocellulolytic enzymes. The bacterium utilized oat spelt xylan substrate and showed xylanolytic activity in wide pH (4.0 – 12.0) and temperature (4 to 90 ºC). Proteomic analysis revealed 1,4-β-xylanase, arabinan endo-1,5-α-l-arabinosidase, and 11 hypothetical proteins in partially purified protein fraction. Multi-substrate enzymatic activity (IU/mg) was observed for beechwood (21.42), oat spelt xylan (19.8), CMC (5.17), avicel (7.7), and starch (1.62) in protein fraction. The hydrolysis of xylan led to the formation of xylose, xylobiose, xylotriose, and xylotetraose upon analysis by LC-MS. The xylooligosaccharides (XOS) containing hydrolysate enhanced the growth of probiotic microbes, suggesting prebiotic potential. Thus, the study provides a new source of xylanases from Paenibacillus sp. PCH8, with potential applications in lignocellulosic biomass hydrolysis and XOS production.
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