Title: Genomic and structural analysis to decipher xylanolytic potential in bacteria
Abstract:
The rumen is a highly specialized anaerobic ecosystem in which diverse microbial populations produce enzymes required for the degradation of plant cell wall polysaccharides. Xylan, the major hemicellulosic component of plant biomass, represents a key substrate in this process, and its efficient utilization depends on the coordinated activity of xylanolytic enzymes. Among rumen bacteria, Prevotella ruminicola plays an important role in hemicellulose breakdown and fermentation. In the present study, whole-genome sequencing and annotation of Prevotella ruminicola strain KHP1 were performed to investigate its genetic potential for xylan degradation, with particular emphasis on xylanase-associated enzymes. The draft genome assembly was analyzed for functional features and carbohydrate-active enzymes (CAZymes). CAZyme annotation using the dbCAN2 pipeline identified a total of 103 putative CAZyme genes, with glycoside hydrolases representing the largest group. Notably, several members of the glycoside hydrolase families GH10 and GH43 were identified. GH10 enzymes typically function as endo-1,4-β-xylanases that cleave the xylan backbone, while GH43 enzymes act as accessory debranching enzymes that remove side-chain substitutions. The presence of both families suggests a coordinated xylanolytic system capable of efficient xylan hydrolysis. Substrate prediction analysis further supported the involvement of these enzymes in xylan degradation, along with activity toward other plant-derived polysaccharides. Overall, the genome-based analysis indicates that P. ruminicola strain KHP1 harbors a well-developed xylan-degrading enzyme repertoire, highlighting its potential as a promising source of xylanases for industrial and biotechnological use.
Keywords: Rumen microbiota; Prevotella ruminicola; xylan degradation; xylanase; CAZymes; whole-genome sequencing; GH10 and GH43
