Xylanase

About: Xylanase is a research topic. Over the lifetime, 7099 publications have been published within this topic receiving 163793 citations.

Synthesis and characterization of chimeric proteins based on cellulase and xylanase from an insect gut bacterium.

Abstract: Insects living on wood and plants harbor a large variety of bacterial flora in their guts for degrading biomass. We isolated a Paenibacillus strain, designated ICGEB2008, from the gut of a cotton bollworm on the basis of its ability to secrete a variety of plant-hydrolyzing enzymes. In this study, we cloned, expressed, and characterized two enzymes, β-1,4-endoglucanase (Endo5A) and β-1,4-endoxylanase (Xyl11D), from the ICGEB2008 strain and synthesized recombinant bifunctional enzymes based on Endo5A and Xyl11D. The gene encoding Endo5A was obtained from the genome of the ICGEB2008 strain by shotgun cloning. The gene encoding Xyl11D was obtained using primers for conserved xylanase sequences, which were identified by aligning xylanase sequences in other species of Paenibacillus. Endo5A and Xyl11D were overexpressed in Escherichia coli, and their optimal activities were characterized. Both Endo5A and Xyl11D exhibited maximum specific activity at 50°C and pH 6 to 7. To take advantage of this feature, we constructed four bifunctional chimeric models of Endo5A and Xyl11D by fusing the encoding genes either end to end or through a glycine-serine (GS) linker. We predicted three-dimensional structures of the four models using the I-TASSER server and analyzed their secondary structures using circular dichroism (CD) spectroscopy. The chimeric model Endo5A-GS-Xyl11D, in which a linker separated the two enzymes, yielded the highest C-score on the I-TASSER server, exhibited secondary structure properties closest to the native enzymes, and demonstrated 1.6-fold and 2.3-fold higher enzyme activity than Endo5A and Xyl11D, respectively. This bifunctional enzyme could be effective for hydrolyzing plant biomass owing to its broad substrate range.

Regulation of Expression of Cellulosomes and Noncellulosomal (Hemi)Cellulolytic Enzymes in Clostridium cellulovorans during Growth on Different Carbon Sources

Abstract: Cellulosomes and noncellulosomal (hemi)cellulolytic enzymes are produced by Clostridium cellulovorans to degrade plant cell walls. To understand their synergistic relationship, changes in mRNA and protein expression in cellulosomes and noncellulosomal (hemi)cellulolytic enzymes (hereafter called noncellulosomal enzymes) of cultures grown on cellobiose, cellulose, pectin, xylan, and corn fiber or mixtures thereof were examined. Cellulase expression, favored particularly by the presence of Avicel, was found with all substrates. Comparison of cellulosome and noncellulosomal enzymes showed that expression profiles were strongly affected by the carbon source. High xylanase or pectate lyase expression was observed when C. cellulovorans was grown on xylan or pectin, respectively. Mixed carbon substrates (cellulose-pectin-xylan mixture or corn fiber) induced a wider variety of enzymes than a single carbon source, such as cellobiose, pectin, or xylan. Cellulosomal proteome profiles were more affected by the carbon source than the noncellulosomal enzymes. Transcription and protein analyses revealed that cellulosomes and noncellulosomal enzymes were expressed simultaneously on mixed carbon sources, but their degree of inducibility varied when the substrate was either cellulose or cellobiose. Cellulosomes and noncellulosomal enzymes had synergistic activity on various carbon substrates. These results indicated that expression of plant cell wall-degrading enzymes is highly influenced by the available carbon source and that synergy between cellulosomes and noncellulosomal enzymes contribute to plant cell wall degradation.

Differential and synergistic effects of xylanase and laccase mediator system (LMS) in bleaching of soda and waste pulps.

Abstract: Aims: Investigation of waste pulps and soda pulp bleaching with xylanase (X) and laccase mediator system (LMS) alone and in conjunction (one after the other) (XLMS). Methods and Results: Soda and different grades of waste pulp fibres [used for making three-layered duplex sheets – top layer (TL), protective layer (PL) and bottom layer (BL)] when pretreated with either xylanase (40·0 IU g−1) or LMS (up to 200·0 U g−1) alone and in combination (one after the other) (XLMS) exhibited an increase in release of reducing sugars [up to 881·0% soda pulp; up to 736·6% (TL), up to 215·7% (PL) and up to 198·0% (BL) waste pulp], reduction in kappa number [up to 17·6% soda pulp; up to 14·0% (TL), up to 25·3% (PL) and up to 10·9% (BL), waste pulp], improvement in brightness [up to 20·4% soda pulp; up to 23·6% (TL), up to 8·6% (PL) and up to 5·0% (BL), waste pulp] when compared with the respective controls. The usage of XLMS along with 15% reduced level of hypochlorite at CEHHXLMS/EHHXLMS bleaching stage reduced kappa number [5·5% soda pulp; 11·4% (TL), 7·9% (PL), waste pulp] and improved brightness [1·0% soda pulp; 0·9% (TL), 1·4% (PL) waste pulp] when compared with the controls. Scanning electron microscopic studies revealed development of cracks, flakes, pores and peeling off the fibres in the enzyme-treated pulp samples. These modifications of the fibre surface during enzymatic bleaching in turn indicated the removal of lignin and derived compounds from the fibre cell wall. Conclusions: The work describes synergistic action of xylanase with LMS for bleaching of waste and nonwood pulps for eco-friendly production of paper and thus reveals a new unexploited arena for enzyme-based pulp bleaching. Significance and Impact of the Study: The drastic improvement in pulp properties obtained after xylanase and LMS treatment would improve the competitiveness of enzyme–based, environmentally benign processes over chemicals both economically and environmentally.

Interrelationship of Xylanase Induction and Cellulase Induction of Trichoderma longibrachiatum.

Abstract: Xylose oligomers rapidly induced xylanase activity of Trichoderma longibrachiatum, whereas induction was delayed in the presence of glucose. Cellobiose, cellopentaose, and xylobiose did not induce detectable levels of cellulase activity. However, mixtures of xylobiose with cellobiose or cellopentaose rapidly induced cellulase activity. In addition, mixtures of xylobiose with cellopentaose or cellobiose induced xylanase activity more effectively than xylobiose alone. Both xylanase and cellulase activity were detected after a lag period in the presence of lactose.