Xylanase

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

Purification and properties of xylanase A from alkali-tolerant Bacillus sp. strain BP-23.

Abstract: Xylanase A from the recently isolated Bacillus sp. strain BP-23 was purified to homogeneity. The enzyme shows a molecular mass of 32 kDa and an isoelectric point of 9.3. Optimum temperature and pH for xylanase activity were 50 degrees C and 5.5 respectively. Xylanase A was completely inhibited by N-bromosuccinimide. The main products of birchwood xylan hydrolysis were xylotetraose and xylobiose. The enzyme was shown to facilitate chemical bleaching of pulp, generating savings of 38% in terms of chlorine dioxide consumption. The amino-terminal sequence of xylanase A has a conserved sequence of five amino acids found in xylanases from family F.

Nutrient digestibility and performance responses of growing pigs fed phytase- and xylanase-supplemented wheat-based diets.

Abstract: Three experiments were conducted to evaluate the effect of supplementing phytase and xyla- nase on nutrient digestibility and performance of grow- ing pigs fed wheat-based diets. In Exp. 1, 10 diets were fed to 60 pigs from 20 to 60 kg of BW to determine the effect of combining phytase and xylanase on apparent total tract digestibility (ATTD) of nutrients and growth performance. The 10 diets included a positive control diet (PC; 0.23% available P; 0.60% Ca) and a negative control diet (NC; 0.16% available P; 0.50% Ca) supple- mented with phytase at 0, 250, and 500 fytase units (FTU)/kg and xylanase at 0, 2,000, and 4,000 xylanase units (XU)/kg in a 3 × 3 factorial arrangement. In Exp. 2, 6 ileally cannulated barrows (initial BW = 35.1 kg) were fed 4 wheat-based diets in a 4 × 4 Latin square design, with 2 added columns to determine the effect of combining phytase and xylanase on apparent ileal digestibility (AID) of nutrients. The 4 diets were NC (same as that used in Exp. 1) or NC supplemented with phytase at 500 FTU/kg, xylanase at 4,000 XU/kg, or phytase at 500 FTU/kg plus xylanase at 4,000 XU/kg. In Exp. 3, 36 barrows (initial BW = 55.5 kg) were fed 4 diets based on prepelleted (at 80°C) and crumpled

Thermostable recombinant xylanases from Nonomuraea flexuosa and Thermoascus aurantiacus show distinct properties in the hydrolysis of xylans and pretreated wheat straw

Abstract: In the hydrolysis of lignocellulosic materials, thermostable enzymes decrease the amount of enzyme needed due to higher specific activity and elongate the hydrolysis time due to improved stability. For cost-efficient use of enzymes in large-scale industrial applications, high-level expression of enzymes in recombinant hosts is usually a prerequisite. The main aim of the present study was to compare the biochemical and hydrolytic properties of two thermostable recombinant glycosyl hydrolase families 10 and 11 (GH10 and GH11, respectively) xylanases with respect to their potential application in the hydrolysis of lignocellulosic substrates. The xylanases from Nonomuraea flexuosa (Nf Xyn11A) and from Thermoascus aurantiacus (Ta Xyn10A) were purified by heat treatment and gel permeation chromatography. Ta Xyn10A exhibited higher hydrolytic efficiency than Nf Xyn11A toward birchwood glucuronoxylan, insoluble oat spelt arabinoxylan and hydrothermally pretreated wheat straw, and it produced more reducing sugars. Oligosaccharides from xylobiose to xylopentaose as well as higher degree of polymerization (DP) xylooligosaccharides (XOSs), but not xylose, were released during the initial hydrolysis of xylans by Nf Xyn11A, indicating its potential for the production of XOS. The mode of action of Nf Xyn11A and Ta Xyn10A on glucuronoxylan and arabinoxylan showed typical production patterns of endoxylanases belonging to GH11 and GH10, respectively. Because of its high catalytic activity and good thermostability, T. aurantiacus xylanase shows great potential for applications aimed at total hydrolysis of lignocellulosic materials for platform sugars, whereas N. flexuosa xylanase shows more significant potential for the production of XOSs.

Production of Enzymes Degrading Plant Cell Walls and Fermentation of Cellobiose by Ruminococcus flavefaciens in Batch and Continuous Culture

Abstract: Summary: Production of enzymes degrading plant cell walls was studied using media containing cellobiose or ammonium ions (NH4 +) as limiting nutrients. Carboxymethylcellulase (CM-cellulase), xylanase and pectin lyase were primarily cell-associated during exponential growth in batch culture but accumulated in the supernatant during the stationary phase. Activities of CM-cellulase and xylanase were higher in cellobiose-limited than in NH4 +-limited continuous cultures, were inversely related to the growth rate and became progressively more cell-associated as the growth rate increased. The proportion of fermentation products in cellobiose-limited continuous cultures was dependent on the growth rate and the calculated cell yields per mol ATP (Y ATP) varied between 11·92 and 16·39. Glutamate dehydrogenase, an ammonia-assimilating enzyme, was most active in NH4 +-limited continuous cultures. These results are discussed in relation to the growth and metabolism of Ruminococcus flavefaciens in vivo.