Xylanase

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

The recombinant xylanase B of Thermotoga maritima is highly xylan specific and produces exclusively xylobiose from xylans, a unique character for industrial applications

Abstract: The xynB of a hyperthermophilic Eubacterium, Thermotoga maritima MSB8, coding xylanase B (XynB) was previously expressed in E. coli and the recombinant protein was characterized using the synthetic substrates [J. Biosci. Bioeng. 92 (2001) 423]. In this study, the same xylanase B was purified to homogeneity with a recovery yield of about 43% using heat treatment followed by the Ni-NTA affinity chromatography. The specificity of XynB towards different natural substrates was evaluated. XynB was highly specific towards xylans tested but exhibited low activities towards lichenan (19%), gellan gum (7.3%), laminarin (3.4%) and carboxymethylcellulose (CMC, 1.4%). The apparent Km values of birchwood xylan and soluble oat-spelt xylan was 0.11 and 0.079 mg/ml, respectively. The XynB hydrolyzed xylooligosaccharides to yield predominantly xylobiose (X2) and a small amount of xylose (X1), suggesting that XynB was possibly an endo-acting xylanase. Analysis of the products from birchwood xylan degradation confirmed that the enzyme was an endo-xylanase with xylobiose and xylose as the main degradation products. HPLC results showed that hydrolyzed products of birchwood xylan by XynB yielded up to 66% of the total reaction product as xylobiose. These results clearly indicated that xylobiose could be mass-produced efficiently by the recombinant hyperthermostable XynB of T. maritima. Additionally, conversion of xylobiose (50 mM) to xylose was observed, while xylotriose (X3) and xylotetraose (X4) were detected in small amounts, indicating that the enzyme converted xylobiose to xylose based on the transglycosylation reaction. The increased binding ability of XynB to Avicel and/or insoluble xylan was also observed indicating the possibilities of roles of surface-aromatic amino acid residues for such action. However, further investigations are required to prove this speculation.

Functional characterization of a novel xylanase from a corn strain of Erwinia chrysanthemi.

Abstract: A β-1,4-xylan hydrolase (xylanase A) produced by Erwinia chrysanthemi D1 isolated from corn was analyzed with respect to its secondary structure and enzymatic function. The pH and temperature optima for the enzyme were found to be pH 6.0 and 35°C, with a secondary structure under those conditions that consists of approximately 10 to 15% α-helices. The enzyme was still active at temperatures higher than 40°C and at pHs of up to 9.0. The loss of enzymatic activity at temperatures above 45°C was accompanied by significant loss of secondary structure. The enzyme was most active on xylan substrates with low ratios of xylose to 4-O-methyl-d-glucuronic acid and appears to require two 4-O-methyl-d-glucuronic acid residues for substrate recognition and/or cleavage of a β-1,4-xylosidic bond. The enzyme hydrolyzed sweetgum xylan, generating products with a 4-O-methyl-glucuronic acid-substituted xylose residue one position from the nonreducing terminus of the oligoxyloside product. No internal cleavages of the xylan backbone between substituted xylose residues were observed, giving the enzyme a unique mode of action in the hydrolysis compared to all other xylanases that have been described. Given the size of the oligoxyloside products generated by the enzyme during depolymerization of xylan substrates, the function of the enzyme may be to render substrate available for other depolymerizing enzymes instead of producing oligoxylosides for cellular metabolism and may serve to produce elicitors during the initiation of the infectious process.

Fungal xylanase production under solid state and submerged fermentation conditions

Abstract: Seventy fungal strains were isolated from soils collected from different parts of southern Kerala, India. The strains were screened for xylanase production using Czapek’s agar medium. On the basis of clearing zones formed, 34 fungal strains were selected and identified. Solid state and submerged fermentation were done to identify strains that could produce maximum amount of xylanase, as well as to identify those strains that could produce cellulase-free xylanase under these conditions. All strains produced cellulase along with xylanase in solid state fermentation, while 70% of the strains produced cellulase-free xylanase during submerged fermentation. Key words: Xylanase, Czapek’s agar, solid state fermentation, submerged fermentation

Xylanase supplementation to a wheat-based diet alleviated the intestinal mucosal barrier impairment of broiler chickens challenged by Clostridium perfringens

Abstract: The present study was carried out to evaluate the protective effects of xylanase on the intestinal mucosal barrier in broiler chickens challenged with Clostridium perfringens in a 21-day experiment. A total of 336 1-day-old male broiler chicks (Ross 308) were assigned to four treatment groups. A 2×2 factorial arrangement of treatments was used in a randomized complete block design to study the effects of enzyme addition (with or without xylanase 5500 U/kg wheat-based diet), pathogen challenge (with or without C. perfringens challenge), and their interactions. Most C. perfringens-challenged birds had a congested mucosa and focal haemorrhagic lesions in the jejunum. Xylanase addition tended to reduce (P=0.09) the intestinal lesion score in the challenged birds. C. perfringens challenge resulted in decreased villus height/crypt depth ratio in the jejunum and ileum (P<0.05). Xylanase supplementation significantly increased this ratio in the jejunum (P<0.05) and also had the tendency to decrease crypt depth (P=0.065) and increase this ratio in the ileum (P=0.087). Xylanase addition significantly decreased the plasma endotoxin levels of the birds challenged with C. perfringens (P<0.05). Occludin mRNA expression in the jejunum and ileum was significantly decreased by C. perfringens challenge (P<0.05), but xylanase addition significantly increased its expression in the ileum. Xylanase supplementation also significantly increased MUC2 mRNA expression in the ileum (P<0.05). C. perfringens challenge resulted in a significant increase in apoptotic index in all three intestinal segments (P<0.05), but xylanase supplementation obviously decreased apoptotic index in the ileum (P<0.05). In conclusion, xylanase supplementation could alleviate the impairment of intestinal mucosal barrier induced by C. perfringens challenge.