Topic
Xylanase
About: Xylanase is a research topic. Over the lifetime, 7099 publications have been published within this topic receiving 163793 citations.
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TL;DR: The major water-soluble arabinoxylan fraction from rye grain, containing 4-linked β-d -xylopyranosyl residues of which about 43% were substituted solely at O-3 and 7% at both O 2 and O 3 with terminal α- l -arabinofuranosyl units, was hydrolysed to different extents using semi-purified xylanase from Trichoderma reesei as discussed by the authors.
64 citations
TL;DR: The red yeast Rhodotorula mucilaginosa produced an esterase that accumulated in the culture supernatant on induction with triacetin that was specific for substrates bearing an O-acetyl group, but was relatively nonspecific for the rest of the molecule.
Abstract: The red yeast Rhodotorula mucilaginosa produced an esterase that accumulated in the culture supernatant on induction with triacetin. The enzyme was specific for substrates bearing an O-acetyl group, but was relatively nonspecific for the rest of the molecule, which could consist of a phenol, a monosaccharide, a polysaccharide, or an aliphatic alcohol. The esterase was more active against acetylxylan and glucose β-d-pentaacetate than were a number of esterases from plant and animal sources, when activities on 4-nitrophenyl acetate were compared. The enzyme exhibited Michaelis-Menten kinetics and was active over a broad pH range (5.5 to 9.2), with an optimum between pH 8 and 10. In addition, the enzyme retained its activity for 2 h at 55°C. The yeast that produced the enzyme did not produce xylanase and, hence, is of interest for the production of acetylxylan esterase that is free of xylanolytic activity.
64 citations
TL;DR: Substrate-specificity experiments and analysis of the main products released from xylan hydrolysis indicate that both recombinant enzymes act as endo-1, 4-beta-xylanases, but differ in their ability to cleave small xylooligosaccharides.
Abstract: The GenBank accession number for the sequence reported in this paper is AF200304.
The nucleotide sequence of the complete xynA gene, encoding a novel multidomain xylanase XynA of ‘Caldibacillus cellulovorans’, was determined by genomic-walking PCR. The putative XynA comprises an N-terminal domain (D1), recently identified as a xylan-binding domain (XBD), homologous to non-catalytic thermostabilizing domains from other xylanases. D1 is followed by a xylanase catalytic domain (D2) homologous to family 10 glycosyl hydrolases. Downstream of this domain two cellulose-binding domains (CBD), D3 and D4, were found linked via proline-threonine (PT)-rich peptides. Both CBDs showed sequence similarity to family IIIb CBDs. Upstream of xynA an incomplete open reading frame was identified, encoding a putative C-terminal CBD homologous to family IIIb CBDs. Two expression plasmids encoding the N-terminal XBD plus the catalytic domain (XynAd1/2) and the xylanase catalytic domain alone (XynAd2) were constructed and the biochemical properties of the recombinant enzymes compared. The absence of the XBD resulted in a decrease in thermostability of the catalytic domain from 70 °C (XynAd1/2) to 60 °C (XynAd2). Substrate-specificity experiments and analysis of the main products released from xylan hydrolysis indicate that both recombinant enzymes act as endo-1,4-β-xylanases, but differ in their ability to cleave small xylooligosaccharides.
64 citations
TL;DR: An uncommon thermophilic fungus, Melanocarpus albomyces, was isolated from soil and compost by incubating samples in a glucose/sorbose/asparagine liquid medium, followed by enrichment culture in medium containing sugarcane bagasse as carbon source.
Abstract: Summary: An uncommon thermophilic fungus, Melanocarpus albomyces, was isolated from soil and compost by incubating samples in a glucose/sorbose/asparagine liquid medium, followed by enrichment culture in medium containing sugarcane bagasse as carbon source. The culture filtrate protein of the fungus grown in the presence of bagasse or xylose hydrolysed xylan and some other polysaccharides but cellulose was not hydrolysed. High extracellular xylanase (EC 3.2.1.8) activity was produced by cultures grown on xylose or hemicellulosic materials. The enzyme was induced in glucose-grown washed mycelia in response to addition of xylose or xylan but not by alkyl or aryl β-D-xylosides. Cultures produced higher enzyme yields in shaken flasks than in a fermenter. Gel-filtration chromatography of culture filtrate protein showed the presence of two isoenzymes of xylanase, whose relative proportions varied with the carbon source used for growth. The extent of hydrolysis of heteroxylans or the hemicellulosic fraction of bagasse by culture filtrate protein preparations was greater when the cultures had been grown on bagasse rather than xylose as the inducing substrate. The activity of xylanase preparations was increased when an exogenous β-glucosidase was added.
64 citations
TL;DR: In this paper, the response surface methodology and central composite design were used to optimize a biosynthesis medium for the production of xylanases by Streptomyces sp. P12-137 in submerged fermentation culture at pH 5.0, with wheat bran as substrate.
Abstract: Response surface methodology and central composite design were used to optimize a biosynthesis medium for the production of xylanases by Streptomyces sp. P12-137 in submerged fermentation culture at pH 5.0, with wheat bran as substrate. The three variables involved in this research were the wheat bran, potassium nitrate and xylose concentrations. Statistical analysis of the results showed that, in the range studied, xylose and potassium nitrate concentrations had a significant effect on xylanase production. The optimized biosynthesis medium contained (in %, w/v): wheat bran 1.0, KNO3 1.0, xylose 0.5. This medium resulted in a 3-fold increased level of the xylanase (27.77 UA/ml) production compared to the initial level (8.30 UA/ml) after 120 h of fermentation, whereas the value predicted by the quadratic model was 26.45 UA/ml.
64 citations