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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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Journal ArticleDOI
TL;DR: Phylogenetic analyses of 16S rRNA and glycosyl hydrolase family 48 gene sequences revealed that two xylan-utilizing isolates were related to a Clostridium clariflavum strain and represent a distinct novel branch within the GH48 family.
Abstract: Nine thermophilic cellulolytic clostridial isolates and four other noncellulolytic bacterial isolates were isolated from self-heated biocompost via preliminary enrichment culture on microcrystalline cellulose. All cellulolytic isolates grew vigorously on cellulose, with the formation of either ethanol and acetate or acetate and formate as principal fermentation products as well as lactate and glycerol as minor products. In addition, two out of nine cellulolytic strains were able to utilize xylan and pretreated wood with roughly the same efficiency as for cellulose. The major products of xylan fermentation were acetate and formate, with minor contributions of lactate and ethanol. Phylogenetic analyses of 16S rRNA and glycosyl hydrolase family 48 (GH48) gene sequences revealed that two xylan-utilizing isolates were related to a Clostridium clariflavum strain and represent a distinct novel branch within the GH48 family. Both isolates possessed high cellulase and xylanase activity induced independently by either cellulose or xylan. Enzymatic activity decayed after growth cessation, with more-rapid disappearance of cellulase activity than of xylanase activity. A mixture of xylan and cellulose was utilized simultaneously, with a significant synergistic effect observed as a reduction of lag phase in cellulose degradation.

114 citations

Book ChapterDOI
01 Feb 2012
TL;DR: Bioethanol can be produced from several different biomass feedstocks: sucrose rich feedstocks, starchy materials (e.g. corn grain), and lignocellulosic biomass, which is promising especially in countries with limited lands availability.
Abstract: Bioethanol can be produced from several different biomass feedstocks: sucrose rich feedstocks (e.g. sugar-cane), starchy materials (e.g. corn grain), and lignocellulosic biomass. This last category, including biomass such as corn stover and wheat straw, woody residues from forest thinning and paper, is promising especially in those countries with limited lands availability. In fact, residues are often widely available and do not compete with food production in terms of land destination. The process converting the biomass biopolymers to fermentable sugars is called hydrolysis. There are two major categories of methods employed. The first and older method uses acids as catalysts, while the second uses enzymes called cellulases. Feedstock pretreatment has been recognized as a necessary upstream process to remove lignin and enhance the porosity of the lignocellulosic materials prior to the enzymatic process (Zhu & Pan, 2010; Kumar et al., 2009). Cellulases are proteins that have been conventionally divided into three major groups: endoglucanase, which attacks low cristallinity regions in the cellulose fibers by endoaction, creating free chain-ends; exoglucanases or cellobiohydrolases which hydrolyze the 1, 4glycocidyl linkages to form cellobiose; and β-glucosidase which converts cellooligosaccharides and disaccharide cellobiose into glucose residues. In addition to the three major groups of cellulose enzymes, there are also a number of other enzymes that attack hemicelluloses, such as glucoronide, acetylesterase, xylanase, β-xylosidase, galactomannase and glucomannase. These enzymes work together synergistically to attack cellulose and hemicellulose. Cellulases are produced by various bacteria and fungi that can have cellulolytic mechanisms significantly different. The use of enzymes in the hydrolysis of cellulose is more effective than the use of inorganic catalysts, because enzymes are highly specific and can work at mild process conditions. In spite of these advantages, the use of enzymes in industrial processes is still limited by

113 citations

Journal ArticleDOI
TL;DR: Both of the oxidative enzymes were found to soften the bread crumb and increase the volume of breads, and the best results were achieved in combination with xylanase.
Abstract: Cross-linking enzymes generate covalent bonds in and between food biopolymers. These enzymes are interesting tools for tailoring dough and bread structures, as the characteristics of the biopolymers significantly determine the viscoelastic and fracture properties of dough and bread. In this study, the influence of oxidative cross-linking enzymes, tyrosinase from the filamentous fungus Trichoderma reesei and laccase from the white rot fungus Trametes hirsuta, on dough and bread were examined. Oxidation of low molecular weight phenolic model compounds of flour, cross-linking of gluten proteins, dough rheology, and bread making were characterized during or after the enzymatic treatments. In the dough and bread experiments, laccase and tyrosinase were also studied in combination with xylanase. Of the model compounds tyrosine, p-coumaric acid, caffeic acid, ferulic acid, and Gly-Leu-Tyr tripeptide, tyrosinase oxidized all except ferulic acid. Laccase was able to oxidize each of the studied compounds. The pheno...

113 citations

Journal ArticleDOI
TL;DR: An extracellular xylanase produced by a cellulase-negative mutant strain of Streptomyces lividans 1326 was purified to homogeneity, indicating that it is a beta-1,4-endoxylanase (EC 3.2.8), and showed no activity towards CM-cellulose and p-nitrophenyl beta-D-xyloside.
Abstract: An extracellular xylanase produced by a cellulase-negative mutant strain of Streptomyces lividans 1326 was purified to homogeneity. The purified enzyme has an apparent Mr of 43,000 and pI of 5.2. The pH and temperature optima for the activity were 6.0 and 60 degrees C respectively, and the Km and Vmax. values, determined with a soluble oat spelts xylan, were 0.78 mg/ml and 0.85 mmol/min per mg of enzyme. The xylanase showed no activity towards CM-cellulose and p-nitrophenyl beta-D-xyloside. The enzyme degraded xylan, producing mainly xylobiose, a mixture of xylo-oligosaccharides and a small amount of xylose as end products. Its pattern of action on beta-1,4-D-xylan indicates that it is a beta-1,4-endoxylanase (EC 3.2.1.8).

112 citations

Journal ArticleDOI
TL;DR: Although xylanase was produced efficiently on cellulose as well as on xylan as the carbon source, significant production of cellulose was observed only on the cellulose-based medium and best production was at lower pH (4.0 minimum).
Abstract: Trichoderma reesei VTT-D-86271 (Rut C-30) was cultivatedon media based on cellulose and xylan as the main carbon source in fermentors with different pH minimum controls. Production of xylanase was favoured by a rather high pH minimum control between 6.0 and 7.0 on both cellulose- and xylan-based media. Although xylanase was produced efficiently on cellulose as well as on xylan as the carbon source, significant production of cellulose was observed only on the cellulose-based medium and best production was at lower pH (4.0 minimum). Production of xylanase at pH 7.0 was shown to be dependent on the nature of the xylan in the cultivation medium but was independent of other organic components. Best production of xylanase was observed on insoluble, unsubstituted beech xylan at pH 7.0. Similar results were obtained in laboratory and pilot (200-l) fermentors. Downstream processing of the xylanase-rich, low-cellulose culture filtrate presented no technical problems despite apparent autolysis of the fungus at the high pH. Enzyme produced in the 200-l pilot fermentor was shown to be suitable for use in enzyme-aided bleaching of kraft pulp. Due to the high xylanase/cellulase ratio of enzyme activities in the culture filtrate, pretreatment for removal of cellulase activity prior to pulp bleaching was unnecessary.

112 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023199
2022463
2021254
2020289
2019278
2018303