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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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TL;DR: In this paper, a new xylanase activity (XynII) was isolated from liquid state cultures of Acrophialophora nainiana containing birchwood xylan as carbon source.
56 citations
TL;DR: Two distinct xylanase genes were subcloned in pUC13 from non-homologous restriction fragments of Ruminococcus flavefaciens 17 DNA originally isolated in lambda EMBL3 and showed similar pH optima for hydrolysis of oat spelt xylan and had little or no activity against carboxymethylcellulose.
Abstract: Summary: Two distinct xylanase genes (designated xynA and xynB) were subcloned in pUC13 from non-homologous restriction fragments of Ruminococcus flavefaciens 17 DNA originally isolated in olD EMBL3. The products of the two genes showed similar pH optima for hydrolysis of oat spelt xylan (around 5·5) and had little or no activity against carboxymethylcellulose. Trace activities against p-nitrophenyl (pNP) cellobioside and pNP-xyloside were detected in clones containing xynA, but not in one harbouring xynB. The xylanase associated with clones carrying xynA produced mainly xylobiose and xylose from xylan and did not give hydrolysis of xylobiose, while that encoded by xynB produced mainly xylobiose and higher xylo-oligosaccharides from xylan. There was evidence of increased expression, at the RNA level, of these two genes, and of another cloned region encoding multiple activities including xylanase, in R. flavefaciens 17 grown with xylan, as compared with cellobiose, as energy source. Total cell-associated xylanase and β-xylosidase activities, and supernatant xylanase activity, were shown to be similarly induced in xylan-grown R. flavefaciens, 17.
56 citations
TL;DR: The resultant xylanase system was pure by the criteria of sodium dodecyl sulfate polyacrylamide electrophoresis, had a very high specific activity, was virtually free of filter paper activity, and had a ratio of contaminatingfilter paper activity of 2 × 10−6.
Abstract: A process has been developed for the bulk purification of cellulase-free β-1,4-D-xylanase from the fungus Trichoderma harzianum E58 The process involved the primary step of ultrafiltering the culture filtrate via a 10,000-molecular-weight cut-off membrane to separate the cellulase (retentate) and xylanase (permeate) fractions The cellulase component was concentrated by 40- to 60-fold, resulting in an enzyme complex that could effectively hydrolyze high concentrations of cellulose and xylan to glucose and xylose The xylanase was concentrated and solvent exchanged by adsorption to a cationic exchanger, SP-ZetaPrep 250, followed by elution with a pH change in the buffer to give a purified and concentrated xylanase complex dissolved in a low-salt buffer The resultant xylanase system was pure by the criteria of sodium dodecyl sulfate polyacrylamide electrophoresis, had a very high specific activity of 2400 IU/mg protein, was virtually free of filter paper activity, and had a ratio of contaminating filter paper activity of 2 × 10−6 (0009% endoglucanase activity) Approximately 33 g protein, which contained in excess of 7 × 106 IU xylanase activity, was obtained from 17 L original culture filtrate The process scheme was designed to facilitate scale-up to an industrial level of production
56 citations
TL;DR: The xylanase pretreatment was found to strongly boost the effects of the laccase–HBT system by facilitating their access to HexA without affecting the lignin content.
56 citations
TL;DR: In this article, the authors proposed a novel application of spent mushroom compost (SMC) as substrate for cultivation of fungi in solid state fermentation (SSF) in order to obtain the enzymes cellulase, xylanase, amylase and β-glucosidase.
56 citations