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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: An extracellular beta-xylosidase from the thermophilic fungus Paecilomyces thermophila J18 was purified 31.9-fold to homogeneity with a recovery yield of 2.27% from the cell-free culture supernatant and the enzyme was stable in the range of pH 6.0-9.0 and at 55 degrees C.

84 citations

Journal ArticleDOI
TL;DR: Substrate competition studies showed that carboxymethylcellulose and xylan appear to compete with methylumbelliferyl cellobioside for the same active site within each domain of celD.
Abstract: A plant polysaccharide hydrolase cDNA, designated celD, was isolated from a cDNA library of the rumen fungus Neocallimastix patriciarum. The enzyme encoded by celD had endoglucanase, cellobiohydrolase and xylanase activities. Deletion analysis revealed that celD cDNA can be truncated to code for three catalytically active domains. Each domain had the same substrate specificity as the enzyme produced by the untruncated celD and also possessed cellulose-binding capacity. Substrate competition studies showed that carboxymethylcellulose and xylan appear to compete with methylumbelliferyl cellobioside for the same active site within each domain. Expression of celD transcript in the rumen fungus was constitutive and was not affected by the presence of cellulose in the culture medium.

84 citations

Journal ArticleDOI
TL;DR: The results suggest that methods that rely on interactions between a dye (Congo red or Gram's iodine) and a polymeric substrate for indirect detection of hydrolysis may require the use of relevant controls and independent confirmation of enzymatic activities.

84 citations

Journal ArticleDOI
TL;DR: An extracellular xylanase produced by a Mexican Aspergillus strain was purified and characterized and showed a higher affinity for 4-O-methyl-d-glucuronoxylan and displayed no activity toward other polysaccharides, including cellulose.
Abstract: An extracellular xylanase produced by a Mexican Aspergillus strain was purified and characterized Aspergillus sp FP-470 was able to grow and produce extracellular xylanases on birchwood xylan, oat spelt xylan, wheat straw, and corncob, with higher production observed on corncob The strain also produced enzymes with cellulase, amylase, and pectinase activities on this substrate A 22-kDa endoxylanase was purified 30-fold Optimum temperature and pH were 60 degrees C and 55, respectively, and isoelectric point was 90 The enzyme has good stability from pH 50 to 100, retaining >80% of its original activity within this range Half-lives of 150 min at 50 degrees C and 65 min at 60 degrees C were found K(m) and activation energy values were 38 mg/mL and 26 kJ/mol, respectively, using birchwood xylan as substrate The enzyme showed a higher affinity for 4-O-methyl-D-glucuronoxylan with a K(m) of 19 mg/mL The enzyme displayed no activity toward other polysaccharides, including cellulose Baking trials were conducted using the crude filtrate and purified enzyme Addition of both preparations improved bread volume However, addition of purified endoxylanase caused a 30% increase in volume over the crude extract

84 citations

Journal ArticleDOI
TL;DR: The results showed that the enzyme activities of amylase, CMCase and xylanase were increased by Tween 80 and rhamnolipid, which, however, had a negative effect on the protease production.

84 citations


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