ArticleFolia microbiologica2004
Purification and characterization of xylanases from Aspergillus giganteus.
Article in Folia microbiologica, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 45 citations in OpenAlex.
- High-Molecular-Weight Xylanase from B. pumilus US570 Strain: Purification, Characterization and Application in Banana and Orange Peels Hydrolysis and Breadmaking.Applied biochemistry and biotechnology · 2024Article
- Purification, Identification, and Characterization of a Glycoside Hydrolase Family 11-Xylanase with High Activity from Aspergillus niger VTCC 017.Molecular biotechnology · 2022Article
- An ascomycota coculture in batch bioreactor is better than polycultures for cellulase production.Folia microbiologica · 2018Article
- Gene Expression and Molecular Characterization of a Xylanase from Chicken Cecum Metagenome.International journal of microbiology · 2017Article
- Purification of Endoxylanase fromIranian journal of biotechnology · 2017Article
- Production of fungal amylases using cheap, readily available agriresidues, for potential application in textile industry.BioMed research international · 2014Article
- Gene cloning, expression and characterization of a novel xylanase from the marine bacterium, Glaciecola mesophila KMM241.Marine drugs · 2013Article
- Molecular cloning and heterologous expression of an acid stable xylanase gene from Alternaria sp. HB186.World journal of microbiology & biotechnology · 2012Article
- Xyn11A, a multidomain multicatalytic enzyme from Pseudobutyrivibrio xylanivorans Mz5T.Folia microbiologica · 2006Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A strain of Aspergillus giganteus cultivated in a medium with xylan produced two xylanases (xylanase I and II) which were purified to homogeneity. Their molar mass, estimated by SDS-PAGE, were 21 and 24 kDa, respectively. Both enzymes are glycoproteins with 50 degrees C temperature optimum; optimum pH was 6.0-6.5 for xylanase I and 6.0 for xylanase II. At 50 degrees C xylanase I exhibited higher thermostability than xylanase II. Hg2+, Cu2+ and SDS were strong inhibitors, 1,4-dithiothreitol stimulated the reaction of both enzymes. Both xylanases are xylan-specific; kinetic parameters indicated higher efficiency in the hydrolysis of oat spelts xylan. In hydrolysis of this substrate, xylotriose, xylotetraose and larger xylooligosaccharides were released and hence the enzymes were classified as endoxylanases.
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Registered trials
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