Article3 Biotech2011
Studies on an alkali-thermostable xylanase from Aspergillus fumigatus MA28.
Article in 3 Biotech, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- EMS-induced mutagenesis of Aspergillus terreus for enhanced xylanase production and subsequent biotransformation of sugarcane bagasse-derived xylose towards xylitol.Archives of microbiology · 2026Article
- Powerful cell wall biomass degradation enzymatic system from saprotrophicCell surface (Amsterdam, Netherlands) · 2024Review
- Screening and Isolation of Xylanolytic Filamentous Fungi from the Gut of Scarabaeidae Dung Beetles and Dung Beetle Larvae.Microorganisms · 2024Article
- Alkaliphilic/Alkali-Tolerant Fungi: Molecular, Biochemical, and Biotechnological Aspects.Journal of fungi (Basel, Switzerland) · 2023Review
- Purification, characterization and partial amino acid sequences of thermo-alkali-stable and mercury ion-tolerant xylanase from Thermomyces dupontii KKU-CLD-E2-3.Scientific reports · 2020Article
- Hot springs of Indian Himalayas: potential sources of microbial diversity and thermostable hydrolytic enzymes.3 Biotech · 2017Article
- Purification, biochemical characterization and structural modelling of alkali-stable β-1,4-xylan xylanohydrolase from Aspergillus fumigatus R1 isolated from soil.BMC biotechnology · 2016Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An alkalitolerant fungus, Aspergillus fumigatus strain MA28 produced significant amounts of cellulase-free xylanase when grown on a variety of agro-wastes. Wheat bran as the sole carbon source supported higher xylanase production (8,450 U/L) than xylan (7,500 U/L). Soybean meal was observed to be the best nitrogen source for xylanase production (9,000 U/L). Optimum medium pH for xylanase production was 8 (9,800 U/L), though, significant quantities of the enzyme was also produced at pH 7 (8,500 U/L), 9 (8,200 U/L) and 10 (4,600 U/L). The xylanase was purified by ammonium sulphate precipitation and carboxymethyl cellulose chromatography, and was found to have a molecular weight of 14.4 kDa with a V(max) of 980 μmol/min/mg of protein and a K(m) of approximately 4.9 mg/mL. The optimum temperature and pH for enzyme activity was 50 °C and pH 8, respectively. However, the enzyme also showed substantial residual activity at 60-70 °C (53-75%) and at alkaline pH 8-9 (56-88%).
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Registered trials
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