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Studies on an alkali-thermostable xylanase from Aspergillus fumigatus MA28

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 th...

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Autores principales: Bajaj, Bijender Kumar, Abbass, Massarat
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3339620/
https://www.ncbi.nlm.nih.gov/pubmed/22611527
http://dx.doi.org/10.1007/s13205-011-0020-x
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author Bajaj, Bijender Kumar
Abbass, Massarat
author_facet Bajaj, Bijender Kumar
Abbass, Massarat
author_sort Bajaj, Bijender Kumar
collection PubMed
description 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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spelling pubmed-33396202012-05-16 Studies on an alkali-thermostable xylanase from Aspergillus fumigatus MA28 Bajaj, Bijender Kumar Abbass, Massarat 3 Biotech Original Article 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%). Springer Berlin Heidelberg 2011-08-13 2011-10 /pmc/articles/PMC3339620/ /pubmed/22611527 http://dx.doi.org/10.1007/s13205-011-0020-x Text en © The Author(s) 2011 https://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Original Article
Bajaj, Bijender Kumar
Abbass, Massarat
Studies on an alkali-thermostable xylanase from Aspergillus fumigatus MA28
title Studies on an alkali-thermostable xylanase from Aspergillus fumigatus MA28
title_full Studies on an alkali-thermostable xylanase from Aspergillus fumigatus MA28
title_fullStr Studies on an alkali-thermostable xylanase from Aspergillus fumigatus MA28
title_full_unstemmed Studies on an alkali-thermostable xylanase from Aspergillus fumigatus MA28
title_short Studies on an alkali-thermostable xylanase from Aspergillus fumigatus MA28
title_sort studies on an alkali-thermostable xylanase from aspergillus fumigatus ma28
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3339620/
https://www.ncbi.nlm.nih.gov/pubmed/22611527
http://dx.doi.org/10.1007/s13205-011-0020-x
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