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Alkalistable endo-β-1,4-xylanase production from a newly isolated alkalitolerant Penicillium sp. SS1 using agro-residues

Thermostable and alkalitolerant xylanases have got intense research focus due to their vast applications in various industries including pulp and paper, food, feed, textile, biofuel, etc. In the present investigation, a Penicillum sp. SS1 isolated from degrading woody material was found to produce m...

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Autores principales: Bajaj, Bijender Kumar, Sharma, Mukul, Sharma, Sunny
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3339607/
https://www.ncbi.nlm.nih.gov/pubmed/22582149
http://dx.doi.org/10.1007/s13205-011-0009-5
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author Bajaj, Bijender Kumar
Sharma, Mukul
Sharma, Sunny
author_facet Bajaj, Bijender Kumar
Sharma, Mukul
Sharma, Sunny
author_sort Bajaj, Bijender Kumar
collection PubMed
description Thermostable and alkalitolerant xylanases have got intense research focus due to their vast applications in various industries including pulp and paper, food, feed, textile, biofuel, etc. In the present investigation, a Penicillum sp. SS1 isolated from degrading woody material was found to produce moderately thermoactive and alkalistable endo-β-1,4-xylanase (xylanase). Maximum xylanase production was observed after fourth day of fermentation (43.84 IU/ml). The organism produced substantial quantities of xylanase using agricultural residues like wheat bran (20.6 IU/ml), rice bran (21.8 IU/ml) and sawdust (10.7 IU/ml) as carbon sources. The enzyme preparation was totally free of filter paper activity (FPase) and possessed negligible carboxymethyl cellulase (CMCase) activity; this could be an important feature of enzyme if the intended application of enzyme is in pulp and paper industries. Among nitrogen sources examined, yeast extract supported maximum xylanase production (45.74 IU/ml), and was followed by soybean meal (22.2 IU/ml) and ammonium sulphate (20 IU/ml). Maximum xylanase production was observed at initial medium pH 9 (25.6 IU/ml); however, at pH 8 and 10 also significantly high enzyme titre was observed (24 and 21.2 IU/ml, respectively). Thus, Penicillium sp. SS1 displayed capability of growing and producing xylanase at high alkaline pH (8–10). Maximum xylanase activity was reported at 50 °C, however, significantly high activity was observed at 60 °C (65.4%), however, at 70–80 °C activity was lost considerably. At 50–60 °C the enzyme retained very high activity up to 30–60 min (91–100%), however, prolonged incubation (90 min) caused considerable activity reduction (residual activity 63–68%).
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spelling pubmed-33396072012-05-09 Alkalistable endo-β-1,4-xylanase production from a newly isolated alkalitolerant Penicillium sp. SS1 using agro-residues Bajaj, Bijender Kumar Sharma, Mukul Sharma, Sunny 3 Biotech Original Article Thermostable and alkalitolerant xylanases have got intense research focus due to their vast applications in various industries including pulp and paper, food, feed, textile, biofuel, etc. In the present investigation, a Penicillum sp. SS1 isolated from degrading woody material was found to produce moderately thermoactive and alkalistable endo-β-1,4-xylanase (xylanase). Maximum xylanase production was observed after fourth day of fermentation (43.84 IU/ml). The organism produced substantial quantities of xylanase using agricultural residues like wheat bran (20.6 IU/ml), rice bran (21.8 IU/ml) and sawdust (10.7 IU/ml) as carbon sources. The enzyme preparation was totally free of filter paper activity (FPase) and possessed negligible carboxymethyl cellulase (CMCase) activity; this could be an important feature of enzyme if the intended application of enzyme is in pulp and paper industries. Among nitrogen sources examined, yeast extract supported maximum xylanase production (45.74 IU/ml), and was followed by soybean meal (22.2 IU/ml) and ammonium sulphate (20 IU/ml). Maximum xylanase production was observed at initial medium pH 9 (25.6 IU/ml); however, at pH 8 and 10 also significantly high enzyme titre was observed (24 and 21.2 IU/ml, respectively). Thus, Penicillium sp. SS1 displayed capability of growing and producing xylanase at high alkaline pH (8–10). Maximum xylanase activity was reported at 50 °C, however, significantly high activity was observed at 60 °C (65.4%), however, at 70–80 °C activity was lost considerably. At 50–60 °C the enzyme retained very high activity up to 30–60 min (91–100%), however, prolonged incubation (90 min) caused considerable activity reduction (residual activity 63–68%). Springer Berlin Heidelberg 2011-06-07 2011-09 /pmc/articles/PMC3339607/ /pubmed/22582149 http://dx.doi.org/10.1007/s13205-011-0009-5 Text en © The Author(s) 2011 https://creativecommons.org/licenses/by/4.0/ This article is published under license to BioMed Central Ltd. Open Access 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
Sharma, Mukul
Sharma, Sunny
Alkalistable endo-β-1,4-xylanase production from a newly isolated alkalitolerant Penicillium sp. SS1 using agro-residues
title Alkalistable endo-β-1,4-xylanase production from a newly isolated alkalitolerant Penicillium sp. SS1 using agro-residues
title_full Alkalistable endo-β-1,4-xylanase production from a newly isolated alkalitolerant Penicillium sp. SS1 using agro-residues
title_fullStr Alkalistable endo-β-1,4-xylanase production from a newly isolated alkalitolerant Penicillium sp. SS1 using agro-residues
title_full_unstemmed Alkalistable endo-β-1,4-xylanase production from a newly isolated alkalitolerant Penicillium sp. SS1 using agro-residues
title_short Alkalistable endo-β-1,4-xylanase production from a newly isolated alkalitolerant Penicillium sp. SS1 using agro-residues
title_sort alkalistable endo-β-1,4-xylanase production from a newly isolated alkalitolerant penicillium sp. ss1 using agro-residues
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3339607/
https://www.ncbi.nlm.nih.gov/pubmed/22582149
http://dx.doi.org/10.1007/s13205-011-0009-5
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