Optimization of cellulase production by Penicillium sp.
The production of cellulolytic enzymes (β-exoglucanase, β-endoglucanase and β-glucosidase) by Penicillium sp. on three different media in liquid shake culture conditions was compared. The organism exhibited relatively highest activity of endoglucanase among three enzymes measured at 7-day interval d...
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| Format: | Online |
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Springer Berlin Heidelberg
2016
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4978645/ |
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pubmed-4978645 |
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pubmed-49786452016-08-10 Optimization of cellulase production by Penicillium sp. Prasanna, H. N. Ramanjaneyulu, G. Rajasekhar Reddy, B. Original Article The production of cellulolytic enzymes (β-exoglucanase, β-endoglucanase and β-glucosidase) by Penicillium sp. on three different media in liquid shake culture conditions was compared. The organism exhibited relatively highest activity of endoglucanase among three enzymes measured at 7-day interval during the course of its growth on Czapek-Dox medium supplemented with 0.5 % (w/v) cellulose. Cellulose at 0.5 %, lactose at 0.5 %, sawdust at 0.5 %, yeast extract at 0.2 % as a nitrogen source, pH 5.0 and 30 °C temperature were found to be optimal for growth and cellulase production by Penicillium sp. Yields of Fpase, CMCase and β-glucosidase, attained on optimized medium with Penicillium sp. were 8.7, 25 and 9.52 U/ml, respectively with increment of 9.2, 5.9 and 43.8-folds over titers of the respective enzyme on unoptimised medium. Cellulase of the fungal culture with the ratio of β-glucosidase to Fpase greater than one will hold potential for biotechnological applications. Springer Berlin Heidelberg 2016-08-09 2016-12 /pmc/articles/PMC4978645/ /pubmed/28330234 http://dx.doi.org/10.1007/s13205-016-0483-x Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Prasanna, H. N. Ramanjaneyulu, G. Rajasekhar Reddy, B. |
| spellingShingle |
Prasanna, H. N. Ramanjaneyulu, G. Rajasekhar Reddy, B. Optimization of cellulase production by Penicillium sp. |
| author_facet |
Prasanna, H. N. Ramanjaneyulu, G. Rajasekhar Reddy, B. |
| author_sort |
Prasanna, H. N. |
| title |
Optimization of cellulase production by Penicillium sp. |
| title_short |
Optimization of cellulase production by Penicillium sp. |
| title_full |
Optimization of cellulase production by Penicillium sp. |
| title_fullStr |
Optimization of cellulase production by Penicillium sp. |
| title_full_unstemmed |
Optimization of cellulase production by Penicillium sp. |
| title_sort |
optimization of cellulase production by penicillium sp. |
| description |
The production of cellulolytic enzymes (β-exoglucanase, β-endoglucanase and β-glucosidase) by Penicillium sp. on three different media in liquid shake culture conditions was compared. The organism exhibited relatively highest activity of endoglucanase among three enzymes measured at 7-day interval during the course of its growth on Czapek-Dox medium supplemented with 0.5 % (w/v) cellulose. Cellulose at 0.5 %, lactose at 0.5 %, sawdust at 0.5 %, yeast extract at 0.2 % as a nitrogen source, pH 5.0 and 30 °C temperature were found to be optimal for growth and cellulase production by Penicillium sp. Yields of Fpase, CMCase and β-glucosidase, attained on optimized medium with Penicillium sp. were 8.7, 25 and 9.52 U/ml, respectively with increment of 9.2, 5.9 and 43.8-folds over titers of the respective enzyme on unoptimised medium. Cellulase of the fungal culture with the ratio of β-glucosidase to Fpase greater than one will hold potential for biotechnological applications. |
| publisher |
Springer Berlin Heidelberg |
| publishDate |
2016 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4978645/ |
| _version_ |
1613624340821049344 |