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Production of Oxidative and Hydrolytic Enzymes by Coprinus cinereus (Schaeff.) Gray from Sisal Wastes Supplemented with Cow Dung Manure
The activity of oxidative and hydrolytic enzymes of the edible and medicinal white rot fungi Coprinus cinereus (Schaeff.) Gray mushroom was observed during mycelia growth and fruiting body development in solid substrate fermentation using sisal waste fractions amended with cow dung manure as supplem...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2015
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4668298/ https://www.ncbi.nlm.nih.gov/pubmed/26664748 http://dx.doi.org/10.1155/2015/650543 |
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author | Raymond, Prosper Mshandete, Anthony Manoni Kajumulo Kivaisi, Amelia |
author_facet | Raymond, Prosper Mshandete, Anthony Manoni Kajumulo Kivaisi, Amelia |
author_sort | Raymond, Prosper |
collection | PubMed |
description | The activity of oxidative and hydrolytic enzymes of the edible and medicinal white rot fungi Coprinus cinereus (Schaeff.) Gray mushroom was observed during mycelia growth and fruiting body development in solid substrate fermentation using sisal waste fractions amended with cow dung manure as supplement. Laccase had the highest titre value among the five detected enzymes. Its activity was higher during mycelia growth compared to fruiting phase, with 10% supplemented substrate formulation unmixed sisal leaf decortication residues [abbreviated SL : SB (100 : 0)] displaying the highest activity of 39.45 ± 12.05 Ug(−1). Lignin peroxidase (LiP) exhibited a characteristic wave-like pattern with the highest peaks found either during full mycelia colonization or soon after first flush harvest; the highest activity of 1.93 ± 0.62 Ug(−1) was observed on unsupplemented SL : SB (100 : 0) substrate formulation during mycelia colonization. For hydrolytic enzymes, the highest carboxymethyl cellulase (CMCase) activity of 2.03 ± 0.70 Ug(−1) was observed on 20% supplemented SL : SB (0 : 100) after first flush; that of pectinase (1.90 ± 0.32 Ug(−1)) was revealed after third flush on 10% supplemented SL : SB (0 : 100) substrate formulation while 10% supplemented SL : SB (25 : 75) exhibited the highest xylanase activity (1.23 ± 0.12 Ug(−1)) after first flush. These findings show that the activities of both oxidative and hydrolytic enzymes were regulated in line with developmental phase of growth of Coprinus cinereus. |
format | Online Article Text |
id | pubmed-4668298 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-46682982015-12-10 Production of Oxidative and Hydrolytic Enzymes by Coprinus cinereus (Schaeff.) Gray from Sisal Wastes Supplemented with Cow Dung Manure Raymond, Prosper Mshandete, Anthony Manoni Kajumulo Kivaisi, Amelia Biotechnol Res Int Research Article The activity of oxidative and hydrolytic enzymes of the edible and medicinal white rot fungi Coprinus cinereus (Schaeff.) Gray mushroom was observed during mycelia growth and fruiting body development in solid substrate fermentation using sisal waste fractions amended with cow dung manure as supplement. Laccase had the highest titre value among the five detected enzymes. Its activity was higher during mycelia growth compared to fruiting phase, with 10% supplemented substrate formulation unmixed sisal leaf decortication residues [abbreviated SL : SB (100 : 0)] displaying the highest activity of 39.45 ± 12.05 Ug(−1). Lignin peroxidase (LiP) exhibited a characteristic wave-like pattern with the highest peaks found either during full mycelia colonization or soon after first flush harvest; the highest activity of 1.93 ± 0.62 Ug(−1) was observed on unsupplemented SL : SB (100 : 0) substrate formulation during mycelia colonization. For hydrolytic enzymes, the highest carboxymethyl cellulase (CMCase) activity of 2.03 ± 0.70 Ug(−1) was observed on 20% supplemented SL : SB (0 : 100) after first flush; that of pectinase (1.90 ± 0.32 Ug(−1)) was revealed after third flush on 10% supplemented SL : SB (0 : 100) substrate formulation while 10% supplemented SL : SB (25 : 75) exhibited the highest xylanase activity (1.23 ± 0.12 Ug(−1)) after first flush. These findings show that the activities of both oxidative and hydrolytic enzymes were regulated in line with developmental phase of growth of Coprinus cinereus. Hindawi Publishing Corporation 2015 2015-11-19 /pmc/articles/PMC4668298/ /pubmed/26664748 http://dx.doi.org/10.1155/2015/650543 Text en Copyright © 2015 Prosper Raymond et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Raymond, Prosper Mshandete, Anthony Manoni Kajumulo Kivaisi, Amelia Production of Oxidative and Hydrolytic Enzymes by Coprinus cinereus (Schaeff.) Gray from Sisal Wastes Supplemented with Cow Dung Manure |
title | Production of Oxidative and Hydrolytic Enzymes by Coprinus cinereus (Schaeff.) Gray from Sisal Wastes Supplemented with Cow Dung Manure |
title_full | Production of Oxidative and Hydrolytic Enzymes by Coprinus cinereus (Schaeff.) Gray from Sisal Wastes Supplemented with Cow Dung Manure |
title_fullStr | Production of Oxidative and Hydrolytic Enzymes by Coprinus cinereus (Schaeff.) Gray from Sisal Wastes Supplemented with Cow Dung Manure |
title_full_unstemmed | Production of Oxidative and Hydrolytic Enzymes by Coprinus cinereus (Schaeff.) Gray from Sisal Wastes Supplemented with Cow Dung Manure |
title_short | Production of Oxidative and Hydrolytic Enzymes by Coprinus cinereus (Schaeff.) Gray from Sisal Wastes Supplemented with Cow Dung Manure |
title_sort | production of oxidative and hydrolytic enzymes by coprinus cinereus (schaeff.) gray from sisal wastes supplemented with cow dung manure |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4668298/ https://www.ncbi.nlm.nih.gov/pubmed/26664748 http://dx.doi.org/10.1155/2015/650543 |
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