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Evaluation of Ten Wild Nigerian Mushrooms for Amylase and Cellulase Activities
Amylases and cellulases are important enzymes that can be utilized for various biological activities. Ten different wild Nigerian mushrooms (Agaricus blazei, Agaricus sp., Corilopsis occidentalis, Coriolus versicolor, Termitomyces clypeatus, Termitomyces globulus, Pleurotus tuber-regium, Podoscypha...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Korean Society of Mycology
2011
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3385104/ https://www.ncbi.nlm.nih.gov/pubmed/22783085 http://dx.doi.org/10.4489/MYCO.2011.39.2.103 |
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author | Jonathan, Segun Gbolagade Adeoyo, Olusegun Richard |
author_facet | Jonathan, Segun Gbolagade Adeoyo, Olusegun Richard |
author_sort | Jonathan, Segun Gbolagade |
collection | PubMed |
description | Amylases and cellulases are important enzymes that can be utilized for various biological activities. Ten different wild Nigerian mushrooms (Agaricus blazei, Agaricus sp., Corilopsis occidentalis, Coriolus versicolor, Termitomyces clypeatus, Termitomyces globulus, Pleurotus tuber-regium, Podoscypha bolleana, Pogonomyces hydnoides, and Nothopanus hygrophanus) were assayed for production of these secondary metabolites. The results revealed that most of the tested wild fungi demonstrated very good amylase and cellulase activities. With the incorporation of carboxymethyl-cellulose (a carbon source) into the culture medium, Agaricus blazei had the highest amylolytic activity of 0.60 unit/mL (at 25℃, pH 6.8). This was followed in order by P. tuber-regium and Agaricus sp. with 0.42 and 0.39 unit/mL, respectively (p ≤ 0.05). Maltose and sucrose supplementation into the submerged liquid medium made N. hygrophanus and P. hydnoides to exhibit very low amylase activities of 0.09 and 0.11 unit/mL, respectively. Introducing peptone (an organic nitrogen source) into the basal medium enhanced the ability of C. versicolor to produce a cellulase value of 0.74 unit/mL. Other organic nitrogen sources that supported good cellulase activities were yeast extract and urea. Sodium nitrate (inorganic nitrogen source) generally inhibited cellulase production in all mushrooms. The best carbon source was carboxymethyl-cellulose, which promoted very high cellulase activity of 0.67 unit/mL in C. versicolor, which was followed in order by P. tuber-regium, T. chypeatus, and C. occidentalis (p ≤ 0.05). Sucrose was the poorest carbon compound, supporting the lowest values of 0.01, 0.01, and 0.14 unit/mL in P. hydnoides, A. blazei, and Agaricus sp., respectively. |
format | Online Article Text |
id | pubmed-3385104 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The Korean Society of Mycology |
record_format | MEDLINE/PubMed |
spelling | pubmed-33851042012-07-10 Evaluation of Ten Wild Nigerian Mushrooms for Amylase and Cellulase Activities Jonathan, Segun Gbolagade Adeoyo, Olusegun Richard Mycobiology Research Article Amylases and cellulases are important enzymes that can be utilized for various biological activities. Ten different wild Nigerian mushrooms (Agaricus blazei, Agaricus sp., Corilopsis occidentalis, Coriolus versicolor, Termitomyces clypeatus, Termitomyces globulus, Pleurotus tuber-regium, Podoscypha bolleana, Pogonomyces hydnoides, and Nothopanus hygrophanus) were assayed for production of these secondary metabolites. The results revealed that most of the tested wild fungi demonstrated very good amylase and cellulase activities. With the incorporation of carboxymethyl-cellulose (a carbon source) into the culture medium, Agaricus blazei had the highest amylolytic activity of 0.60 unit/mL (at 25℃, pH 6.8). This was followed in order by P. tuber-regium and Agaricus sp. with 0.42 and 0.39 unit/mL, respectively (p ≤ 0.05). Maltose and sucrose supplementation into the submerged liquid medium made N. hygrophanus and P. hydnoides to exhibit very low amylase activities of 0.09 and 0.11 unit/mL, respectively. Introducing peptone (an organic nitrogen source) into the basal medium enhanced the ability of C. versicolor to produce a cellulase value of 0.74 unit/mL. Other organic nitrogen sources that supported good cellulase activities were yeast extract and urea. Sodium nitrate (inorganic nitrogen source) generally inhibited cellulase production in all mushrooms. The best carbon source was carboxymethyl-cellulose, which promoted very high cellulase activity of 0.67 unit/mL in C. versicolor, which was followed in order by P. tuber-regium, T. chypeatus, and C. occidentalis (p ≤ 0.05). Sucrose was the poorest carbon compound, supporting the lowest values of 0.01, 0.01, and 0.14 unit/mL in P. hydnoides, A. blazei, and Agaricus sp., respectively. The Korean Society of Mycology 2011-06 2011-06-16 /pmc/articles/PMC3385104/ /pubmed/22783085 http://dx.doi.org/10.4489/MYCO.2011.39.2.103 Text en © The Korean Society of Mycology http://creativecommons.org/licenses/by-nc/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Jonathan, Segun Gbolagade Adeoyo, Olusegun Richard Evaluation of Ten Wild Nigerian Mushrooms for Amylase and Cellulase Activities |
title | Evaluation of Ten Wild Nigerian Mushrooms for Amylase and Cellulase Activities |
title_full | Evaluation of Ten Wild Nigerian Mushrooms for Amylase and Cellulase Activities |
title_fullStr | Evaluation of Ten Wild Nigerian Mushrooms for Amylase and Cellulase Activities |
title_full_unstemmed | Evaluation of Ten Wild Nigerian Mushrooms for Amylase and Cellulase Activities |
title_short | Evaluation of Ten Wild Nigerian Mushrooms for Amylase and Cellulase Activities |
title_sort | evaluation of ten wild nigerian mushrooms for amylase and cellulase activities |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3385104/ https://www.ncbi.nlm.nih.gov/pubmed/22783085 http://dx.doi.org/10.4489/MYCO.2011.39.2.103 |
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