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Production and Catalytic Properties of Amylases from Lichtheimia ramosa and Thermoascus aurantiacus by Solid-State Fermentation
The present study compared the production and the catalytic properties of amylolytic enzymes obtained from the fungi Lichtheimia ramosa (mesophilic) and Thermoascus aurantiacus (thermophilic). The highest amylase production in both fungi was observed in wheat bran supplemented with nutrient solution...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4931097/ https://www.ncbi.nlm.nih.gov/pubmed/27413773 http://dx.doi.org/10.1155/2016/7323875 |
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author | de Oliveira, Ana Paula Aguero Silvestre, Maria Alice Garcia, Nayara Fernanda Lisboa Alves-Prado, Heloíza Ferreira Rodrigues, André da Paz, Marcelo Fossa Fonseca, Gustavo Graciano Leite, Rodrigo Simões Ribeiro |
author_facet | de Oliveira, Ana Paula Aguero Silvestre, Maria Alice Garcia, Nayara Fernanda Lisboa Alves-Prado, Heloíza Ferreira Rodrigues, André da Paz, Marcelo Fossa Fonseca, Gustavo Graciano Leite, Rodrigo Simões Ribeiro |
author_sort | de Oliveira, Ana Paula Aguero |
collection | PubMed |
description | The present study compared the production and the catalytic properties of amylolytic enzymes obtained from the fungi Lichtheimia ramosa (mesophilic) and Thermoascus aurantiacus (thermophilic). The highest amylase production in both fungi was observed in wheat bran supplemented with nutrient solution (pH 4.0) after 96 hours of cultivation, reaching 417.2 U/g of dry substrate (or 41.72 U/mL) and 144.5 U/g of dry substrate (or 14.45 U/mL) for L. ramosa and T. aurantiacus, respectively. The enzymes showed higher catalytic activity at pH 6.0 at 60°C. The amylases produced by L. ramosa and T. aurantiacus were stable between pH 3.5–10.5 and pH 4.5–9.5, respectively. The amylase of L. ramosa was stable at 55°C after 1 hour of incubation, whereas that of T. aurantiacus maintained 60% of its original activity under the same conditions. Both enzymes were active in the presence of ethanol. The enzymes hydrolyzed starch from different sources, with the best results obtained with corn starch. The enzymatic complex produced by L. ramosa showed dextrinizing and saccharifying potential. The enzymatic extract produced by the fungus T. aurantiacus presented only saccharifying potential, releasing glucose monomers as the main hydrolysis product. |
format | Online Article Text |
id | pubmed-4931097 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-49310972016-07-13 Production and Catalytic Properties of Amylases from Lichtheimia ramosa and Thermoascus aurantiacus by Solid-State Fermentation de Oliveira, Ana Paula Aguero Silvestre, Maria Alice Garcia, Nayara Fernanda Lisboa Alves-Prado, Heloíza Ferreira Rodrigues, André da Paz, Marcelo Fossa Fonseca, Gustavo Graciano Leite, Rodrigo Simões Ribeiro ScientificWorldJournal Research Article The present study compared the production and the catalytic properties of amylolytic enzymes obtained from the fungi Lichtheimia ramosa (mesophilic) and Thermoascus aurantiacus (thermophilic). The highest amylase production in both fungi was observed in wheat bran supplemented with nutrient solution (pH 4.0) after 96 hours of cultivation, reaching 417.2 U/g of dry substrate (or 41.72 U/mL) and 144.5 U/g of dry substrate (or 14.45 U/mL) for L. ramosa and T. aurantiacus, respectively. The enzymes showed higher catalytic activity at pH 6.0 at 60°C. The amylases produced by L. ramosa and T. aurantiacus were stable between pH 3.5–10.5 and pH 4.5–9.5, respectively. The amylase of L. ramosa was stable at 55°C after 1 hour of incubation, whereas that of T. aurantiacus maintained 60% of its original activity under the same conditions. Both enzymes were active in the presence of ethanol. The enzymes hydrolyzed starch from different sources, with the best results obtained with corn starch. The enzymatic complex produced by L. ramosa showed dextrinizing and saccharifying potential. The enzymatic extract produced by the fungus T. aurantiacus presented only saccharifying potential, releasing glucose monomers as the main hydrolysis product. Hindawi Publishing Corporation 2016 2016-06-20 /pmc/articles/PMC4931097/ /pubmed/27413773 http://dx.doi.org/10.1155/2016/7323875 Text en Copyright © 2016 Ana Paula Aguero de Oliveira et al. https://creativecommons.org/licenses/by/4.0/ 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 de Oliveira, Ana Paula Aguero Silvestre, Maria Alice Garcia, Nayara Fernanda Lisboa Alves-Prado, Heloíza Ferreira Rodrigues, André da Paz, Marcelo Fossa Fonseca, Gustavo Graciano Leite, Rodrigo Simões Ribeiro Production and Catalytic Properties of Amylases from Lichtheimia ramosa and Thermoascus aurantiacus by Solid-State Fermentation |
title | Production and Catalytic Properties of Amylases from Lichtheimia ramosa and Thermoascus aurantiacus by Solid-State Fermentation |
title_full | Production and Catalytic Properties of Amylases from Lichtheimia ramosa and Thermoascus aurantiacus by Solid-State Fermentation |
title_fullStr | Production and Catalytic Properties of Amylases from Lichtheimia ramosa and Thermoascus aurantiacus by Solid-State Fermentation |
title_full_unstemmed | Production and Catalytic Properties of Amylases from Lichtheimia ramosa and Thermoascus aurantiacus by Solid-State Fermentation |
title_short | Production and Catalytic Properties of Amylases from Lichtheimia ramosa and Thermoascus aurantiacus by Solid-State Fermentation |
title_sort | production and catalytic properties of amylases from lichtheimia ramosa and thermoascus aurantiacus by solid-state fermentation |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4931097/ https://www.ncbi.nlm.nih.gov/pubmed/27413773 http://dx.doi.org/10.1155/2016/7323875 |
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