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Catalytic Properties of Amylolytic Enzymes Produced by Gongronella butleri Using Agroindustrial Residues on Solid-State Fermentation
Amylases catalyze the hydrolysis of starch, a vegetable polysaccharide abundant in nature. These enzymes can be utilized in the production of syrups, alcohol, detergent, pharmaceutical products, and animal feed formulations. The aim of this study was to optimize the production of amylases by the fil...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Hindawi
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5742443/ https://www.ncbi.nlm.nih.gov/pubmed/29376074 http://dx.doi.org/10.1155/2017/7507523 |
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author | Cavalheiro, Gabriéla Finoto Sanguine, Isadora Stranieri Santos, Flávia Regina da Silva da Costa, Ana Carolina Fernandes, Matheus da Paz, Marcelo Fossa Fonseca, Gustavo Graciano Leite, Rodrigo Simões Ribeiro |
author_facet | Cavalheiro, Gabriéla Finoto Sanguine, Isadora Stranieri Santos, Flávia Regina da Silva da Costa, Ana Carolina Fernandes, Matheus da Paz, Marcelo Fossa Fonseca, Gustavo Graciano Leite, Rodrigo Simões Ribeiro |
author_sort | Cavalheiro, Gabriéla Finoto |
collection | PubMed |
description | Amylases catalyze the hydrolysis of starch, a vegetable polysaccharide abundant in nature. These enzymes can be utilized in the production of syrups, alcohol, detergent, pharmaceutical products, and animal feed formulations. The aim of this study was to optimize the production of amylases by the filamentous fungus Gongronella butleri by solid-state fermentation and to evaluate the catalytic properties of the obtained enzymatic extract. The highest amylase production, 63.25 U g(−1) (or 6.32 U mL(−1)), was obtained by culturing the fungus in wheat bran with 55% of initial moisture, cultivated for 96 h at 25°C. The enzyme presented optimum activity at pH 5.0 and 55°C. The amylase produced was stable in a wide pH range (3.5–9.5) and maintained its catalytic activity for 1 h at 40°C. Furthermore, the enzymatic extract hydrolyzed starches from different vegetable sources, presenting predominant dextrinizing activity for all substrates evaluated. However, the presence of glucose was observed in a higher concentration during hydrolysis of corn starch, indicating the synergistic action of endo- and exoamylases, which enables the application of this enzymatic extract to produce syrups from different starch sources. |
format | Online Article Text |
id | pubmed-5742443 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Hindawi |
record_format | MEDLINE/PubMed |
spelling | pubmed-57424432018-01-28 Catalytic Properties of Amylolytic Enzymes Produced by Gongronella butleri Using Agroindustrial Residues on Solid-State Fermentation Cavalheiro, Gabriéla Finoto Sanguine, Isadora Stranieri Santos, Flávia Regina da Silva da Costa, Ana Carolina Fernandes, Matheus da Paz, Marcelo Fossa Fonseca, Gustavo Graciano Leite, Rodrigo Simões Ribeiro Biomed Res Int Research Article Amylases catalyze the hydrolysis of starch, a vegetable polysaccharide abundant in nature. These enzymes can be utilized in the production of syrups, alcohol, detergent, pharmaceutical products, and animal feed formulations. The aim of this study was to optimize the production of amylases by the filamentous fungus Gongronella butleri by solid-state fermentation and to evaluate the catalytic properties of the obtained enzymatic extract. The highest amylase production, 63.25 U g(−1) (or 6.32 U mL(−1)), was obtained by culturing the fungus in wheat bran with 55% of initial moisture, cultivated for 96 h at 25°C. The enzyme presented optimum activity at pH 5.0 and 55°C. The amylase produced was stable in a wide pH range (3.5–9.5) and maintained its catalytic activity for 1 h at 40°C. Furthermore, the enzymatic extract hydrolyzed starches from different vegetable sources, presenting predominant dextrinizing activity for all substrates evaluated. However, the presence of glucose was observed in a higher concentration during hydrolysis of corn starch, indicating the synergistic action of endo- and exoamylases, which enables the application of this enzymatic extract to produce syrups from different starch sources. Hindawi 2017 2017-12-10 /pmc/articles/PMC5742443/ /pubmed/29376074 http://dx.doi.org/10.1155/2017/7507523 Text en Copyright © 2017 Gabriéla Finoto Cavalheiro 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 Cavalheiro, Gabriéla Finoto Sanguine, Isadora Stranieri Santos, Flávia Regina da Silva da Costa, Ana Carolina Fernandes, Matheus da Paz, Marcelo Fossa Fonseca, Gustavo Graciano Leite, Rodrigo Simões Ribeiro Catalytic Properties of Amylolytic Enzymes Produced by Gongronella butleri Using Agroindustrial Residues on Solid-State Fermentation |
title | Catalytic Properties of Amylolytic Enzymes Produced by Gongronella butleri Using Agroindustrial Residues on Solid-State Fermentation |
title_full | Catalytic Properties of Amylolytic Enzymes Produced by Gongronella butleri Using Agroindustrial Residues on Solid-State Fermentation |
title_fullStr | Catalytic Properties of Amylolytic Enzymes Produced by Gongronella butleri Using Agroindustrial Residues on Solid-State Fermentation |
title_full_unstemmed | Catalytic Properties of Amylolytic Enzymes Produced by Gongronella butleri Using Agroindustrial Residues on Solid-State Fermentation |
title_short | Catalytic Properties of Amylolytic Enzymes Produced by Gongronella butleri Using Agroindustrial Residues on Solid-State Fermentation |
title_sort | catalytic properties of amylolytic enzymes produced by gongronella butleri using agroindustrial residues on solid-state fermentation |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5742443/ https://www.ncbi.nlm.nih.gov/pubmed/29376074 http://dx.doi.org/10.1155/2017/7507523 |
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