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Enzymatic Biotransformation of Pomegranate Ellagitannins: Initial Approach to Reaction Conditions
BACKGROUND: Ellagitannase (Ellagitannin acyl hydrolase) is an inducible enzyme with great potential use in food industry since allows the ellagic acid release from ellagitannins. OBJECTIVE: In this work, ellagitannase was produced by the fungus Aspergillus niger GH1 in solid state fermentation using...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Institute of Genetic Engineering and Biotechnology
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7856397/ https://www.ncbi.nlm.nih.gov/pubmed/33542933 http://dx.doi.org/10.30498/IJB.2020.137202.2305 |
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author | Buenrostro-Figueroa, Juan Mireles, Marcela Ascacio-Valdés, J.A. Aguilera-Carbo, Antonio Sepúlveda, Leonardo Contreras-Esquivel, Juan Rodríguez-Herrera, Raúl N. Aguilar, C. |
author_facet | Buenrostro-Figueroa, Juan Mireles, Marcela Ascacio-Valdés, J.A. Aguilera-Carbo, Antonio Sepúlveda, Leonardo Contreras-Esquivel, Juan Rodríguez-Herrera, Raúl N. Aguilar, C. |
author_sort | Buenrostro-Figueroa, Juan |
collection | PubMed |
description | BACKGROUND: Ellagitannase (Ellagitannin acyl hydrolase) is an inducible enzyme with great potential use in food industry since allows the ellagic acid release from ellagitannins. OBJECTIVE: In this work, ellagitannase was produced by the fungus Aspergillus niger GH1 in solid state fermentation using polyurethane foam as solid support and pomegranate husk ellagitannins as sole carbon source and ellagitannase inducer and an initial approach to the enzymatic reaction conditions was reached. MATERIALS AND METHODS: Ellagitannase was produced by Aspergillus niger GH1 in solid state fermentation and the ideal reaction conditions for ellagitannase activity based on ellagic acid quantification as ellagitannins biotransformation product by high performance liquid chromatographic are reported. RESULTS: The enzyme ideal reaction conditions were substrate concentration of 1 mg.mL(-1), 60 °C and pH 5.0, during 10 min of reaction. The kinetic enzyme constants (V(max) = 30.34 mM.mL(-1).min(-1) and K(m) = 1.48 x 10(3) mM) using punicalagin assubstrate were determined. CONCLUSION: The assay was completed in a short time and may find application in future studies of ellagic acid production. |
format | Online Article Text |
id | pubmed-7856397 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | National Institute of Genetic Engineering and Biotechnology |
record_format | MEDLINE/PubMed |
spelling | pubmed-78563972021-02-03 Enzymatic Biotransformation of Pomegranate Ellagitannins: Initial Approach to Reaction Conditions Buenrostro-Figueroa, Juan Mireles, Marcela Ascacio-Valdés, J.A. Aguilera-Carbo, Antonio Sepúlveda, Leonardo Contreras-Esquivel, Juan Rodríguez-Herrera, Raúl N. Aguilar, C. Iran J Biotechnol Research Article BACKGROUND: Ellagitannase (Ellagitannin acyl hydrolase) is an inducible enzyme with great potential use in food industry since allows the ellagic acid release from ellagitannins. OBJECTIVE: In this work, ellagitannase was produced by the fungus Aspergillus niger GH1 in solid state fermentation using polyurethane foam as solid support and pomegranate husk ellagitannins as sole carbon source and ellagitannase inducer and an initial approach to the enzymatic reaction conditions was reached. MATERIALS AND METHODS: Ellagitannase was produced by Aspergillus niger GH1 in solid state fermentation and the ideal reaction conditions for ellagitannase activity based on ellagic acid quantification as ellagitannins biotransformation product by high performance liquid chromatographic are reported. RESULTS: The enzyme ideal reaction conditions were substrate concentration of 1 mg.mL(-1), 60 °C and pH 5.0, during 10 min of reaction. The kinetic enzyme constants (V(max) = 30.34 mM.mL(-1).min(-1) and K(m) = 1.48 x 10(3) mM) using punicalagin assubstrate were determined. CONCLUSION: The assay was completed in a short time and may find application in future studies of ellagic acid production. National Institute of Genetic Engineering and Biotechnology 2020-04-01 /pmc/articles/PMC7856397/ /pubmed/33542933 http://dx.doi.org/10.30498/IJB.2020.137202.2305 Text en Copyright: © 2020 The Author(s); Published by Iranian Journal of Biotechnology http://creativecommons.org/licenses/by-nc/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-Share Alike 4.0 Unported, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 Unported License, ( http://creativecommons.org/licenses/by-nc/4.0/ ) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Buenrostro-Figueroa, Juan Mireles, Marcela Ascacio-Valdés, J.A. Aguilera-Carbo, Antonio Sepúlveda, Leonardo Contreras-Esquivel, Juan Rodríguez-Herrera, Raúl N. Aguilar, C. Enzymatic Biotransformation of Pomegranate Ellagitannins: Initial Approach to Reaction Conditions |
title | Enzymatic Biotransformation of Pomegranate Ellagitannins: Initial Approach to Reaction Conditions |
title_full | Enzymatic Biotransformation of Pomegranate Ellagitannins: Initial Approach to Reaction Conditions |
title_fullStr | Enzymatic Biotransformation of Pomegranate Ellagitannins: Initial Approach to Reaction Conditions |
title_full_unstemmed | Enzymatic Biotransformation of Pomegranate Ellagitannins: Initial Approach to Reaction Conditions |
title_short | Enzymatic Biotransformation of Pomegranate Ellagitannins: Initial Approach to Reaction Conditions |
title_sort | enzymatic biotransformation of pomegranate ellagitannins: initial approach to reaction conditions |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7856397/ https://www.ncbi.nlm.nih.gov/pubmed/33542933 http://dx.doi.org/10.30498/IJB.2020.137202.2305 |
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