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Immobilization of Trypsin in Lignocellulosic Waste Material to Produce Peptides with Bioactive Potential from Whey Protein
In this study, trypsin (Enzyme Comission 3.4.21.4) was immobilized in a low cost, lignocellulosic support (corn cob powder—CCP) with the goal of obtaining peptides with bioactive potential from cheese whey. The pretreated support was activated with glyoxyl groups, glutaraldehyde and IDA-glyoxyl. The...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5503075/ https://www.ncbi.nlm.nih.gov/pubmed/28773482 http://dx.doi.org/10.3390/ma9050357 |
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author | Bassan, Juliana Cristina de Souza Bezerra, Thaís Milena Peixoto, Guilherme da Cruz, Clariana Zanutto Paulino Galán, Julián Paul Martínez Vaz, Aline Buda dos Santos Garrido, Saulo Santesso Filice, Marco Monti, Rubens |
author_facet | Bassan, Juliana Cristina de Souza Bezerra, Thaís Milena Peixoto, Guilherme da Cruz, Clariana Zanutto Paulino Galán, Julián Paul Martínez Vaz, Aline Buda dos Santos Garrido, Saulo Santesso Filice, Marco Monti, Rubens |
author_sort | Bassan, Juliana Cristina |
collection | PubMed |
description | In this study, trypsin (Enzyme Comission 3.4.21.4) was immobilized in a low cost, lignocellulosic support (corn cob powder—CCP) with the goal of obtaining peptides with bioactive potential from cheese whey. The pretreated support was activated with glyoxyl groups, glutaraldehyde and IDA-glyoxyl. The immobilization yields of the derivatives were higher than 83%, and the retention of catalytic activity was higher than 74%. The trypsin-glyoxyl-CCP derivative was thermally stable at 65 °C, a value that was 1090-fold higher than that obtained with the free enzyme. The trypsin-IDA-glyoxyl-CCP and trypsin-glutaraldehyde-CCP derivatives had thermal stabilities that were 883- and five-fold higher, respectively, then those obtained with the free enzyme. In the batch experiments, trypsin-IDA-glyoxyl-CCP retained 91% of its activity and had a degree of hydrolysis of 12.49%, while the values for trypsin-glyoxyl-CCP were 87% and 15.46%, respectively. The stabilized derivative trypsin-glyoxyl-CCP was also tested in an upflow packed-bed reactor. The hydrodynamic characterization of this reactor was a plug flow pattern, and the kinetics of this system provided a relative activity of 3.04 ± 0.01 U·g(−1) and an average degree of hydrolysis of 23%, which were suitable for the production of potentially bioactive peptides. |
format | Online Article Text |
id | pubmed-5503075 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-55030752017-07-28 Immobilization of Trypsin in Lignocellulosic Waste Material to Produce Peptides with Bioactive Potential from Whey Protein Bassan, Juliana Cristina de Souza Bezerra, Thaís Milena Peixoto, Guilherme da Cruz, Clariana Zanutto Paulino Galán, Julián Paul Martínez Vaz, Aline Buda dos Santos Garrido, Saulo Santesso Filice, Marco Monti, Rubens Materials (Basel) Article In this study, trypsin (Enzyme Comission 3.4.21.4) was immobilized in a low cost, lignocellulosic support (corn cob powder—CCP) with the goal of obtaining peptides with bioactive potential from cheese whey. The pretreated support was activated with glyoxyl groups, glutaraldehyde and IDA-glyoxyl. The immobilization yields of the derivatives were higher than 83%, and the retention of catalytic activity was higher than 74%. The trypsin-glyoxyl-CCP derivative was thermally stable at 65 °C, a value that was 1090-fold higher than that obtained with the free enzyme. The trypsin-IDA-glyoxyl-CCP and trypsin-glutaraldehyde-CCP derivatives had thermal stabilities that were 883- and five-fold higher, respectively, then those obtained with the free enzyme. In the batch experiments, trypsin-IDA-glyoxyl-CCP retained 91% of its activity and had a degree of hydrolysis of 12.49%, while the values for trypsin-glyoxyl-CCP were 87% and 15.46%, respectively. The stabilized derivative trypsin-glyoxyl-CCP was also tested in an upflow packed-bed reactor. The hydrodynamic characterization of this reactor was a plug flow pattern, and the kinetics of this system provided a relative activity of 3.04 ± 0.01 U·g(−1) and an average degree of hydrolysis of 23%, which were suitable for the production of potentially bioactive peptides. MDPI 2016-05-12 /pmc/articles/PMC5503075/ /pubmed/28773482 http://dx.doi.org/10.3390/ma9050357 Text en © 2016 by the authors; Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Bassan, Juliana Cristina de Souza Bezerra, Thaís Milena Peixoto, Guilherme da Cruz, Clariana Zanutto Paulino Galán, Julián Paul Martínez Vaz, Aline Buda dos Santos Garrido, Saulo Santesso Filice, Marco Monti, Rubens Immobilization of Trypsin in Lignocellulosic Waste Material to Produce Peptides with Bioactive Potential from Whey Protein |
title | Immobilization of Trypsin in Lignocellulosic Waste Material to Produce Peptides with Bioactive Potential from Whey Protein |
title_full | Immobilization of Trypsin in Lignocellulosic Waste Material to Produce Peptides with Bioactive Potential from Whey Protein |
title_fullStr | Immobilization of Trypsin in Lignocellulosic Waste Material to Produce Peptides with Bioactive Potential from Whey Protein |
title_full_unstemmed | Immobilization of Trypsin in Lignocellulosic Waste Material to Produce Peptides with Bioactive Potential from Whey Protein |
title_short | Immobilization of Trypsin in Lignocellulosic Waste Material to Produce Peptides with Bioactive Potential from Whey Protein |
title_sort | immobilization of trypsin in lignocellulosic waste material to produce peptides with bioactive potential from whey protein |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5503075/ https://www.ncbi.nlm.nih.gov/pubmed/28773482 http://dx.doi.org/10.3390/ma9050357 |
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