by Bassan, Juliana Cristina, de Souza Bezerra, Thais Milena, Peixoto, Guilherme, da Cruz, Clariana Zanutto Paulino, Galán, Julián Paul Martínez, Vaz, Aline Buda Dos Santos, Garrido, Saulo Santesso, Filice, Marco and Monti, Rubens
Abstract:
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 textdegreeC, 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 textpm 0.01 Utextperiodcenteredg-1and an average degree of hydrolysis of 23%, which were suitable for the production of potentially bioactive peptides.
Reference:
Immobilization of Trypsin in Lignocellulosic Waste Material to Produce Peptides with Bioactive Potential from Whey Protein. (Bassan, Juliana Cristina, de Souza Bezerra, Thais Milena, Peixoto, Guilherme, da Cruz, Clariana Zanutto Paulino, Galán, Julián Paul Martínez, Vaz, Aline Buda Dos Santos, Garrido, Saulo Santesso, Filice, Marco and Monti, Rubens), In Materials, Multidisciplinary Digital Publishing Institute, volume 9, 2016.
Bibtex Entry:
@article{Bassan:2016joa,
author = {Bassan, Juliana Cristina and de Souza Bezerra, Thais Milena and Peixoto, Guilherme and da Cruz, Clariana Zanutto Paulino and Gal{'a}n, Juli{'a}n Paul Mart{'i}nez and Vaz, Aline Buda Dos Santos and Garrido, Saulo Santesso and Filice, Marco and Monti, Rubens},
title = {{Immobilization of Trypsin in Lignocellulosic Waste Material to Produce Peptides with Bioactive Potential from Whey Protein.}},
journal = {Materials},
year = {2016},
volume = {9},
number = {5},
pages = {357},
month = may,
publisher = {Multidisciplinary Digital Publishing Institute},
affiliation = {Faculdade de Ci{^e}ncias Farmac{^e}uticas, UNESP-Univ. Estadual Paulista, 14800-903, Departamento de Alimentos e Nutri{c c}{~a}o, Araraquara-SP, Brazil. julianacbassan@gmail.com.},
doi = {10.3390/ma9050357},
pmid = {28773482},
pmcid = {PMC5503075},
language = {English},
rating = {0},
date-added = {2018-03-16T12:40:45GMT},
date-modified = {2018-03-16T13:14:13GMT},
abstract = {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 {textdegree}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 {textpm} 0.01 U{textperiodcentered}g-1and an average degree of hydrolysis of 23%, which were suitable for the production of potentially bioactive peptides.},
url = {http://www.mdpi.com/1996-1944/9/5/357},
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uri = {url{papers3://publication/doi/10.3390/ma9050357}}
}