Immobilization of trypsin in lignocellulosic waste material to produce peptides with bioactive potential from whey protein

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-gl...

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Autores:
Bassan, Juliana Cristina
de Souza Bezerra, Thaís Milena
Peixoto, Guilherme
Paulino da Cruz, Clariana Zanutto
Martínez Galán, Julián Paul
dos Santos Vaz, Aline Buda
Santesso Garrido, Saulo
Filice, Marco
Monti, Rubens
Tipo de recurso:
Article of investigation
Fecha de publicación:
2016
Institución:
Universidad de Antioquia
Repositorio:
Repositorio UdeA
Idioma:
eng
OAI Identifier:
oai:bibliotecadigital.udea.edu.co:10495/11714
Acceso en línea:
http://hdl.handle.net/10495/11714
Palabra clave:
Corn cob powder functionalized
Trypsin
Immobilization
Reactor
Whey protein hydrolysates
Peptides
Rights
openAccess
License
Atribución-NoComercial-SinDerivadas 2.5 Colombia
Description
Summary: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 ̋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.