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...
- 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
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. |
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