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Addendum published on 19 August 2016, see Materials 2016, 9(8), 705.

Open AccessArticle
Materials 2016, 9(5), 357; doi:10.3390/ma9050357

Immobilization of Trypsin in Lignocellulosic Waste Material to Produce Peptides with Bioactive Potential from Whey Protein

1
Faculdade de Ciências Farmacêuticas, UNESP—Univ. Estadual Paulista, 14800-903, Departamento de Alimentos e Nutrição, Araraquara-SP, Brazil
2
Instituto de Química, UNESP—Univ. Estadual Paulista, 14800-060, Departamento de Bioquímica e Tecnologia Química, Araraquara-SP, Brazil
3
Faculdade de Ciências Farmacêuticas, UNESP—Univ. Estadual Paulista, 14800-903, Departamento de Bioprocessos e Biotecnologia, Araraquara-SP, Brazil
4
Fundación Centro Nacional de Investigaciones Cardiovasculares Carlos III, Melchor Fernández Almagro, Madrid 28029, Spain
*
Authors to whom correspondence should be addressed.
Academic Editors: Jalel Labidi and Susana C. M. Fernandes
Received: 30 March 2016 / Revised: 3 May 2016 / Accepted: 4 May 2016 / Published: 12 May 2016
(This article belongs to the Special Issue Advances in Functionalization of Lignocellulosic Materials)
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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. View Full-Text
Keywords: corn cob powder functionalized; trypsin; immobilization; reactor; whey protein hydrolysates; peptides corn cob powder functionalized; trypsin; immobilization; reactor; whey protein hydrolysates; peptides
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MDPI and ACS Style

Bassan, J.C.; de Souza Bezerra, T.M.; Peixoto, G.; da Cruz, C.Z.P.; Galán, J.P.M.; Vaz, A.B.S.; Garrido, S.S.; Filice, M.; Monti, R. Immobilization of Trypsin in Lignocellulosic Waste Material to Produce Peptides with Bioactive Potential from Whey Protein. Materials 2016, 9, 357.

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