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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Bassan, Juliana Cristina [1] ; de Souza Bezerra, Thais Milena [2] ; Peixoto, Guilherme [3] ; Paulino da Cruz, Clariana Zanutto [2] ; Martinez Galan, Julian Paul [1] ; dos Santos Vaz, Aline Buda [2] ; Garrido, Saulo Santesso ; Filice, Marco [4] ; Monti, Rubens [1]
Total Authors: 9
Affiliation:
[1] UNESP Univ Estadual Paulista, Fac Ciencias Farmaceut, Dept Alimentos & Nutr, BR-14800903 Araraquara, SP - Brazil
[2] UNESP Univ Estadual Paulista, Inst Quim, Dept Bioquim & Tecnol Quim, BR-14800060 Araraquara, SP - Brazil
[3] UNESP Univ Estadual Paulista, Fac Ciencias Farmaceut, Dept Bioproc & Biotecnol, BR-14800903 Araraquara, SP - Brazil
[4] Fdn Ctr Nacl Invest Cardiovasc Carlos III, Madrid 28029 - Spain
Total Affiliations: 4
Document type: Journal article
Source: MATERIALS; v. 9, n. 5 MAY 2016.
Web of Science Citations: 7
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 degrees 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. (AU)

FAPESP's process: 14/12563-2 - Agro industrial residues as solid support for immobilization and stabilization of enzymes of biotechnological interest
Grantee:Rubens Monti
Support type: Regular Research Grants
FAPESP's process: 12/07680-4 - Partial hydrolysates of whey proteins from bovine and buffalo milk obtained with immobilised proteases: peptides transportation and absorption through dialyzability and Caco-2 cell culture
Grantee:Juliana Cristina Bassan
Support type: Scholarships in Brazil - Doctorate