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

Materials

Rubens Monti¹  Julián Paul Martínez Galán¹  Juliana Cristina Bassan¹  Guilherme Peixoto²  Marco Filice³  Saulo Santesso Garrido⁴  Clariana Zanutto Paulino da Cruz⁴  Thaís Milena de Souza Bezerra⁴  Aline Buda dos Santos Vaz⁴ 

[1] Faculdade de Ciências Farmacêuticas, UNESP—Univ. Estadual Paulista, 14800-903, Departamento de Alimentos e Nutrição, Araraquara-SP, Brazil;Faculdade de Ciências Farmacêuticas, UNESP—Univ. Estadual Paulista, 14800-903, Departamento de Bioprocessos e Biotecnologia, Araraquara-SP, Brazil;Fundación Centro Nacional de Investigaciones Cardiovasculares Carlos III, Melchor Fernández Almagro, Madrid 28029, Spain;Instituto de Química, UNESP—Univ. Estadual Paulista, 14800-060, Departamento de Bioquímica e Tecnologia Química, Araraquara-SP, Brazil;

关键词: corn cob powder functionalized;    trypsin;    immobilization;    reactor;    whey protein hydrolysates;    peptides;   

DOI  :  10.3390/ma9050357

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown