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

Autor(es)

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]

Afiliação do(s) autor(es)

^[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

• Tipo de documento: Artigo Científico
• Fonte: MATERIALS; v. 9, n. 5 MAY 2016.
• Citações Web of Science: 7

Resumo

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)

• Processo FAPESP: 12/07680-4 - Hidrolisados parciais de soroproteínas lácteas bovina e bubalina obtidos com proteases imobilizadas: ensaios de transporte e absorção de peptídeos através das técnicas da dialisabilidade e cultura de células Caco-2
• Beneficiário: Juliana Cristina Bassan
• Modalidade de apoio: Bolsas no Brasil - Doutorado
• Processo FAPESP: 14/12563-2 - Utilização de resíduos agroindustriais para imobilização e estabilização de enzimas de interesse biotecnológico
• Beneficiário: Rubens Monti
• Modalidade de apoio: Auxílio à Pesquisa - Regular