Assessment of the Bioactive Potential of Cheese Whey Protein Hydrolysates Using Immobilized Alcalase

• Autor(a) principal: da Cruz, Clariana Zanutto Paulino [UNESP]
• Data de Publicação: 2020
• Outros Autores: de Mendonça, Ricardo José, Guimaraes, Luís Henrique Souza, dos Santos Ramos, Matheus Aparecido [UNESP], Garrido, Saulo Santesso [UNESP], de Paula, Ariela Veloso [UNESP], Monti, Rubens [UNESP], Massolini, Gabriella
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UNESP
• Texto Completo: http://dx.doi.org/10.1007/s11947-020-02552-4; http://hdl.handle.net/11449/208121
• topic: Alcalase; Bioactive peptides; Enzyme immobilization; Whey proteins

The hydrolysis of bovine cheese whey (BCW) proteins was performed by the Alcalase immobilized on the support glyoxyl-corn-cob-powder (AGCCP). The whey protein hydrolysates (WPH) obtained with AGCPP were fractionated by RP-HPLC according to the hydrophilicity of the peptides (F1, hydrophilic; F2, intermediate hydrophilicity; and F3, hydrophobic). The fractions were analyzed by MALDI-TOF, and molecular weight peptides (< 1500 m/z) were identified. Total WPH obtained by AGCCP presented high capacity reduction of the ABTS radical (57.82%) and high chelating activity of iron II (76.2%). The obtained peptides showed high antimicrobial activity (87.75–100%) against the species Escherichia coli (ATCC 43895) and Listeria monocytogenes (ATCC 7644). Only F2 was effective against the Candida albicans strain ATCC 18804 tested (MIC = 10 mg/mL). The results of this study show that the hydrolysis of BCW proteins using the AGCCP derivative represents a very interesting and viable way for obtention of bioactive peptides from cheese whey.