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

Abstract

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.