Hydrolysis of Casein by Pepsin Immobilized on Heterofunctional Supports to Produce Antioxidant Peptides.

Abstract

A study was carried out on the immobilization of pepsin in activated carbon functionalized by different techniques (glutaraldehyde, genipin, and metallization) aiming at its application in obtaining bioactive peptides through casein hydrolysis. Studies of the immobilized derivatives were carried out in addition to the evaluation of the antioxidant potential of the peptides. Among the pH range studied, pH 3.0 was selected due to the higher activity of the derivatives at this pH. The support modification by metallization was the method with the best results, providing a 121% increase in enzymatic activity compared to other immobilization methods. In addition, this derivative provided activity closer to the soluble enzyme activity (3.30 U) and better storage stability, and allows reuse for more than 8 cycles. In turn, the peptides from casein hydrolysis showed potential as antioxidant agents, with a DPPH radical scavenging activity higher than 70%, maximum protection against β-carotene oxidation close to 70%, and a maximum reducing power of Fe(III) into Fe(II) of 400 uM by the FRAP assay. The results showed that the new techniques for modification of activated carbon can be a promising approach for pepsin immobilization.