Resumo

TOVAR-JIMENEZ, Xochitl et al. Antioxidant and antihypertensive activity of bovine whey protein concentrate enzymatic hydrolysates. Biotecnia [online]. 2021, vol.23, n.1, pp.161-169.  Epub 18-Jun-2021. ISSN 1665-1456.  https://doi.org/10.18633/biotecnia.v23i1.1321.

Whey is a polluting by-product of cheese processing. However, it has valuable nutritional properties that can be exploited for diverse applications. Research has shown how whey proteins enzymatic hydrolysis releases bioactive peptides. In the present study, the whey protein concentrate (WCP) hydrolysis was performed using purified Sporisorium reilianum aspartyl protease (Eap1), with commercial enzymes chymotrypsin (C) and trypsin (T), as well as different enzymatic combinations in order to determine which enzyme or combination allowed for the release of peptides presenting the highest antioxidant and antihypertensive activity levels. Our results indicated that hydrolysis with Eap1 releases the best-performing peptides (1467.30 mM AAEAA/100g WCP; 835.20 mM FeSO4 /100g WCP and 83.36 % ACE inhibition) in comparison with individual enzymes (Q: 1164.60 mM AAEAA/100g WCP; 305.35 mM FeSO4/100g WCP; 92.35 % ACE inhibition and T: 354.87 mM AAEAA/100g WCP; 205.82 mM FeSO4/100g WCP; 83.8 % ACE inhibition) and their combinations (Eap1-C: 1050.23 mM AAEAA/100g WCP; 399.09 mM FeSO4/100g WCP; 85.58 % ACE inhibition, Eap1-T: 882.5 mM AAEAA/100g WCP; 220.63 mM FeSO4/100g WCP; 85.40 % ACE inhibition, C-T: 994.67 mM AAEAA/100g WCP; 310.43 mM FeSO4/100g WCP; 61.27 % ACE inhibition and C-Eap1-T: 93.23 mM AAEAA/100g WCP; 23.3 mM FeSO4/100g WCP; 38.35 % ACE inhibition).

Palavras-chave : antioxidant peptides; antihypertensive peptides; protein concentrate from bovine whey; aspartyl protease of Sporisorium reilianum; commercial enzymes.

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