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New mixed Alcalase-hydrolysates were developed using corn gluten meal (CP) and soy protein (SP) hydrolysates, namely CPH, SPH, SPH30:CPH70, SPH70:CPH30, and SPH50:CPH50. Amino acid profile, surface hydrophobicity ( ), molecular weight (MW) distribution, antioxidant activity, angiotensin-converting enzyme (ACE), α-amylase, and α-glucosidase inhibitory activities, and functional characteristics of hydrolysates were determined. Hydrolysis changed the amount of hydrophilic and hydrophobic amino acid composition and significantly increased the values of hydrolysates, especially for CPH. The DPPH radical scavenging activity (RSA) was higher for CPH, SPH30:CPH70, and SPH50:CPH50 than SPH and SPH70:CPH30. Moreover, SPH, SPH70:CPH30, and SPH50:CPH50 showed lower MW than CPH, and this correlated with the higher hydrophilicity, and ABTS and hydroxyl RSA values obtained for SPH and the mixed hydrolysates with predominantly SPH. SPH70:CPH30 exhibited higher ACE, α-glucosidase, and α-amylase inhibitory activities among all samples due to its specific peptides with high capacity to interact with amino acid residues located at the enzyme active site and also low binding energy. At 15% degree of hydrolysis, both SPH and CPH showed enhanced solubility at pH 4.0, 7.0 and 9.0, emulsifying activity, and foaming capacity. Taken together, SPH70:CPH30 displayed strong antioxidant, antihypertensive, and antidiabetic attributes, emulsifying activity and stability indexes, and foaming capacity and foaming stability, making it a promising multifunctional ingredient for the development of functional food products.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10003021 | PMC |
| http://dx.doi.org/10.1002/fsn3.3160 | DOI Listing |
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