Chemometric Analysis of the Amino Acid Requirements of Antioxidant Food Protein Hydrolysates
AbstractThe contributions of individual amino acid residues or groups of amino acids to antioxidant activities of some food protein hydrolysates were investigated using partial least squares (PLS) regression method. PLS models were computed with amino acid composition and 3-z scale descriptors in the X-matrix and antioxidant activities of the samples in the Y-matrix; models were validated by cross-validation and permutation tests. Based on coefficients of the resulting models, it was observed that sulfur-containing (SCAA), acidic and hydrophobic amino acids had strong positive effects on scavenging of 2,2-diphenyl-1-picrylhydrazyl (DPPH) and H2O2 radicals in addition to ferric reducing antioxidant power. For superoxide radicals, only lysine and leucine showed strong positive contributions while SCAA had strong negative contributions to scavenging by the protein hydrolysates. In contrast, positively-charged amino acids strongly contributed negatively to ferric reducing antioxidant power and scavenging of DPPH and H2O2 radicals. Therefore, food protein hydrolysates containing appropriate amounts of amino acids with strong contribution properties could be potential candidates for use as potent antioxidant agents. We conclude that information presented in this work could support the development of low cost methods that will efficiently generate potent antioxidant peptide mixtures from food proteins without the need for costly peptide purification.
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Udenigwe, C.C.; Aluko, R.E. Chemometric Analysis of the Amino Acid Requirements of Antioxidant Food Protein Hydrolysates. Int. J. Mol. Sci. 2011, 12, 3148-3161.
Udenigwe CC, Aluko RE. Chemometric Analysis of the Amino Acid Requirements of Antioxidant Food Protein Hydrolysates. International Journal of Molecular Sciences. 2011; 12(5):3148-3161.Chicago/Turabian Style
Udenigwe, Chibuike C.; Aluko, Rotimi E. 2011. "Chemometric Analysis of the Amino Acid Requirements of Antioxidant Food Protein Hydrolysates." Int. J. Mol. Sci. 12, no. 5: 3148-3161.