| Literature DB >> 25977026 |
Cunshan Zhou1, Jiali Hu2, Haile Ma3, Abu ElGasim A Yagoub4, Xiaojie Yu2, John Owusu5, Haiyan Ma6, Xiaopei Qin2.
Abstract
Protamex catalyzed corn gluten meal (CGM) hydrolysis peptides (CHP) were prepared. Orthogonal design L16 (4(5)) was used to optimize processing variables of CGM concentration, CGM heat pretreatment (121 °C) time, and enzymolysis pH, temperature, and time. Degree of hydrolysis (DH), undigested residue ratio, molecular weight (MW) distribution and DPPH radical inhibition were selected as analysis indicators. Optimum variables were CGM concentration of 18%, heat pretreatment time of 40 min, and enzymolysis pH, temperature and time of 7.5, 55 °C and 24h, respectively. Verification test showed that CHP IC50 for scavenging hydroxyl radical was the best and then followed by reducing power. Oligopeptides improved after hydrolysis at the expense of di- and tripeptides, suggesting formation of soluble aggregates from low MW peptides. The increase in the DH, oligopeptides, Alanyl-Tyrosine, and antioxidant free amino acids coincided with the improvement in the antioxidant activity of CHP.Entities:
Keywords: 1,1-Diphenyl-2-picrylhydrazyl (PubChem CID: 2735032); Antioxidant activity; Aprotinin (PubChem CID: 16197280); Comprehensive balance analysis; Corn gluten meal; Cytochrome C (PubChem CID: 439171); Hydrolysate peptides; Orthogonal experiment; Protamex; Pyrogallol (PubChem CID: 1057); Sulfosalicylic acid (PubChem CID: 7322); Superoxide (PubChem CID: 5359597); Trifluoroacetic acid (PubChem CID: 6422); Tris hydrochloride (PubChem CID: 93573); l-Alanyl-l-Tyrosine (PubChem CID: 92946); l-tryptophan (PubChem CID: 6305)
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Year: 2015 PMID： 25977026 DOI： 10.1016/j.foodchem.2015.04.092
Source DB: PubMed Journal: Food Chem ISSN： 0308-8146 Impact factor: 7.514