期刊
FOOD CHEMISTRY
卷 237, 期 -, 页码 350-355出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2017.05.112
关键词
Whey protein concentrate; Enzymatic hydrolysates; Antioxidant peptides; Immobilization
资金
- Scientific Research Commission of the Province of Buenos Aires (CIC) grant
- Science Basic Department of the National University of Lujan (UNLu) grant
An aspartic protease from Salpichroa origanifolia fruits was successfully immobilized onto an activated support of glutaraldehyde agarose. The immobilized enzyme presented higher thermal stability than the free enzyme from 40 degrees C to 50 degrees C and high reusability, retaining 54% of the initial activity after ten cycles of the process. Whey protein concentrates (WPC) were hydrolyzed with both free and immobilized enzyme, reaching a similar degree of hydrolysis of approximately 6-8% after 20 h. In addition, the immobilized derivate hydrolyzed alpha-lactalbumin protein with a higher affinity than beta-lactoglobulin. The hydrolysate was ultra-filtrated, and the fractions were evaluated for antioxidant activities with the 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity method. The fraction containing peptides with a molecular mass below 3 kDa demonstrated a strong radical quenching effect (IC50: 0.48 mg/ml). These results suggest that hydrolyzed WPC could be considered as a promising source of natural food antioxidants for the development of functional food. (C) 2017 Elsevier Ltd. All rights reserved.
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