Journal
FOOD CHEMISTRY
Volume 232, Issue -, Pages 753-762Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2017.04.071
Keywords
Buffalo casein; Bovine casein; Hydrolysate; Alcalase; Trypsin; Antioxidant peptides
Funding
- National Natural Science Foundation of China [31471583]
- National High-Tech Research and Development Program of China (863 program) [2013AA102200]
- '12th-Five' National Science and Technology Support Program of China [2012BAD37B01]
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Buffalo and bovine caseins were hydrolysed by alcalase and trypsin to produce novel antioxidant peptides. The casein hydrolysates were purified using ultrafiltration (UF) and further characterized by RP-HPLC. The fractions produced higher antioxidant activities were identified for their peptides using LC MS/MS. All UF-VI (MW < 1 kDa) fractions showed higher antioxidant activity. Hydrolysate produced by alcalase for buffalo casein (UF-VI with 54.84-fold purification) showed higher antioxidant activity than that obtained by trypsin. Trypsin hydrolysate contained high amount of hydrophobic amino acids while alcalase hydrolysate consisted mainly of Ser, Arg, Ala and Leu. The antioxidant peptides identified by LC MS/MS were RELEE, MEDNKQ and TVA, EQL in buffalo casein hydrolysates produced by trypsin and alcalase, respectively. Mechanism and reaction pathways of selected antioxidant peptides with ABTS were proposed. Conclusively, buffalo casein provided antioxidant peptides similar to bovine, suggesting that buffalo casein is a novel source of antioxidant. (C) 2017 Elsevier Ltd. All rights reserved.
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