Isolation and Purification of Antioxidant Peptide from Cheese Whey Hydrolysates Produced with Alkaline Protease

doi:10.7506/spkx1002-6630-201513032

Abstract

Abstract:

Cheese whey hydrolysates were obtained by enzymatic hydrolysis with an alkaline protease “alcalase” for 2 h
at 50 ℃ and an initial pH of 9.5 with an [E]/[S] ratio of 4%. The antioxidant peptide was purified from cheese whey
hydrolysates by ultrafiltration, polydextran gel chromatography and tricine-sodium dodecyl sulfate-polyacrylamide
gelelectrophoresis (tricine SDS-PAGE). The optimal operating pressure, hydrolysate temperature and pH and ultrafiltration
time for the improved ultrafiltration membrane flux were found to be 0.25 MPa, 30 ℃, 9.0 and 120 min, respectively. The
peptide with molecular weights ranging from 4 000 to 6 000 D had the highest inhibitory activity on lipid peroxidation, with
an inhibitory rate of approximately 47.28%. After purification with Sephadex G-50, the separated fractions were determined
by tricine SDS-PAGE and lipid peroxidation inhibition, respectively. Fraction 34 with molecular weight distribution ranging
from 4 000 to 4 100 D had the highest inhibitory activity on lipid peroxidation.

Key words: cheese whey, ultrafiltration, Alaclase 2.4L, antioxidant peptide

CLC Number:

TS252.9

HUO Jianxin1, YUAN Huiyan1, WANG Yan1, WANG Yan1, BAI Caiyan1, ZHAO Wenbo2,*. Isolation and Purification of Antioxidant Peptide from Cheese Whey Hydrolysates Produced with Alkaline Protease[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201513032.

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Isolation and Purification of Antioxidant Peptide from Cheese Whey Hydrolysates Produced with Alkaline Protease

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