TY - JOUR
T1 - Antioxidant activity of soy protein hydrolysates in a liposomal system
AU - Peña-Ramos, E. A.
AU - Xiong, Y. L.
PY - 2002/10
Y1 - 2002/10
N2 - Native and heated soy protein isolate was hydrolyzed with 3 purified (pepsin, papain, and chymotrypsin) and 3 crude (Alcalase®, Protamex™, and Flavourzyme™) proteases. The hydrolysates were incubated (37°C, 1 h) with a liposome-oxidizing system (50 μM FeCl3/0.1 mM ascorbate, pH 7.0) to test antioxidant activities by determining the concentrations of TBARS. Degree of hydrolysis of SPI hydrolysates ranged from 1.7 to 20.6%. Both hydrolyzed and nonhydrolyzed SPI decreased TBARS (by 28 to 65%), except for papain-hydrolyzed samples. Samples of chymotrypsin- and Flavourzyme-hydrolyzed (0.5 h) preheated SPI had the greatest inhibitory effect on lipid oxidation.
AB - Native and heated soy protein isolate was hydrolyzed with 3 purified (pepsin, papain, and chymotrypsin) and 3 crude (Alcalase®, Protamex™, and Flavourzyme™) proteases. The hydrolysates were incubated (37°C, 1 h) with a liposome-oxidizing system (50 μM FeCl3/0.1 mM ascorbate, pH 7.0) to test antioxidant activities by determining the concentrations of TBARS. Degree of hydrolysis of SPI hydrolysates ranged from 1.7 to 20.6%. Both hydrolyzed and nonhydrolyzed SPI decreased TBARS (by 28 to 65%), except for papain-hydrolyzed samples. Samples of chymotrypsin- and Flavourzyme-hydrolyzed (0.5 h) preheated SPI had the greatest inhibitory effect on lipid oxidation.
KW - Antioxidants
KW - Hydrolysis
KW - Oxidation
KW - Soy protein
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U2 - 10.1111/j.1365-2621.2002.tb08844.x
DO - 10.1111/j.1365-2621.2002.tb08844.x
M3 - Article
AN - SCOPUS:0036813306
SN - 0022-1147
VL - 67
SP - 2952
EP - 2956
JO - Journal of Food Science
JF - Journal of Food Science
IS - 8
ER -