Antioxidant Activity of Soy Protein Hydrolysates in a Liposomal System

Authors

  • E.A. Peñta-Ramos,

    1. Author Peña-Ramos is with the Animal Derived Food Dept., Centro de Investigación en Alimentación y Desarrollo, A. C., Hermosillo, Sonora, C.P. 83000, México. AuthorXiongis with the Dept. of Animal Sciences, Food Science Section, Univ. of Kentucky, Lexington, KY 40546, USA. Direct inquiries to author Xiong (E-mail: ylxiong@uky.edu).
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  • Y.L. Xiong

    1. Author Peña-Ramos is with the Animal Derived Food Dept., Centro de Investigación en Alimentación y Desarrollo, A. C., Hermosillo, Sonora, C.P. 83000, México. AuthorXiongis with the Dept. of Animal Sciences, Food Science Section, Univ. of Kentucky, Lexington, KY 40546, USA. Direct inquiries to author Xiong (E-mail: ylxiong@uky.edu).
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  • Published as journal article 02-07-32 of the Kentucky Agricultural Experiment Station.

Abstract

ABSTRACT: Native and heated soy protein isolate was hydrolyzed with 3 purified (pepsin, papain, and chymotrypsin) and 3 crude (Alcalase®, ProtamexTM, and FlavourzymeTM) 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.

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