期刊
CHEMOSPHERE
卷 135, 期 -, 页码 1-6出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.chemosphere.2015.03.036
关键词
Aflatoxin B1; Laccase; Prooxidant; Mutation; Enzyme affinity
资金
- Tehran University of Medical Sciences, Tehran, Iran [15812]
In this paper, the enzymatic detoxification of aflatoxin B1 (AFB1) by laccase was studied, and the prooxidant properties and mutagenicity of the detoxification products were compared with those of AFB1. The optimal enzymatic reaction occurred in 0.1 M of citrate buffer containing 20% DMSO at 35 degrees C, a pH of 4.5, and a laccase activity of 30 U mL(-1). After 2 d, sixty-seven percent of the toxic substrate was removed. The prooxidative properties of the detoxified products (27% versus 86%) and the mutagenicity were significantly decreased in comparison with the parent toxin. Unlike AFB1, which promoted metabolism-dependent genetic mutations by base-pair substitution, the detoxified products did not induce genotoxicity. Comparison of the K-m values for AFB1 and riboflavin, a valuable food nutrient, indicated that laccase showed greater affinity for the toxin than for riboflavin. (C) 2015 Elsevier Ltd. All rights reserved.
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