Affinity purification of trypsin inhibitor with anti-Aspergillus flavus activity from cultivated and wild soybean
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Updated: Jun 29, 2026
Inhibition of Aspergillus flavus Growth and Aflatoxin Production in Transgenic Maize Expressing the α-amylase Inhibitor from Lablab purpureus L.
Published on: February 15, 2019
Bin Zhang1, Dong-Feng Wang, Yan Fan
1Department of Food Chemistry and Nutrition, College of Food Science and Technology, Ocean University of China, Yu Shan Road 5, Qingdao, 266003, People's Republic of China.
Abstract:
Trypsin inhibitors (TI) from wild-type soybean (Glycine soya) (WBTI) and domesticated soybean (Glycine max) (SBTI) were purified using prepared chitosan resin-trypsin as filler on the affinity chromatography column. The SBTI/WBTI purification fold by affinity chromatography was 718- and 279-fold, with the activity recovery of 62% and 59%, respectively. It was found that SBTI and WBTI exerted a strong inhibition of Aspergillus. flavus growth, with IC(50) of 1.6 and 1.0 micromol/l. This growth inhibition was possibly the result of the inhibition on alpha-amylase activity of A. flavus by both the SBTI and WBTI. This was further supported by the fact that in the presence of SBTI and WBTI at 9.0 and 6.0 microg/g (peanut) on peanuts inhibited the germination and growth of A. flavus. Accordingly, characterization of the mode of action of SBTI and WBTI could constitute a first step leading to resistance to A. flavus invasion.
