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Characterization, Mechanism, and Application of Dipeptidyl Peptidase III: An Aflatoxin B<sub>1</sub>-Degrading Enzyme from <i>Aspergillus terreus</i> HNGD-TM15

Hongxin Zhang, Lanbin Cui, Yanli Xie, Xiao Li, Renyong Zhao, Yuhui Yang, Shumin Sun, Qian Li, Weibin Ma, Hang Jia

2024Journal of Agricultural and Food Chemistry18 citationsDOI

Abstract

Aflatoxin B 1 is a notorious mycotoxin with mutagenicity and carcinogenicity, posing a serious hazard to human and animal health. In this study, an AFB 1 -degrading dipeptidyl-peptidase III mining from Aspergillus terreus HNGD-TM15 (ADPP III) with a molecular weight of 79 kDa was identified. ADPP III exhibited optimal activity toward AFB 1 at 40 °C and pH 7.0, maintaining over 80% relative activity at 80 °C. The key amino acid residues that affected enzyme activity were identified as H450, E451, H455, and E509 via bioinformatic analysis and site-directed mutagenesis. The degradation product of ADPP III toward AFB 1 was verified to be AFD 1. The zebrafish hepatotoxicity assay verified the toxicity of the AFB 1 degradation product was significantly weaker than that of AFB 1 . The result of this study proved that ADPP III presented a promising prospect for industrial application in food and feed detoxification.

Topics & Concepts

Aspergillus terreusAflatoxinEnzymeAspergillusChemistryDipeptidyl peptidaseMechanism (biology)BiochemistryFood scienceBiologyMicrobiologyPhilosophyEpistemologyPeptidase Inhibition and AnalysisProtein Hydrolysis and Bioactive PeptidesEnzyme Production and Characterization
Characterization, Mechanism, and Application of Dipeptidyl Peptidase III: An Aflatoxin B<sub>1</sub>-Degrading Enzyme from <i>Aspergillus terreus</i> HNGD-TM15 | Litcius