Engineering substrate specificity of quinone-dependent dehydrogenases for efficient oxidation of deoxynivalenol to 3-keto-deoxynivalenol

Ma, Bin; Niu, Jiafeng; Zhu, Hao; Chi, Huibing; Lu, Zhaoxin; Lu, Fengxia; Zhu, Ping

doi:10.1016/j.ijbiomac.2024.130484

Cited by 3 publications

(1 citation statement)

References 38 publications

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“…Lin et al introduced positively charged lysine mutations on the surface of the zearalenone degrading enzyme ZHD101, and obtained two mutants, D157K and E171K, with increased catalytic efficiencies under acidic conditions [ 14 ]. In the study of Ma et al, a double-mutant L110V/V429A of the deoxynivalenol degrading enzyme DADH with improved preference for deoxynivalenol was constructed based on pocket reshaping [ 15 ]. Additionally, in the study of Liu et al, a CotA-laccase mutant, Q441A, was constructed with improved AFB 1 degradation ability [ 16 ].…”

Section: Introductionmentioning

confidence: 99%

Combined Strategies for Improving Aflatoxin B1 Degradation Ability and Yield of a Bacillus licheniformis CotA-Laccase

Liu,

Huang

et al. 2024

IJMS

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Aflatoxin B1 (AFB1) contamination is a serious threat to nutritional safety and public health. The CotA-laccase from Bacillus licheniformis ANSB821 previously reported by our laboratory showed great potential to degrade AFB1 without redox mediators. However, the use of this CotA-laccase to remove AFB1 in animal feed is limited because of its low catalytic efficiency and low expression level. In order to make better use of this excellent enzyme to effectively degrade AFB1, twelve mutants of CotA-laccase were constructed by site-directed mutagenesis. Among these mutants, E186A and E186R showed the best degradation ability of AFB1, with degradation ratios of 82.2% and 91.8% within 12 h, which were 1.6- and 1.8-times higher than those of the wild-type CotA-laccase, respectively. The catalytic efficiencies (kcat/Km) of E186A and E186R were found to be 1.8- and 3.2-times higher, respectively, than those of the wild-type CotA-laccase. Then the expression vectors pPICZαA-N-E186A and pPICZαA-N-E186R with an optimized signal peptide were constructed and transformed into Pichia pastoris GS115. The optimized signal peptide improved the secretory expressions of E186A and E186R in P. pastoris GS115. Collectively, the current study provided ideal candidate CotA-laccase mutants for AFB1 detoxification in food and animal feed and a feasible protocol, which was desperately needed for the industrial production of CotA-laccases.

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Section: Introductionmentioning

confidence: 99%

Combined Strategies for Improving Aflatoxin B1 Degradation Ability and Yield of a Bacillus licheniformis CotA-Laccase

Liu,

Huang

et al. 2024

IJMS

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Expression, characterization and application of the deoxynivalenol dehydrogenase from Devosia yakushimensis

Xu,

Yao,

Shi

et al. 2024

J Sci Food Agric

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BACKGROUNDDeoxynivalenol (DON) is one of the type‐B trichothecene mycotoxins generally produced by Fusarium fungi and widely pollutes wheat and other grains, causing a great loss in grain yield and significant threat to human health. Enzymatic treatment of DON has displayed a significant role in controlling its levels in recent years.RESULTSHere, the DON dehydrogenase from Devosia yakushimensis (DeDDH) is reported. DeDDH exhibited the highest activity in an environment of 35 °C and pH 7.5. In addition, the residual activity of DeDDH was about 40% after pre‐incubation at 80 °C for 0.5 h, suggesting a good thermostability. The presence of Ca2+ significantly boosted the activity of DeDDH, but substituting Ca2+ with other ions could hardly retain the activity. At the optimal conditions, DeDDH efficiently degraded 75% DON (45 μg mL−1) within 4 h. Notably, when three cofactors, PQQ, PMS and DCPIP, were added together, more than 90% DON (45 μg mL−1) was quickly degraded in the first 40 min.CONCLUSIONThe residues Thr485 and Leu521 were found to be significant to the activity of DeDDH by site‐directed mutagenesis, much different from other DON dehydrogenases. Nevertheless, further research on the crystal structure determination of DeDDH, key catalytic residue identification, catalytic activity and thermostability modification still needs to be conducted for application in industry. © 2024 Society of Chemical Industry.

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Characterization of deoxynivalenol dehydrogenase from Pelagibacterium sp. SCN 63–126 and its application

Xu,

Yao,

et al. 2024

Arch Microbiol

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Engineering substrate specificity of quinone-dependent dehydrogenases for efficient oxidation of deoxynivalenol to 3-keto-deoxynivalenol

Cited by 3 publications

References 38 publications

Combined Strategies for Improving Aflatoxin B1 Degradation Ability and Yield of a Bacillus licheniformis CotA-Laccase

Combined Strategies for Improving Aflatoxin B1 Degradation Ability and Yield of a Bacillus licheniformis CotA-Laccase

Expression, characterization and application of the deoxynivalenol dehydrogenase from Devosia yakushimensis

Characterization of deoxynivalenol dehydrogenase from Pelagibacterium sp. SCN 63–126 and its application

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