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TitleStructure-guided protein engineering and immobilization of an amidohydrolase for efficient ochratoxin A detoxification.
Journal, issue, pagesInt J Biol Macromol, Vol. 358, Page 151671, Year 2026
Publish dateMar 26, 2026
AuthorsYumei Hu / Yuhang Xu / Biyu He / Du Niu / Xuechun Yang / Jiaping Huang / Zhenzhen Xie / Panpan Shen / Xian Li / Maosen Bai / Ziwei Liu / Hao Li / Yunyun Yang / Jian-Wen Huang / Chun-Chi Chen / Rey-Ting Guo / Longhai Dai /
PubMed AbstractOchratoxin A (OTA) is a pervasive and significant mycotoxin that poses serious health risks to humans and animals. The development of efficient biocatalysts for the enzymatic detoxification of OTA is ...Ochratoxin A (OTA) is a pervasive and significant mycotoxin that poses serious health risks to humans and animals. The development of efficient biocatalysts for the enzymatic detoxification of OTA is of great importance. In this study, we enhanced the OTA-degrading activity of three amidohydrolases (ADHs) by up to ninefold. This improvement was achieved by reducing steric hindrance in the binding pocket and fine-tuning the hydrophilic interactions between the enzyme and substrate. The most efficient variant, PwADH/DM, was immobilized onto magnetic FeO nanoparticles functionalized by the co-deposition of dopamine and polyethyleneimine. Under optimal conditions, this immobilization process achieved a high immobilization efficiency (85.4%) and activity recovery (76.9%). The immobilized enzyme exhibited enhanced pH stability and thermostability, along with good storage stability, reusability, and recyclability. More importantly, the immobilized enzyme completely degraded 100 ng/mL OTA in contaminated milk without affecting the milk's properties. These findings expand our understanding of the molecular mechanisms governing substrate binding and catalysis in OTA-degrading ADHs. Furthermore, they provide a blueprint for enzyme-based OTA decontamination during food processing.
External linksInt J Biol Macromol / PubMed:41903634
MethodsEM (single particle)
Resolution2.69 - 2.9 Å
Structure data

62778

9l2o

EMDB-62778, PDB-9l2o:
Cryo-EM structure and rational engineering of a novel efficient ochratoxin A-detoxifying amidohydrolase
Method: EM (single particle) / Resolution: 2.86 Å

62780

9l2t

EMDB-62780, PDB-9l2t:
Cryo-electron microscopic structure of a novel amidohydrolase with three mutations
Method: EM (single particle) / Resolution: 2.69 Å

62861

9l6p

EMDB-62861, PDB-9l6p:
Cryo-electron microscopic structure of a highly efficient ochratoxin detoxification enzyme LlADH
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-97U:
(2~{S})-2-[[(3~{R})-5-chloranyl-3-methyl-8-oxidanyl-1-oxidanylidene-3,4-dihydroisochromen-7-yl]carbonylamino]-3-phenyl-propanoic acid / toxin*YM

Source
  • pseudoxanthomonas wuyuanensis (bacteria)
  • novilysobacter luteus (bacteria)
KeywordsHYDROLASE / amide hydrolase / Iron-binding / Ochratoxin A / ZN / TOXIN

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