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Characterization of Two Dehydrogenases from Gluconobacter oxydans Involved in the Transformation of Patulin to Ascladiol
| Content Provider | MDPI |
|---|---|
| Author | Chan, Edicon T. S. Zhu, Yan Li, Xiu-Zhen Zhou, Ting Seah, Stephen Y. K. |
| Copyright Year | 2022 |
| Description | Patulin is a mycotoxin that primarily contaminate apples and apple products. Whole cell or cell-free extracts of Gluconobacter oxydans ATCC 621 were able to transform patulin to E-ascladiol. Proteins from cell-free extracts were separated by anion exchange chromatography and fractions with patulin transformation activity were subjected to peptide mass fingerprinting, enabling the identification of two NADPH dependent short chain dehydrogenases, GOX0525 and GOX1899, with the requisite activity. The genes encoding these enzymes were expressed in E. coli and purified. Kinetic parameters for patulin reduction, as well as pH profiles and thermostability were established to provide further insight on the potential application of these enzymes for patulin detoxification. |
| Starting Page | 423 |
| e-ISSN | 20726651 |
| DOI | 10.3390/toxins14070423 |
| Journal | Toxins |
| Issue Number | 7 |
| Volume Number | 14 |
| Language | English |
| Publisher | MDPI |
| Publisher Date | 2022-06-21 |
| Access Restriction | Open |
| Subject Keyword | Toxins Toxicology Mycotoxin Patulin Ascladiol Gluconobacter Oxydans Detoxification Enzyme Dehydrogenase |
| Content Type | Text |
| Resource Type | Article |