دورية أكاديمية
Characterization, Structural Analysis, and Thermal Stability Mutation of a New Zearalenone-Degrading Enzyme Mined from Bacillus subtilis
| العنوان: | Characterization, Structural Analysis, and Thermal Stability Mutation of a New Zearalenone-Degrading Enzyme Mined from Bacillus subtilis |
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| المؤلفون: | Jinghao Shi, Fred Mwabulili, Yanli Xie, Yuhui Yang, Shumin Sun, Qian Li, Weibin Ma, Hang Jia |
| سنة النشر: | 2024 |
| مصطلحات موضوعية: | Biophysics, Biochemistry, Microbiology, Genetics, Biotechnology, Computational Biology, Chemical Sciences not elsewhere classified, causes serious damage, binding mode within, optimal enzyme activity, gene sequence encoding, bacillus subtilis zearalenone, 5 , 24 , 18 , 45 ° c, 37 ° c, fifth residue n, achieve zen biodegradation, degrading enzyme mined, degradative enzyme zeny, thermal stability mutation, thermal stability, sequence comparison, new zearalenone, zen hydrolases, zen degradation, yielded 80, widespread mycotoxin, structural analysis |
| الوصف: | Zearalenone (ZEN) is a widespread mycotoxin that causes serious damage to animal husbandry and poses a threat to human health. A screen of ZEN-degrading soil bacteria yielded Bacillus subtilis YT-4, which yielded 80% ZEN degradation after 6 h and 95% after 36 h. The gene sequence encoding the degradative enzyme ZENY was mined from the genome of YT-4 and expressed in yeast. ZENY is an α/β-hydrolase with an optimal enzyme activity at 37 °C and pH 8. By breaking the lactone ring of ZEN, it produces ZENY-C 18 H 24 O 5 with a molecular weight of 320.16 g/mol. Sequence comparison and molecular docking analyses identified the catalytic ZENY triad 99S-245H-123E and the primary ZEN-binding mode within the hydrophobic pocket of the enzyme. To improve the thermal stability of the enzyme for industrial applications, we introduced a mutation at the N-terminus, specifically replacing the fifth residue N with V, and achieved a 25% improvement in stability at 45 °C. These findings aim to achieve ZEN biodegradation and provide insight into the structure and function of ZEN hydrolases. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | unknown |
| العلاقة: | https://figshare.com/articles/journal_contribution/Characterization_Structural_Analysis_and_Thermal_Stability_Mutation_of_a_New_Zearalenone-Degrading_Enzyme_Mined_from_Bacillus_subtilis/25129982Test |
| DOI: | 10.1021/acs.jafc.3c06767.s001 |
| الإتاحة: | https://doi.org/10.1021/acs.jafc.3c06767.s001Test https://figshare.com/articles/journal_contribution/Characterization_Structural_Analysis_and_Thermal_Stability_Mutation_of_a_New_Zearalenone-Degrading_Enzyme_Mined_from_Bacillus_subtilis/25129982Test |
| حقوق: | CC BY-NC 4.0 |
| رقم الانضمام: | edsbas.3F6F91A4 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1021/acs.jafc.3c06767.s001 |
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