Characterization of Urease from Providencia sp. LBBE and Its Application in Degrading Urea and Ethyl Carbamate in Rice Wine DOI Creative Commons
Han Wang, Dandan Li, Sibao Zhu

et al.

Fermentation, Journal Year: 2024, Volume and Issue: 10(12), P. 653 - 653

Published: Dec. 17, 2024

Enzymatic degradation of the carcinogen ethyl carbamate (EC) and its precursor urea is a promising method for controlling EC levels in alcoholic beverages. However, limited enzymes with EC-hydrolyzing activity low ethanol or acid tolerance hinder their practical application. Here, new urease urea- activities from Providencia sp. LBBE was characterized. The enzyme displayed considerable tolerance, retaining 42.4% after 1 h incubation 30% (v/v) at 37 °C. It exhibited broad pH (pH 3.0–8.0), optimal 7.0 7.5 urea. After treatment 4.5 5.0, it retained 41.3% 59.4% activity, respectively. Km Vmax were 515.6 mM, 33.9 µmol/(min⸱mg) 32.0 263.6 µmol/(min⸱mg), Using 6000 U/L purified 30 °C 9 h, 49.8% 81.6% removed rice wine 7.0), No appreciable reduction observed under identical conditions, which may be ascribed to minimal affinity. This study contributes future realization effective control content

Language: Английский

A highly thermostable ethyl carbamate-degrading urethanase from Thermoflavimicrobium dichotomicum DOI
Qingtao Liu,

Han Wang,

Xu Li

et al.

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: unknown, P. 142245 - 142245

Published: March 1, 2025

Language: Английский

Citations

0
Salt-Resistant and Ethanol-Resistant Monoamine Oxidases: New Sight for yobN Mining from Bacillus and Biogenic Amine Degradation Mechanism in Fermented Food DOI

Qilin Yang,

Shuangping Liu,

Anthony M. Sun

et al.

Journal of Agricultural and Food Chemistry, Journal Year: 2025, Volume and Issue: unknown

Published: April 14, 2025

Amine oxidases have strong capabilities for the degradation of biogenic amines (BAs) in fermented foods. However, their application is limited by substrate specificity, and high concentrations ethanol salt can hinder effectiveness. This study presents a novel approach utilizing comparative genomics, protein clustering analysis, full homology modeling to identify three amine oxidases: KCYOBN from salt-resistant Bacillus subtilis, LYYOBN1 LYYOBN2 ethanol-resistant cereus. These enzymes are highly similar structure exhibit broad specificities. maintains over 84% relative activity at 20% (w/v) NaCl, while retain 32 21% 25% vol ethanol. Variations key residues one reasons differences tolerance. In foods, degraded 45.97% total BAs cooking wine 38.33% fish sauce. achieved highest rate 32.93% huangjiu. exhibited rates 30.00% soy sauce 35.14% with no significant impact on flavor compounds. The significance this work lies identification through new method, which simultaneously degrade multiple potential.

Language: Английский

Citations

0
Mechanisms of efficient polyacrylamide degradation: From multi-omics analysis to structural characterization of two amidohydrolases DOI
Rui Feng, Lili Ma,

Juyi Zhao

et al.

International Journal of Biological Macromolecules, Journal Year: 2024, Volume and Issue: 281, P. 136329 - 136329

Published: Oct. 8, 2024

Language: Английский

Citations

0
Characterization of Urease from Providencia sp. LBBE and Its Application in Degrading Urea and Ethyl Carbamate in Rice Wine DOI Creative Commons
Han Wang, Dandan Li, Sibao Zhu

et al.

Fermentation, Journal Year: 2024, Volume and Issue: 10(12), P. 653 - 653

Published: Dec. 17, 2024

Enzymatic degradation of the carcinogen ethyl carbamate (EC) and its precursor urea is a promising method for controlling EC levels in alcoholic beverages. However, limited enzymes with EC-hydrolyzing activity low ethanol or acid tolerance hinder their practical application. Here, new urease urea- activities from Providencia sp. LBBE was characterized. The enzyme displayed considerable tolerance, retaining 42.4% after 1 h incubation 30% (v/v) at 37 °C. It exhibited broad pH (pH 3.0–8.0), optimal 7.0 7.5 urea. After treatment 4.5 5.0, it retained 41.3% 59.4% activity, respectively. Km Vmax were 515.6 mM, 33.9 µmol/(min⸱mg) 32.0 263.6 µmol/(min⸱mg), Using 6000 U/L purified 30 °C 9 h, 49.8% 81.6% removed rice wine 7.0), No appreciable reduction observed under identical conditions, which may be ascribed to minimal affinity. This study contributes future realization effective control content

Language: Английский

Citations

0