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New urethanase from the yeast Candida parapsilosis
Kazuo Masaki1, Taichi Mizukure2, Dararat Kakizono3
1National Research Institute of Brewing, 3-7-1 Kagamiyama, Higashihiroshima 739-0046, Japan; Graduate School of Biosphere Science, Hiroshima University, 1-4-4 Kagamiyama, Higashihiroshima 739-8528, Japan.
Journal of Bioscience and Bioengineering
|April 8, 2020
Summary
A new urethanase (CPUTNase) from Candida parapsilosis effectively removes ethyl carbamate (EC) from alcoholic beverages. This enzyme is stable in ethanol and functions optimally at 43°C and pH 10.
Area of Science:
- Enzymology
- Biotechnology
- Food Science
Background:
- Urethanase (EC 3.5.1.75) is crucial for removing ethyl carbamate (EC) in alcoholic beverages.
- Urethanase research is limited, hindering practical applications.
- Candida parapsilosis utilizes EC as a nitrogen source, suggesting potential for urethanase discovery.
Purpose of the Study:
- To discover and characterize a novel urethanase from Candida parapsilosis.
- To investigate the enzymatic properties, sequence, and recombinant expression of the new urethanase.
- To assess the potential of amidase family proteins as urethanases.
Main Methods:
- Enzyme extraction and purification from Candida parapsilosis using ion-exchange chromatography.
- Determination of enzyme characteristics including stability in ethanol, optimal temperature, and pH activity.
- Gene identification, recombinant enzyme expression in Saccharomyces cerevisiae, and sequence analysis.
Main Results:
- A novel urethanase, CPUTNase, was purified from Candida parapsilosis.
- CPUTNase demonstrated stability in 0%-40% ethanol solutions, with optimal activity at 43°C and pH 10.
- Recombinant CPUTNase exhibited identical characteristics to the native enzyme and was identified as an amidase family protein.
Conclusions:
- CPUTNase is a promising enzyme for ethyl carbamate removal in alcoholic beverages.
- Amidase family proteins are potential candidates for urethanase applications.
- This study contributes to a deeper understanding of urethanase enzymes and their potential industrial use.
