Characterization of a novel meta-fission product hydrolase from Dyella ginsengisoli LA-4 |
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| Institution: | 1. Renorbio/UECE, Av. Paranjana, 1.700, CEP 60740-000 Fortaleza, CE, Brazil;2. Department of Morphology and Animal Physiology, Universidade Federal Rural de Pernambuco-UFRPE, Av. Dom Manoel de Medeiros s/n, 52171-900 Recife, PE, Brazil;3. Institute for Biotechnology and Bioengineering, Centre of Biological Engineering, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal;4. Academic Unit of Garanhuns/UFRPE, Avenida Bom Pastor, s/n, Boa Vista, CEP: 55292-270 Garanhuns, PE, Brazil |
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| Abstract: | A novel meta-fission product hydrolase gene (mfphA) located in the bphX gene region of Dyella ginsengisoli LA-4 was successfully cloned and heterologously expressed in this study. The deduced amino acid sequence of MfphA showed 75% identity with the sequence of 2-hydroxymuconic semialdehyde hydrolase from Pseudomonas putida UCC22. The results suggested that MfphA belonged to the α/β hydrolase family, which could hydrolyze the meta-fission products (MFPs) during the biodegradation process of monocyclic compounds. The His-Tag MfphA was purified, and the subunit molecular mass of MfphA was about 35.3 kDa by SDS-PAGE analysis. According to the apparent kinetic parameters, the specificity of MfphA was determined in the following order: 6-methyl-HODA > HODA > 5-methyl-HODA > 6-phenyl-HODA > 5-chloro-HODA (HODA, 2-hydroxy-6-oxohexa-2,4-dienoate). The activity of MfphA for HODA was higher than that for 6-methyl-HODA. It was shown that the maximum activity was at 70 °C, and MfphA was stable for storage at low temperature for 30 days. |
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