Characterization of a novel alkaline esterase from Altererythrobacter epoxidivorans CGMCC 1.7731T
| Autor: | Ying-Yi Huo, Xue-Wei Xu, Zhen Rong, Shu-Ling Jian, Yue-Hong Wu |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Esterase Gene medicine.disease_cause Biochemistry Esterase Chromatography Affinity Substrate Specificity 03 medical and health sciences chemistry.chemical_compound Enzyme Stability medicine Glycerol Lipase Phylogeny Alphaproteobacteria chemistry.chemical_classification biology Molecular mass Chemistry Altererythrobacter epoxidivorans Esterases Temperature Substrate (chemistry) General Medicine Hydrogen-Ion Concentration 030104 developmental biology Enzyme Genes Bacterial Metals biology.protein Biotechnology |
| DOI: | 10.6084/m9.figshare.5568706 |
| Popis: | A novel esterase gene (e25) was identified from Altererythrobacter epoxidivorans CGMCC 1.7731T by genome sequence screening. The e25 gene is 948 nucleotides in length and encodes a 315 amino acid protein (E25) with a predicted molecular mass of 33,683 Da. A phylogenetic tree revealed that E25 belongs to the hormone-sensitive lipase (HSL) family of lipolytic enzymes. An activity assay of E25 showed that it exhibited the highest catalytic efficiency when using p-nitrophenyl caproate (C6) as a substrate. The optimum pH and temperature were determined to be approximately pH 9 and 45��C, and the Km and Vmax values were 0.12 mM and 1,772 ��mol/min/mg, respectively. After an incubation at 40��C for 80 min, E25 retained 75% of its basal activity. The enzyme exhibited good tolerance to metal cations, such as Ba2+, Ca2+, and Cu2+ (10 mM), but its activity was strongly inhibited by Co2+, Ni2+, Mn2+, and Zn2+. The E25 enzyme was stimulated by glycerol and retained over 60% of its basal activity in the presence of 1% Tween-80 and Triton X-100. Overall, the activity of E25 under alkaline conditions and its organic solvent and detergent tolerance indicate that E25 could be useful as a novel industrial catalyst in biotechnological applications. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|