This title appears in the Scientific Report :
2014
Please use the identifier:
http://dx.doi.org/10.1007/s00253-014-5775-7 in citations.
A novel thermoalkalostable esterase from Acidicaldus sp. strain USBA-GBX-499 with enantioselectivity isolated from an acidic hot springs of Colombian Andes
A novel thermoalkalostable esterase from Acidicaldus sp. strain USBA-GBX-499 with enantioselectivity isolated from an acidic hot springs of Colombian Andes
Several thermo- and mesoacidophilic bacterial strains that revealed high lipolytic activity were isolated from water samples derived from acidic hot springs in Los Nevados National Natural Park (Colombia). A novel lipolytic enzyme named 499EST was obtained from the thermoacidophilic alpha-Proteobact...
Saved in:
Personal Name(s): | López, Gina |
---|---|
Chow, Jennifer / Bongen, Patrick / Lauinger, Benjamin / Pietruszka, Jörg / Streit, Wolfgang R. (Corresponding Author) / Baena, Sandra | |
Contributing Institute: |
Institut für Bioorganische Chemie (HHUD); IBOC Biotechnologie; IBG-1 |
Published in: | Applied microbiology and biotechnology, 98 (2014) 20, S. 8603 - 8616 |
Imprint: |
Berlin
Springer
2014
|
DOI: |
10.1007/s00253-014-5775-7 |
PubMed ID: |
24818691 |
Document Type: |
Journal Article |
Research Program: |
ohne Topic |
Publikationsportal JuSER |
Several thermo- and mesoacidophilic bacterial strains that revealed high lipolytic activity were isolated from water samples derived from acidic hot springs in Los Nevados National Natural Park (Colombia). A novel lipolytic enzyme named 499EST was obtained from the thermoacidophilic alpha-Proteobacterium Acidicaldus USBA-GBX-499. The gene estA encoded a 313-amino-acid protein named 499EST. The deduced amino acid sequence showed the highest identity (58 %) with a putative α/β hydrolase from Acidiphilium sp. (ZP_08632277.1). Sequence alignments and phylogenetic analysis indicated that 499EST is a new member of the bacterial esterase/lipase family IV. The esterase reveals its optimum catalytic activity at 55 °C and pH 9.0. Kinetic studies showed that 499EST preferentially hydrolyzed middle-length acyl chains (C6-C8), especially p-nitrophenyl (p-NP) caproate (C6). Its thermostability and activity were strongly enhanced by adding 6 mM FeCl3. High stability in the presence of water-miscible solvents such as dimethyl sulfoxide and glycerol was observed. This enzyme also exhibits stability under harsh environmental conditions and enantioselectivity towards naproxen and ibuprofen esters, yielding the medically relevant (S)-enantiomers. In conclusion, according to our knowledge, 499EST is the first thermoalkalostable esterase derived from a Gram-negative thermoacidophilic bacterium. |