Purification, characterisation and expression in Saccharomyces cerevisiae of LipG7 an enantioselective, cold-adapted lipase from the Antarctic filamentous fungus Geomyces sp. P7 with unusual thermostability characteristics
| Autor: | Andrew D. Bates, Aneta Białkowska, Lesley A. Iwanejko, Marianna Turkiewicz, Mark C. Wilkinson, Tomasz Florczak, Maurycy Daroch |
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| Rok vydání: | 2013 |
| Předmět: |
Saccharomyces cerevisiae
Antarctic Regions Bioengineering Biology Polymerase Chain Reaction Applied Microbiology and Biotechnology Biochemistry Microbiology Transcriptome chemistry.chemical_compound Ascomycota Bacterial Proteins Enzyme Stability Cloning Molecular Lipase Thermostability Cloning Inverse polymerase chain reaction Fungi Stereoisomerism Hydrogen-Ion Concentration biology.organism_classification Adaptation Physiological Cold Temperature Kinetics chemistry biology.protein Pyrosequencing PMSF Biotechnology |
| Zdroj: | Enzyme and Microbial Technology. 53:18-24 |
| ISSN: | 0141-0229 |
| DOI: | 10.1016/j.enzmictec.2013.03.021 |
| Popis: | A lipase, LipG7, has been purified from the Antarctic filamentous fungus Geomyces sp. P7 which was found to be cold-adapted and able to retain/regain its activity after heat denaturation. The LipG7 exhibits 100% residual activity following 1h incubation at 100°C whilst simultaneously showing kinetic adaptations to cold temperatures. LipG7 was also found to have industrial potential as an enantioselective biocatalyst as it is able to effectively catalyse the enantioselective transesterification of a secondary alcohol. The LipG7 coding sequence has been identified and cloned using 454 pyrosequencing of the transcriptome and inverse PCR. The LipG7 protein has been heterologously expressed in Saccharomyces cerevisiae BJ5465 and shown to exhibit the same characteristics as the native protein. |
| Databáze: | OpenAIRE |
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