Open AccessScreening for Thermostable Esterases: From Deep Sea to Industry
Author(s) -
Ravot G.,
Buteux D.,
FavreBulle O.,
Wahler D.,
Veit T.,
Lefèvre F.
Publication year - 2004
Publication title -
engineering in life sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.547
H-Index - 57
eISSN - 1618-2863
pISSN - 1618-0240
DOI - 10.1002/elsc.200402149
Subject(s) - thermophile , esterase , chemoselectivity , biocatalysis , archaea , directed evolution , biochemistry , enzyme , organic synthesis , chemistry , biology , biochemical engineering , microbiology and biotechnology , computational biology , gene , catalysis , engineering , ionic liquid , mutant
Abstract Lipases/esterases represent one of the most important classes of industrial biocatalysts due to their ability to catalyze reactions in organic media. These enzymes fulfill many important industrial specifications such as chemoselectivity, regioselectivity and stereoselectivity. The recent use of thermostable enzymes opens novel perspectives in applications involving poorly soluble substrates (or products), such as the synthesis of specialty intermediates for cosmetics. In order to discover novel thermostable esterases we have screened various thermophilic microorganisms selected within the Archaea and the Bacteria domains using CLIPS‐O™ substrates. One of these strains which showed activity at very high temperature was selected and the corresponding esterase gene was cloned and characterized. After recombinant expression optimization, a complete production process of this thermophilic esterase was developed, turning a ‘gene discovery’ into a biocatalyst available for industry.