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Unformatted text preview: REVIEW PAPER Erick A. Snellman Æ Rita R. Colwell Acinetobacter lipases: molecular biology, biochemical properties and biotechnological potential Received: 12 March 2004/ Accepted: 8 August 2004/Published online: 16 September 2004 Ó Society for Industrial Microbiology 2004 Abstract Lipases (EC 126.96.36.199) have received increased attention recently, evidenced by the increasing amount of information about lipases in the current literature. The renewed interest in this enzyme class is due pri- marily to investigations of their role in pathogenesis and their increasing use in biotechnological applica- tions . Also, many microbial lipases are available as commercial products, the majority of which are used in detergents, cosmetic production, food ﬂavoring, and organic synthesis. Lipases are valued biocatalysts be- cause they act under mild conditions, are highly stable in organic solvents, show broad substrate specificity, and usually show high regio- and/or stereo-selectivity in catalysis. A number of lipolytic strains of Acineto- bacter have been isolated from a variety of sources and their lipases possess many biochemical properties sim- ilar to those that have been developed for biotechno- logical applications. This review discusses the biology of lipase expression in Acinetobacter , with emphasis on those aspects relevant to potential biotechnology applications. Keywords Acinetobacter Æ LipA Æ Lipase Æ Biocatalysts Introduction Lipases (EC 188.8.131.52) are best defined as carboxyles- terases that catalyze both the hydrolysis and synthesis of long-chain acylglycerols . True lipidic substrates are insoluble in water, and lipases commonly show activation upon contact with substrate micelles or emulsions, although they may also hydrolyze more soluble acylglycerols or monoester substrates. Micro- bial lipases have been studied for their role in viru- lence and their applications in biotechnology. Lipases are attractive biocatalysts because they act under extremely mild conditions, are stable in organic sol- vents, show low substrate specificity, and exhibit high regio- and/or enantioselectivity . Their use in chiral synthesis of various pharmaceuticals and agrochemi- cals is growing, as is their penetration into detergent and food commodity markets. Lipases also serve as model catalysts to develop strategies for enhancing substrate enantioselectivity via directed evolution [36, 38, 39]. This versatility enhances the possibility of success in further development of existing technolo- gies, as well as offering excellent promise for discov- eries with novel applications. Acinetobacter is a strictly aerobic, Gram-negative coccobacillus that is ubiquitous in geographical distri- bution. The genus is best known for its capacity for bioremediation of alkanes and aromatic hydrocarbons, as well as production of high molecular weight hetero- polysaccharides that act as powerful emulsifiers, many with high commercial potential [41, 62, 69]. Acineto- bacter...
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This note was uploaded on 12/13/2010 for the course GENETIK 12 taught by Professor Atillabasar during the Spring '10 term at Istanbul Technical University.
- Spring '10