Acinetobacter lipases: molecular biology, biochemical properties and biotechnological potential

Abstract

Lipases (EC 3.1.1.3) 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 primarily to investigations of their role in pathogenesis and their increasing use in biotechnological applications. 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 because 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 Acinetobacter have been isolated from a variety of sources and their lipases possess many biochemical properties similar to those that have been developed for biotechnological applications. This review discusses the biology of lipase expression in Acinetobacter, with emphasis on those aspects relevant to potential biotechnology applications.

SIFAT-SIFAT BIOKIMIAWI EKSTRAK KASAR LIPASE EKSTRASELULER DARI BAKTERI Azospirillum sp. JG3

“…Lipase mengkatalisis reaksi hidrolisis ester asam karboksilat atau reaksi sintesis monoester secara stereoselektif dan enantioselektif (Snellman and Colwell, 2004). Lipase merupakan enzim yang paling banyak digunakan sebagai katalis berbagai reaksi senyawa organik (Reetz, 2002).…”

Acinetobacter baumannii Is Dependent on the Type II Secretion System and Its Substrate LipA for Lipid Utilization and In Vivo Fitness

“…This difference is likely due to a reduction in secretion of LipA, as it has been shown that proper folding of LipA is required for the outer membrane translocation of LipA via the T2S system in Pseudomonas glumae (49). Members of lipase homology group I have been classified as serine hydrolases with active sites containing the residues Ser-His-Asp/Glu (50,51). Consistent with the overall high sequence homology, sequence alignments indicate that the A. baumannii LipA has the catalytic residues Ser-His-Asp (Fig.…”

Identification of amino acids involved in the hydrolytic activity of lipase LipBL from Marinobacter lipolyticus

“…Microbial esterases and lipases are valuable biocatalysts due to their broad substrate specificity and high chemo-, regioand stereoselectivity (Chahinian et al, 2005;Houde et al, 2004;Jaeger & Eggert, 2002;Park et al, 2009;Rodriguez et al, 2008;Snellman & Colwell, 2004). Thus, these enzymes are currently used as detergent additives, in the food and paper industries, and as enantioselective biocatalysts for production of fine-grade chemicals (Breuer et al, 2004;Hasan et al, 2006;Jaeger & Eggert, 2002;Jaeger & Holliger, 2010;Jaeger & Reetz, 1998;Snellman et al, 2002;Schmid et al, 2001).…”