Abstrait

Structural homogeneity in microbial lipases.

Swati V, Gautam KM, Rajender K

Enzyme lipase (triacylglycerol hydrolases E.C.3.1.1.3) catalyzes the hydrolysis of triacylglycerols to glycerol and free fatty acids. In recent years, progressively more consideration is being rewarded to lipases produced by microorganisms. In nature, some of the most important lipase-producing bacteria are Pseudomonas, Bacillus, Staphylococcus, etc., and fungi are Rhizopus sp., Aspergillus, Penicillium, Geotrichum, Mucor, Rhizomucor, etc. [1,2]. The bacterial lipases from Bacillus sp. exhibit interesting properties that make them potential candidates for biotechnological applications [1-3]. Bacillus alcalophilus are the most common lipase producing strains. Lipases are classified into different families based on the amino-acid sequences similarity and their biological properties [4]. Microbial lipases are relatively stable and are capable of catalyzing a variety of reactions; they hold immense potential for diverse industrial applications.