G. Soberonchavez et B. Palmeros, PSEUDOMONAS LIPASES - MOLECULAR-GENETICS AND POTENTIAL INDUSTRIAL APPLICATIONS, Critical reviews in microbiology, 20(2), 1994, pp. 95-105
Lipases are esterases able to hydrolyze water-insoluble esters such as
long-chain triglycerides. These enzymes also catalyze the formation o
f esters (esterification) and the exchange of ester bonds (transesteri
fication) when present in nonaqueous media. Lipases display a high deg
ree of specificity and enantioselectivity for esterification and trans
esterification reactions, and thus their potential uses in industry ar
e very wide. These potential industrial applications have been an impo
rtant driving force for lipase research during the last several years,
and in particular for the study of lipases produced by microorganisms
. Pseudomonas lipases are very interesting because they display specia
l biochemical characteristics not common among the lipases produced by
other microorganisms, such as their thermoresistance and activity at
alkaline pHs. Recently, several Pseudomonas genes have been cloned and
sequenced, and the regulation of their expression is beginning to be
understood. The molecular genetic approach to the study of Pseudomonas
lipases will permit the construction of recombinant strains with incr
eased lipase productivity and will provide the opportunity to modify t
hese enzymes to suit particular industrial applications.