Open AccessMicrobial lipases and their applications – a review
Author(s) -
Saba Shamim,
Unsa Liaqat,
Abdul Rehman
Publication year - 2018
Publication title -
abasyn journal of life sciences
Language(s) - English
Resource type - Journals
eISSN - 2663-1040
pISSN - 2616-9754
DOI - 10.34091/ajls.1.2.2
Subject(s) - lipase , biotransformation , hydrolysis , glycerol , enzyme , biochemistry , transesterification , glyceride , microorganism , chemistry , food science , biology , bacteria , fatty acid , catalysis , genetics
This review focuses on the key aspects of lipases. Lipases (EC 3.1.1.3) aretriacylglycerol acylhydrolases that act on carboxylic ester bonds. Theybreakdown triacylglycerides into glycerides (diglycerides ormonoglycerides), fatty acids and glycerol. Their mass ranges from 19 kDafor B. stratosphericus to 92 kDa for P. gessardii. Their optimumtemperature and pH ranges from 15 °C to 80 °C for Acinetobacter sp. andJanibacter sp. and 5 to 11 for P. gessardii and E. faecium respectively.Lipases chemo-, regio-, and enantio- specific features make them firstchoice of enzymes in research. Their kinetics for substrate hydrolysisdepends on different esters. Mostly lipases are extracellular. Type 1secretory system (T1SS) and Type 2 secretory system (T2SS) are involvedin secreting lipases to external medium. They are found in eukaryotesand prokaryotes including animals, plants and microorganisms.Moreover, bacterial and fungal enzymes have diverse industrialapplications in food, health, pharmaceutical, medical, textile, detergent,cosmetic and paper industries. Genetic engineering is employed toimprove the properties of lipases. Their increasing demand in market hasmade them a hot topic in scientific research. Scientists are trying todiscover novel lipase producing microorganisms due to their expandingcommercial value.Keywords: Lipases, esterification, transesterification, biochemical andphysicochemical properties, recombinant DNA technology