An Introduction to Lipase

by Adebayo Osesusi

Lipases are a group of water-soluble enzymes that catalyze the hydrolysis (and synthesis) of ester bonds in insoluble acylglycerols at lipid-water interfaces. Lipases hydrolyze triacylglycerides into  diacylglycerides, monoacylglycerides, free fatty acids  and glycerols. Lipase reaction occurs at the  interface between the aqueous and the oil phases  because of an opposite polarity between the enzyme  (hydrophilic) and their substrates (lipophilic).

Lipases are ubiquitous in nature, that is, they are found in plants, animals and microorganisms.  Lipases from microbial sources are of considerable commercial importance because of their high versatility and stability; moreover, they have the advantage of being readily produced in high yields, of which bacterial lipases are more  economical and stable. Bacterial lipases are mostly inducible enzymes, requiring some form of oil, fatty acid, fatty  acid alcohol or fatty acid ester for their induction. Although there are reported cases of constitutive lipase production by bacteria and they are non-specific in  their choice of substrate with a few being thermostable

Such features are responsible for lipases being extensively used for biotechnological  applications in the food technology, dairy industry,  cosmetics, textile and detergent industries. In the food industry, lipases play a vital role  during the fermentative steps of sausage manufacture  and to determine changes in long-chain fatty acids  liberated during ripening. Lipases remain enzymatically  active in organic solvents which enhances their potential and  flexibility as biocatalysts against a wide range of  unnatural substrates. 


Also, they are known to catalyze other reactions like esterification,  trans-esterification and inter-esterification between a  fatty acid and an alcohol which are the reverse reactions  of hydrolysis, making them the most widely used biocatalysts in organic chemistry. In addition to lipases, esterases are also grouped into hydrolases and these two enzymes can often be confused with each other, but they are really different from each other in terms of substrate  specificity.

Lipases have been observed to be monomeric  proteins, with molecular weight in the range of 19-60  kDa. Generally, bacterial lipases have neutral or alkaline pH value and show activity in a broad pH  range (pH 4 to pH 11). The thermal stability of lipases range from 20oC to 60oC. Lipase activity depends on the presence of large surface area  and requires mild to extreme conditions, with stability  in organic solvents a desirable property in synthetic  reactions. 

Most known bacterial lipases are stable in  organic solvents. The ability of  lipases to remain stable in organic solvent without any stabilizer has been found to be in favour of some  reactions, highlighting various  biotechnological applications of lipases such as the  synthesis of chirally important drugs and drug  intermediates. Reactions catalyzed  by lipases usually occur in organic-aqueous interfaces  which is desirable because this ensures the separation of enzyme from substrates or products easily, thus a reduction in cost during downstream processing, which is a highly desired feature in bioprocess engineering.  

Adebayo Osesusi is our consultant on industrial biotechnology in MicroBiotics. To get in touch with him, kindly visit our industrial biotechnology page.

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Updated: January 31, 2021 — 11:12 am

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