Saturday, December 11, 2021

Lipase enzyme

Lipases (triacylglycerol ester hydrolase) are enzymes that catalyze the total or partial hydrolysis of fats and oils, releasing free fatty acids, diacylglycerols, monoacylglycerols and glycerol. Lipases occur widely in nature, but only microbial lipases are commercially significant.

Lipase was first discovered in pancreatic juice as an enzyme by Claude Bernard in 1856, which hydrolyzed unsolvable oil droplets and transformed them to soluble products. After that the productions of lipase have been observed in the bacteria Bacillus prodigiosus, B. pyocyaneus and B. fluorescens in 1901.

A true lipase will split emulsified esters of glycerine and long-chain fatty acids such as triolein and tripalmitin. Lipases, in thermodynamic favorable conditions (i.e., low water activity), catalyze a large variety of synthesis reactions which can be classified into two main types of reactions, i.e.,
*Esterification
*Transesterification

They do not require any cofactor and belongs to the class of serine hydrolases. Triglycerides hydrolyzed into diglycerides, monoglycerides, fatty acids, and glycerol by using the lipases naturally.

Esterification is the reaction where a fatty acid is linked, through the action of the enzyme, to an alcohol by a covalent bond, producing an ester and releasing a water molecule. Thioesterification and amidation are similar reactions but with a thiol or an amine as substrates.

Transesterification groups alcoholysis, acidolysis, aminolysis, and interesterification reactions.
The molecular weight of lipases is in the range of 19–60 kDa and reported to be monomeric protein. The position of the fatty acid in the glycerol backbone, chain length of the fatty acid, and its degree of unsaturation are the factors and the physical properties of lipases depend on it.

The many applications of lipases include speciality organic syntheses, hydrolysis of fats and oils, modification of fats, flavor enhancement in food processing, resolution of racemic mixtures, and chemical analyses.

In the food industry, lipases can be used as flavor modifiers by synthesis of short chain fatty acids esters and alcohols, and to obtain products of increased nutritional value by modifying the triacylglycerol structure for inter- or transesterification. In bakery, lipases are potential candidate substitutes for emulsifiers.

Microbial lipases are produced mostly by submerged culture, but solid-state fermentation methods. Lipase production is influenced by the type and concentration of carbon and nitrogen sources, the culture pH, the growth temperature, and the dissolved oxygen concentration.
Lipase enzyme

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