Directory Image
This website uses cookies to improve user experience. By using our website you consent to all cookies in accordance with our Privacy Policy.

An Important Enzyme—Lipase

Author: Iva Colter
by Iva Colter
Posted: Feb 09, 2023

Lipase (glyceride hydrolase) belongs to the class of carboxyl ester hydrolase, which can gradually hydrolyze triglycerides into glycerol and fatty acids. Lipase exists in fat-containing animal, plant and microbial (such as mold, bacteria, etc.) tissues. Including phosphatase, sterolase and carboxylesterase. Fatty acids are widely used in food, medicine, leather, daily chemicals, etc.

Lipases are widely present in animals, plants and microorganisms. Plants containing more lipase are seeds of oil crops, such as castor bean and rapeseed. When oil seeds germinate, lipase can cooperate with other enzymes to catalyze the decomposition of oils and fats to produce sugars, and provide nutrients and energy necessary for seed rooting and germination. The pancreas and adipose tissue of higher animals contain more lipases in animals. The intestinal juice contains a small amount of lipase, which is used to supplement the insufficiency of pancreatic lipase for fat digestion, and the gastric juice of carnivorous animals contains a small amount of butyric acid glyceryl esterase.

Properties of lipase

Lipase is a class of enzymes with a variety of catalytic abilities, which can catalyze the hydrolysis, alcoholysis, esterification, transesterification and reverse synthesis of esters of triacylglycerides and other water-insoluble esters. In addition, it also shows the activities of other enzymes, such as phospholipase, lysophospholipase, cholesterol esterase, acyl peptide hydrolase activity, etc. The different activities of lipase depend on the characteristics of the reaction system, such as promoting ester hydrolysis at the oil-water interface, and enzymatic synthesis and transesterification in the organic phase.

The properties of lipase mainly include the optimum temperature and pH, temperature and pH stability, and substrate specificity. So far, a large number of microbial lipases have been separated and purified, and their properties have been studied. They are different in molecular weight, optimum pH, optimum temperature, pH and thermal stability, isoelectric point and other biochemical properties. In general, microbial lipases have a broader pH, temperature range, high stability and activity than animal and plant lipases, and are specific to substrates.

Lipase is one of the important types of industrial enzyme preparations, which can catalyze reactions such as lipolysis, transesterification, and ester synthesis. It is widely used in oil processing, food, medicine, daily chemical and other industries. Lipases from different sources have different catalytic characteristics and catalytic activities. Among them, the large-scale production of lipases with transesterification or esterification functions for organic phase synthesis is of great significance for the enzyme-catalyzed synthesis of fine chemicals and chiral compounds.

The main use of lipase

Lipase from microbial sources can be used to enhance the flavor of cheese products. The limited hydrolysis of fat in milk can be used in the production of chocolate milk. Lipase can make food form a special milk flavor.

Lipase can prevent the taste of baked goods by releasing monoglycerides and diglycerides. The degreasing of bones in the production of gelatin needs to be carried out under mild conditions, and the hydrolysis catalyzed by lipase can accelerate the degreasing process.

About the Author

Creative Enzymes is a remarkable supplier and manufacturer in the Enzymology field. If you want to learn more information about Creative Enzymes, please visit us at https://www.creative-enzymes.com

Rate this Article
Leave a Comment
Author Thumbnail
I Agree:
Comment 
Pictures
Author: Iva Colter

Iva Colter

Member since: Apr 29, 2019
Published articles: 102

Related Articles