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CLPS


Official Full Name
CLPS
Background
Colipase is a protein co-enzyme required for optimal enzyme activity of pancreatic lipase. It is secreted by the pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by trypsin. Its function is to prevent the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides. In humans, the colipase protein is encoded by the CLPS gene.
Synonyms
CLPS; colipase; pancreatic colipase

Catalog
Product Name
EC No.
CAS No.
Source
Price
CatalogNATE-0144
EC No.
CAS No.
SourcePorcine pancrea...
Related Reading

Colipase belongs to the class of carboxyl ester hydrolases, which can gradually hydrolyze triglycerides into glycerol and fatty acids. Colipase exists in the tissues of animals, plants and microorganisms (such as mold, bacteria, etc.) containing fat. Including phosphatase, sterolase and carboxylesterase. Fatty acids are widely used in food, medicine, leather, daily chemical industry and so on.

CLPSFigure 1. Protein structure of colipase.

Source

Colipase is widely found in animals, plants and microorganisms. Plants that contain more Colipase are the seeds of oil crops, such as castor seeds and rapeseed. When the oil seeds germinate, colipase can cooperate with other enzymes to catalyze the decomposition of oils and fats to produce sugars, and provide rooting nutrients and energy necessary for germination; the animal body contains more colipase is the pancreas and adipose tissue of higher animals, contains a small amount of colipase in the intestinal fluid, used to supplement the insufficiency of pancreatic colipase for fat digestion in carnivorous animals The gastric juice contains a small amount of glyceryl butyrate. In the animal body, various colipases control the processes of digestion, absorption, fat reconstruction and lipoprotein metabolism; the colipase content in bacteria, fungi and yeast is more abundant. Due to the variety of microorganisms, fast reproduction, and easy genetic variation, it has a wider range of action than animals and plants, the temperature range of action, and substrate specificity, and colipases derived from microorganisms are generally secreted extracellular enzymes. The main fermenting microorganisms are aspergillus niger, Candida, etc. It is suitable for large-scale industrial production and obtaining high-purity samples. Therefore, microbial Colipase is an important source of industrial colipase. In general, colipases from different sources have different characteristics and have important significance in theoretical research.

Classification

According to the specificity of colipase to substrate, it can be divided into three categories: fatty acid specificity, position specificity and stereospecificity. According to the different sources of colipase, colipase can also be divided into animal colipase, plant colipase and microbial colipase. Colipases from different sources can catalyze the same reaction, but when the reaction conditions are the same, the rate and specificity of the enzymatic reaction are not the same.

Property

Colipase is a class of enzymes with multiple catalytic capabilities that can catalyze the hydrolysis, alcoholysis, esterification, transesterification and reverse synthesis of esters of triacylglycerides and other water-insoluble esters It also shows the activity of other enzymes, such as lysophospholipidase, cholesterol esterase, acyl peptide hydrolase activity, etc. The performance of different activities of colipase depends on the characteristics of the reaction system, such as promoting the hydrolysis of esters at the oil-water interface, and enzymatic synthesis and transesterification in the organic phase. The study of the properties of colipase mainly includes the optimal temperature and pH, temperature and pH stability, substrate specificity and so on. To date, a large number of microbial colipases have been isolated and purified, and their properties have been studied. They differ in molecular weight, optimal pH, optimal temperature, pH and thermal stability, isoelectric point, and other biochemical properties. In general, microbial colipases have a wider range of pH, temperature range, high stability and activity than animal and plant colipases, and they are specific to substrates. The catalytic property of colipase is that it has the largest catalytic activity at the oil-water interface. Water-soluble enzymes act on water-insoluble substrates, and the reaction is performed at the interface of two completely different phases separated from each other. This is a feature that distinguishes colipase from esterase. The substrate of esterase is water-soluble, and the most suitable substrate is an ester formed by short-chain fatty acid (≤C8).

Applications

Microbial colipases 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. Colipase can make food produce special milk flavor. Colipase 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. Hydrolysis catalyzed by colipase can accelerate the degreasing process.

Reference

  1. Murakami, M, et al. Phospholipase A2. Journal of Biochemistry. 2002, 131(3), 285-292.

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