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Creative Enzymes exceeds in hydrolases activity testing. Through the in-depth study of enzymology, our experts bring the most suitable method for triacylglycerol lipase to meet different demands. The results are given with the smart chromatograph, which guarantees precision and accuracy
Triacylglycerol lipase (EC 3.1.1.3) plays a key role in dietary fat absorption in the intestine. This enzyme converts insoluble long-chain triacylglycerol into diacylglycerol and carboxylate. The smaller and more polar product molecules are able to cross the enterocytes membrane when mixed with bile salts. Crystal structures of the human lipases have shown that the polypeptide chain is divided into two domains bearing specific functions. The N-terminal domain contains the catalytic triad and is responsible for triglyceride hydrolysis, whereas the C-terminal domain is involved in colipase binding.
Besides the role in triglyceride digestion through lipid emulsification and intestinal fat absorption, triacylglycerol lipase has various applications. In biotechnology, the enzyme can be used for hydrolysis and synthesis of various esters, mutagenic modification, and properties optimization. In biofuel production, this enzyme acts on degummed soybean oil, synthesizing lipase biodiesel. In food industry, it contributes to the improvement of food texture, flavor modification, and the production of fatty acids. Triacylglycerol lipase can also be used to remove fatty stains under conditions of a modern machine wash and in the alkaline environment. The extensive applications of this enzyme trigger an increasing number of related studies. However, because it acts only on an ester-water interface, ions, salts, and surfactants are often used to facilitate the enzymatic reaction and stabilize the enzyme. Thus, there may be interferences from many ingredients in the reaction mixture when testing the enzyme activity. Fully considering the influences from various factors, Creative Enzymes chooses the most suitable method to perform activity quantification by chromatographic assays.
Figure: The crystal structure of the pancreatic lipase-colipase complex.
Reference: van Tilbeurgh, H. et al. Nature 1992 359: 159-162.
The chromatographic assay is the most reliable method to achieve precise quantification of enzyme activity. With both the experienced enzymologists and the advanced equipment of Creative Enzymes, the results are of high reproducibility and less variations. In the future, Creative Enzymes will continue to be a strong supporter for your research.
Catalog | Product Name | EC No. | CAS No. | Source | Price |
---|---|---|---|---|---|
NATE-1753 | Native Aspergillus sp. Lipase (immobilized) | EC 3.1.1.3 | 9001-62-1 | Aspergillus sp. | Inquiry |
NATE-1752 | Native Aspergillus sp. Lipase (API) | EC 3.1.1.3 | 9001-62-1 | Aspergillus sp. | Inquiry |
EXWM-3455 | triacylglycerol lipase | EC 3.1.1.3 | 9001-62-1 | Inquiry | |
NATE-1621 | Immobilized Lipase-A from Serratia marcescens, Recombinant | EC 3.1.1.3 | 9001-62-1 | E. Coli | Inquiry |
NATE-1615 | Native wheat germ Lipase | EC 3.1.1.3 | 9001-62-1 | Wheat germ | Inquiry |
NATE-1614 | Native Thermus flavus Lipase | EC 3.1.1.3 | 9001-62-1 | Thermus flavus | Inquiry |
NATE-1613 | Native Thermus thermophilus Lipase | EC 3.1.1.3 | 9001-62-1 | Thermus thermop... | Inquiry |
NATE-1612 | Native Rhizopus niveus Lipase | EC 3.1.1.3 | 9001-62-1 | Rhizopus niveus | Inquiry |
NATE-1611 | Lipase from Pseudomonas cepacia | EC 3.1.1.3 | 9001-62-1 | Pseudomonas cep... | Inquiry |
NATE-1610 | Native Aspergillus oryzae Lipase (Solution) | EC 3.1.1.3 | 9001-62-1 | Aspergillus ory... | Inquiry |
NATE-1609 | Native Mucor miehei Lipase | EC 3.1.1.3 | 9001-62-1 | Mucor miehei | Inquiry |
NATE-1608 | Native Aspergillus oryzae Lipase | EC 3.1.1.3 | 9001-62-1 | Aspergillus ory... | Inquiry |
NATE-1607 | Native Aspergillus niger Lipase | EC 3.1.1.3 | 9001-62-1 | Aspergillus nig... | Inquiry |
NATE-0406 | Lipase from Candida sp., Recombinant | EC 3.1.1.3 | 9001-62-1 | Aspergillus ory... | Inquiry |
NATE-0399 | Native Candida rugosa Lipase | EC 3.1.1.3 | 9001-62-1 | Candida rugosa | Inquiry |
NATE-0404 | Native Rhizopus oryzae Lipase | EC 3.1.1.3 | 9001-62-1 | Rhizopus oryzae | Inquiry |
NATE-0403 | Native Porcine Lipase | EC 3.1.1.3 | 9001-62-1 | Porcine pancrea... | Inquiry |
NATE-0402 | Native Penicillium camemberti Lipase | EC 3.1.1.3 | 9001-62-1 | Penicillium cam... | Inquiry |
NATE-0401 | Native Human Lipase | EC 3.1.1.3 | 9001-62-1 | Human pancreas | Inquiry |
NATE-0400 | Native Chromobacterium viscosum Lipase | EC 3.1.1.3 | 9001-62-1 | Chromobacterium... | Inquiry |
NATE-0405 | Lipase from Candida sp., Recombinant | EC 3.1.1.3 | 9001-62-1 | Aspergillus nig... | Inquiry |
NATE-0398 | Lipase B from Candida Antarctica, Recombinant | EC 3.1.1.3 | 9001-62-1 | Aspergillus ory... | Inquiry |
NATE-0397 | Lipase A from Candida Antarctica, Recombinant | EC 3.1.1.3 | 9001-62-1 | Aspergillus ory... | Inquiry |