Lipases enzymatic activity

An example of the appropriate application of organically-modified silica precursors is alkoxides with an alkyl group. When methyltrimethoxy- or methyl-triethoxysilane (Figure 3.2) was added in formulations to increase the hydro-phobicity of ORMOSILs, it resulted in a better enzymatic activity of lipases immobilized in the alkyl-modified silica than in a hydrophilic matrix fabricated by means ofTEOS alone [51,80,129-133]. Similarly, an increased stability of lipase from Candida antarctica B was observed after its immobilization in a silica matrix... 

Y. Kakizawa, K. Akiyoshi, K. Nakamura, and J. Sunamoto, in Enzymatic Activity of Lipase Complexed with Nanoparticle of Hydrophobized Polysaccharide, Kyoto, Japan, 1998, p. III-806. Society of Polymer Science, Japan (Spsj). 

The second reaction studied using lipase as catalyst was the reversible re-gioselective esterification of propionic acid and 2-ethyl- 1,3-hexanediol [180]. While the previously described reaction was almost irreversible, this reaction is equilibrium limited with an apparent equilibrium constant of 0.6 0.1. In addition, the accumulated water inhibits the enzyme. Therefore, only the removal of the water from the reaction zone assures high enzymatic activity as well as drives the reaction beyond thermodynamic equilibrium. Experiments with two... 

Saario SM, Savinainen JR, Laitinen JT, Jarvinen T, Niemi R (2004) Monoglyceride lipase-like enzymatic activity is responsible for hydrolysis of 2-arachidonoylglycerol in rat cerebellar membranes. Biochem Pharmacol 67(7) 1381-7... 

Hydrolytic activities of free and immobilized lipase were assayed by the olive oil emulsion method according to the modification proposed by Soares et al. (11). One unit of enzyme activity was defined as the amount of enzyme that liberated 1 imol of free fatty acid/min under the assay conditions (37°C, pH 7.0,150 rpm). Analyses of hydrolytic activities carried out on the lipase loading solution and immobilized preparations were used to determine the activity-coupling yield (r %), which measures the recovered enzymatic activity according to Eq. 1 ... 

Muzzarelli RAA (1997) Human enzymatic activities related to the therapeutic administration of chitin derivatives. Cell Mol Life Sci 53 131-140 Muzzarelli RAA, Xia W, Tomasetti M and Ilari P (1995) Depolymerization of chitosan and substituted chitosans with the aid of a wheat germ lipase preparation. Enz Microbial Tech 17 541-545... 

Houlihan, A.V. 1992. Enzymatic activity other than lipase. Bulletin 271, pp. 21-25, International Dairy Federation, Brussels. 

To restore nutrient digestion in exocrine pancreatic insufficiency, sufficient enzymatic activity must be administered into the duodenal lumen simultaneously with meal substrates. Intraluminal lipid digestion in postprandial chyme requires lipase activity of at least 40-60 IU/mL throughout the digestive period, which translates into 25,000 to 40,000 IU intraduodenal lipase for digestion of a regular meal. Because plain enzyme preparations undergo rapid lipase inactivation due to acid and proteolytic destruction, it is necessary to administer up to 10-fold more lipase orally to achieve these quantities within the duodenum. 

Not all ILs are good solvents for proteins, however. There is the interesting example of lipase. Lipase is soluble in both aqueous and organic solvents, so it can be easily solubilized in ILs. Certain lipases even become dispersed or dissolved in some ILs. Since lipase is a very stable enzyme, it catalyzes the hydrolysis of lipids. Enzymatic activity is reported to be maintained in ILs [1]. There is not much published on the solubilization of biomaterials in ILs. In the present chapter we introduce a procedure to use in solubilizing biomaterials in ILs. First we consider the preparation of the IL, and then the chemical modification of biomaterials suitable for dissolution. We have found this procedure helpful when we tried to use electrochemicaUy active biomaterials in ILs. 

It is generally stated that biocatalysis in organic solvents refers to those systems in which the enzymes are suspended (or, sometimes, dissolved) in neat organic solvents in the presence of enough aqueous buffer (less than 5%) to ensure enzymatic activity. However, in the case of hydrolases water is also a substrate and it might be critical to find the water activity (a ) value to which the synthetic reaction (e.g. ester formation) can be optimized. Vahvety et al. [5] found that, in some cases, the activity of Candida rugosa lipase immobihzed on different supports showed the same activity profile versus o but a different absolute rate. With hpase from Burkholderia cepacia (lipase BC), previously known as lipase from Pseudomonas cepacia, and Candida antarctica lipase B (CALB) it was found that the enzyme activity profile versus o and even more the specific activity were dependent on the way the enzyme was freeze dried or immobihzed [6, 7]. A comparison of the transesterification activity of different forms of hpase BC or CALB can be observed in Tables 5.1 and 5.2, respectively. 

Sol-gel matrices can also provide a chemical surrounding that favors enzymatic reactions. Lipases act on ester bonds and are able to hydrolyze fats and oils into fatty acids and glycerol. These are interphase-active enzymes with lipophilic domains and the catalytic times reaction occurs at the water-lipid interface. Entrapped lipases can be almost 100 times more active when a chemically modified silica matrix is used. The cohydrolysis of Si(OMe)4 and RSi(OMe)3 precursors provides alkyl groups that offer a lipophihc environment that can interact with the active site of Upases and increase their catalytic activity. Such entrapped lipases are now commercially available and offer new possibilities for organic syntheses, food industry, and oil processing. ... 

An industrially significant application of the tailored enzymatic activity was reported by Gonzalez and Braco [22]. A bio-imprinted lipase was employed for the... 

D. Colipase aids pancreatic lipase. It does not have enzymatic activity. 

Continuous assays are rarely described for lipases, but are frequently described for esterases. Similar to lipases, esterases hydrolyze ester bonds. However, in contrast to lipases, their substrates are water-soluble and thus water-soluble fluorescent substrates can be used to measure their enzymatic activity. Some of these water-soluble substrates have been proposed for the measurement of lipolytic ac-... 

Enzymatic Activity and Effects on Cellular Lipid Metabolism of Endothelial Lipase... 

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