Lipase components

Pancreatic enzyme doses are initiated at 500 to 1000 units/kg per meal of lipase component with half-doses given with snacks. Infants are typically started at 1500 to 2500 units of... 

The temperature optimum for interesterification is 85°C or higher, and the half-life in continuous acidolysis of spy bean oil with lauric acid at 60°C is above 2500 h. The non-specificity makes the catalyst useful in random interesterification of different fats. The catalyst has some saturated fatty acid specificity. Two lipase components (A and B) were purified. Lipase A is important for interesterification, and Lipase B is important in ester synthesis. 

Purification of the Lipase Components. Two lipase components, designated A and B, respectively, have been purified from the crude C. antarctica lipase preparation by well-known chromatographic techniques (8). The crude lipase preparation may contain other lipases, but we consider lipases A and B to be the important ones. 

The hydrolytic activities of the two lipase components on olive oil, diolein, and methylesters have been compared (Table VI). 

Table VII. Acidolytic Activity of Immobilized Lipase Components...

The non-specificity indices of the lipase components have been measured (Table VIII). 

The activities of the immobilized lipase components in ester synthesis have also been tested. Myristic acid was esterified with propanol, isopropanol, and oleic alcohol, respectively (Table X). 

The given examples of the actions of the lipase components allow one to give a summary of the contribution of the components to the qualities of the immobilized crude enzyme (Table XI). 

Optically Active Acids and Esters. Enantioselective hydrolysis of esters of simple alcohols is a common method for the production of pure enantiomers of esters or the corresponding acids. Several representative examples are summarized ia Table 4. Lipases, esterases, and proteases accept a wide variety of esters and convert them to the corresponding acids, often ia a highly enantioselective manner. For example, the hydrolysis of (R)-methyl hydratropate [34083-55-1] (40) catalyzed by Hpase P from Amano results ia the corresponding acid ia 50% yield and 95% ee (56). Various substituents on the a-carbon (41—44) are readily tolerated by both Upases and proteases without reduction ia selectivity (57—60). The enantioselectivity of many Upases is not significantly affected by changes ia the alcohol component. As a result, activated esters may be used as a means of enhancing the reaction rate. 

In addition to having the required spedfidty, lipases employed as catalysts for modification of triglycerides must be stable and active under the reaction conditions used. Lipases are usually attached to supports (ie they are immobilised). Catalyst activity and stability depend, therefore, not only on the lipase, but also the support used for its immobilisation. Interesterification reactions are generally run at temperatures up to 70°C with low water availability. Fortunately many immobilised lipases are active and resistant to heat inactivation under conditions of low water availability, but they can be susceptible to inactivation by minor components in oils and fats. If possible, lipases resistant to this type of poisoning should be selected for commercial operations. 

Within the small intestine, bile-acid binding interferes with micelle formation. Nauss et al. [268] reported that, in vitro, chitosan binds bile acid micelles in toto, with consequent reduced assimilation of all micelle components, i.e., bile acids, cholesterol, monoglycerides and fatty acids. Moreover, in vitro, chitosan inhibits pancreatic lipase activity [269]. Dissolved chitosan may further depress the activity of lipases by acting as an alternative substrate [270]. 

The outstanding influence of the anionic component on the activity and selectivity of enzymes was demonstrated in the Candida rugosa lipase-catalyzed kinetic resolution of ibuprofen, a nonsteroidal antiinflammatory drug with sales of USD 183 million in 2006 (Scheme 5.15) [63]. 

With few exceptions, small particles of vegetable foods are generally stripped of their more accessible nutrients during digestion in the GI tract. In this way starch, protein, fat and water-soluble small components (sugars, minerals) are usually well absorbed. This is not always the case, however, for larger food particles or for molecules that cannot diffuse out of the celF tissue. Neither is it the case for the lipid-soluble components. These need to be dissolved in lipid before they can be physically removed from the cell to the absorptive surface, since the cell wall is unlikely to be permeable to lipid emulsions or micelles, and the presence of lipases will strip away the solvating lipid. 

Irrespective of the physical form of the carotenoid in the plant tissue it needs to be dissolved directly into the bulk lipid phase (emulsion) and then into the mixed micelles formed from the emulsion droplets by the action of lipases and bile. Alternatively it can dissolve directly into the mixed micelles. The micelles then diffuse through the unstirred water layer covering the brush border of the enterocytes and dissociate, and the components are then absorbed. Although lipid absorption at this point is essentially complete, bile salts and sterols (cholesterol) may not be fully absorbed and are not wholly recovered more distally, some being lost into the large intestine. It is not known whether carotenoids incorporated into mixed micelles are fully or only partially absorbed. 

The anaerobic biological conversion of the major polymeric components of MSW identified require appropriate microorganisms and hydrolytic enzyme systems. Extracellular hydrolytic enzymes, such as cellulases and lipases, have been shown to be effective in the post hydrolysis of anaerobic digester efQuent solids 34) or pretreatment of complex organic polymers before the digestion process 48),... 

A novel continuous-flow SCCO2 process for the kinetic resolution of 1-phenyethanol enantiomers (Figure 30) using Novozym 435 immobilized enzyme from Candida antarctica was described by Matsuda et al. [51], The lipase enzyme, selectively acetylated the R)-alcohol component. A mixture of starting material and vinyl acetate was passed through the enzyme with supercritical carbon-dioxide (Figure 31). The reaction zone was pressurized and heated, so the reaction could be performed imder supercritical conditions, synthesizing the desired (i )-acetate with 99.7% ee. and 47% yield. 

The effects of chemical structure of diisocyanate component on the hydrolysis of polyurethanes by R. delemar lipase were examined (Figure 8). The rates of hydrolysis of the polyurethanes containing MDI or tolylene-2,U-diisocyanate (TDI) were smaller than that of the polyurethane containing 1,6-hexamethylene-diisocyanate (HDI). 

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