Lipase powdered

The microbial lipolytic activity is determined by comparing the rate at which a solution of microbial lipase powder hydrolyzes a substrate of olive oil emulsion... 

Yamane, T., Ichiryu, T., Nagata, M., Ueno, A., and Shimizu, S., Intramolecular esterification by lipase powder in microequeous benzene factors affecting activity of pure enzyme, Biotechnol. Bioeng., 36, 1063-1069, 1990. 

The microbial lipolytic activity is determined by comparing the rate at which a solution of microbial lipase powder hydrolyzes a substrate of olive oil emulsion with the rate at which a solution of microbial lipase F.I.P. standard hydrolyzes the same substrate under the same conditions. It should be clearly stated that a lipase of microbial origin is involved to prevent confusion with the assay for pancreatic lipase. 

SP 523 Lipase powder from Thermomy-ces lanuginosus (formerly Humi-cola lanuginosa) CHIRAZYME L-8, lyo Roche Diagnostics... 

SP 524 Lipase powder from Rhizomucor miehei, rec. in Aspergillus oryzae CHIRAZYME L-9, lyo Roche Diagnostics... 

For immobilization, the support 43 or support 45 was suspended by dissolving lipase powder in buffer solution, and incubated at 30 °C. The immobilized enzyme was lyophilized. The high thermal stability of P-CD polymer is due to its crosslinking it is known that crosslinking results in increased thermal stability. 

Only one detergent lipase, ie, Lipolase introduced by Novo in 1988, has been marketed. The first household powder detergent containing Upase was introduced in Japan in the same year in Europe and the United States in 1990—1991. Lipase is often incorporated into the new compact powder formulations. 

Crude powder lipase from Pseudomonas cepecia Asymmetrical hydrolysis of ( + )l-chloro-2-acetoxy-3-(l-naphthyloxy)-propane T etrahydrofuran- phosphate buffer pH 7.1 (1 /3) No lag period observed for the product formation 8... 

Oral pancreatic enzyme supplements are available as powders, uncoated or coated tablets, capsules, enteric-coated spheres and microspheres, or enteric-coated microtablets encased in a cellulose or gelatin capsule (Table 28-2). Microencapsulated enteric-coated products are not superior to recommended doses of conventional non-enteric-coated enzyme preparations. The quantity of active lipase delivered to the duodenum appears to be a more important determinant in pancreatic enzyme replacement therapy than the dosage form. GI side effects appear to be dose related but occur less frequently with enteric-coated products. 

Performing a systematic comparison of lipase-catalyzed kinetic resolutions of several seeondaiy aleohols in continuous flow mode (Figure 7) and shake flask batch mode using immobilized and non-mobilized lipases was reported by Csajagi and eo-workers [25]. The results indieated that immobilized as well as lyophilized powder forms of liphases can be effeetively used in eontinuous flow mode kinetie resolutions of raeemic alcohols in non-aqueous solvent systems. The produetivity of the lipases was higher in continuous flow reactors than in batch mode systems, whereas the enantiomer selectivities were similar. 

The particle size of each polyester powder was ranked A, B, C, D, or E, corresponding respectively to roughly less than 0.25 mm, less than 0.50 mm, less than 1.0 mm, 0.25-1.5 mm, 0.25-3 mm. Each reaction mixture contained ioo p mol of phosphate buffer (pH T.O), 1 mg of surfactant Plysurf A210G, 300 mg of the polyester powder and 60 y g of R. arrhizus lipase (or 300 pg of R. delemar lipase) in a total volume of 10.0 ml. In the case of R. delemar lipase, surfactant was omitted and pH of phosphate buffer was 6.0. In the substrate and enzyme controls, enzyme or substrate was omitted from the reaction mixture. 

Effect of the Particle Size of PEA Powders on the Hydrolysis by R. delemar Lipase. In the case of PEA, small particles were hydrolyzed better than large ones as shown in Figure 3. So it was assumed that the enzymatic hydrolysis depends on the amounts of surface area of polyester powders. 

Figure 3. Effect of the particle size of PEA powders on the hydrolysis by R. delemar lipase. Reaction mixtures were incubated at 30 °C. Particle size -0-, 0-0.25 mm 0-1.00 mm,...

Figure 9 Effect of molar ratio of PCL and aromatic polyester on the biodegradability of CPE by R. dememar lipase, (a), (b), and (c) indicate PCL-PETG, PCL-PBT, and PCL-PEIP systems, respectively. Each reaction mixture for biodegradability assay contained CPE powder or its films ( 20 mg as polyester moiety) in a total volume of 1.0 ml. Reaction mixtures were incubated at 37 °C for l6 hours. Formation of the water-soluble TOC was in proportion to substrate amounts (up to 50 mg as PCL moiety) in this reaction system. (Reproduced from Reference l6. Copyright 1981 John Wiley. )...

Gitlesen, T., Bauer, M. and Adlercreutz, P. (1997) Adsorption of lipase on polypropylene powder. Biochemica et Biophysica Acta-Lipids and Lipid Metabolisme, 1345, 188-196. 

Biological detergents and washing powders use lipase enzymes to break down fats, and protease enzymes that hydrolyze proteins from food stained fabrics. 

Oral Tablets, powder, or delayed-release capsules containing varying amounts of lipase, protease, and amylase activity. See manufacturers literature for details. 

Although rancidity is a serious defect in market milk, it has also been utilized profitably. Whole milk powder made from lipase-modified milk has generally been accepted by chocolate manufacturers. It is used as a partial replacement for whole milk because it imparts a rich, distinctive flavor to milk chocolate, other chocolate products like fudge, and compound coatings, caramels, toffees, and butter creams (Ziemba 1969). 

Dissolve powders in warm water, add 0.8 M phosphate buffer (pH 8.0) and lipase, shake for 5 min. Incubate tubes at 37°C for 2 h in an ultrasonic bath, cool. Add EtOH/MeOH (95 5) + solid K,C03 + cholesteryl phenylacetate (internal standard) and extract twice with hexane. 

The lipase used was isolated from Pseudomonas tluorescens and was commercially available from Amano International Enzyme Co., Inc. (Troy, VA) as a powder, specific activity 32,000 units/g (P-30). 

Lipase was immobilized by ADS on the support following the methodology of Pereira et al. (10) with slight modifications. Pure silica (1 g dry wt) was soaked previously in hexane under agitation (100 rpm) for 1 h. Excess hexane was then removed with a 10 mLpipet, and 0.3 g of powdered lipase dissolved in 10 mL of distilled water was added. The fixation of lipase onto the support was performed under agitation for 3 h at room temperature and followed by an additional period of 18 h under static conditions at 4°C. The derivative was filtered (Whatman filter paper no. 41) and thoroughly rinsed with hexane. 

A = activity of pancreas powder (amylase and lipase) BRP in Ph. Bur. Units per milligram... 

The lipases have been found to be concentrated in the cream on separation and in the curd on rennet-induced coagulation (Kishonti and Sjostrom, 1970 Driessen and Stadhouders, 1975 Stead, 1983). They can survive during the manufacture of dried milk (Shamsuzzaman et al., 1987) and cause lipolytic defects in a wide range of fat-containing foods in which milk powder is an ingredient (Stead, 1986). 

Chen, L., Daniel, R.M., Coolbear, T. 2003. Detection and impact of protease and lipase activities in milk and milk powders. Int.Dairy J. 13, 255-275. 

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