Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0040822 (tremor)
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In situ adsorption, known as an in situ-roduct removal (ISPR) technique for low molecular mass bioproducts, was in this study applied to a bacterial exoenzyme proving that this method is also suitable for the separation of macromolecules like proteins. For this, adsorbent particles were added to growing cultures of Staphylococcus carnosus rec., therefore both production and adsorption occurred simultaneously in shaking flasks, stirred tank, or airlift bioreactor as the chosen types of fermenters. The exoenzyme lipase adsorbed rapidly and, after separating cells and adsorbents, desorbed in a packed bed column. Up to 85% of the produced lipase were recovered, fractions of these had been concentrated up to the factor 20 and purified up to a factor of 40 by the procedure. By using the airlift bioreactor an enhancement of biomass production was observed, but the necessity of the addition of an anti-foam reagent resulted in higher product losses in adsorption as well as in desorption. Production and adsorption kinetics have been modeled and applied to in situ-adsorption. The model was used to perform a parameter study in which the influence of biological and physical parameters as well as process parameters on discontinuous and continuous in situ-adsorption was investigated.
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PMID:Process modeling of in situ-adsorption of a bacterial lipase. 1626 49

Immobilized Candida antarctica lipase B (Novozym 435)-catalyzed enantioselective hydrolysis of D,L-phenylglycine methyl ester to enatiopure D-phenylglycine was successfully conducted in the systems with ionic liquids (ILs). Novozym 435 exhibited excellent activity and enantioselectivity in the system containing the IL BMIMxBF(4) compared to several typical organic solvents tested. It has been found that the cations and, particularly, the anions of ILs have a significant effect on the reaction, and the IL BMIMxBF(4), which shows to be the most suitable for the reaction, gave the highest initial rate and enantioselectivity among various ILs examined. The reaction became much less active and enantioselective in the systems with BMIMxHSO(4). Also, it was noticed that the enzymatic hydrolysis was strongly dependent on BMIMxBF(4) content in the co-solvent systems and the favorable content of the IL was 20% (v/v). Of the assayed four co-solvents and phosphate buffer, the lowest apparent K(m) and activation energy, and the highest V(max) of the reaction were achieved using 20% (v/v) BMIMxBF(4) co-solvent with phosphate buffer. Additionally, various influential variables were investigated. The optimum pH, substrate concentration, reaction temperature and shaking rate were 8.0, 80mM, 25-30 degrees Celsius and 150rpm, respectively, under which the initial rate, the residual substrate e.e. and the enantioselectivity were 2.46mM/min, 93.8% (at substrate conversion of 53.0%) and 38, respectively. When the hydrolysis was performed under reduced pressure, the initial rate (2.64mM/min) and the enantioselectivity (E=43) were boosted.
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PMID:Efficient enantioselective hydrolysis of D,L-phenylglycine methyl ester catalyzed by immobilized Candida antarctica lipase B in ionic liquid containing systems. 1656 44

alpha-chymotrypsin (CT) and lipase (LP) were immobilized in hierarchically-ordered mesocellular mesoporous silica (HMMS) in a simple but effective way for the enzyme stabilization, which was achieved by the enzyme adsorption followed by glutaraldehyde (GA) crosslinking. This resulted in the formation of nanometer scale crosslinked enzyme aggregates (CLEAs) entrapped in the mesocellular pores of HMMS (37 nm), which did not leach out of HMMS through narrow mesoporous channels (13 nm). CLEA of alpha-chymotrypsin (CLEA-CT) in HMMS showed a high enzyme loading capacity and significantly increased enzyme stability. No activity decrease of CLEA-CT was observed for 2 weeks under even rigorously shaking condition, while adsorbed CT in HMMS and free CT showed a rapid inactivation due to the enzyme leaching and presumably autolysis, respectively. With the CLEA-CT in HMMS, however, there was no tryptic digestion observed suggesting that the CLEA-CT is not susceptible to autolysis. Moreover, CLEA of lipase (CLEA-LP) in HMMS retained 30% specific activity of free lipase with greatly enhanced stability. This work demonstrates that HMMS can be efficiently employed as host materials for enzyme immobilization leading to highly enhanced stability of the immobilized enzymes with high enzyme loading and activity.
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PMID:Crosslinked enzyme aggregates in hierarchically-ordered mesoporous silica: a simple and effective method for enzyme stabilization. 1698 68

For the first time, lipozyme TL IM, an inexpensive lipase from Thermomyces lanuginosa, was successfully applied to the regioselective synthesis of lipophilic 5-fluorouridine ester derivatives. The ESI-MS and (13)C NMR analysis confirmed that the end products of the acylation were 5'-O-acyl 5-fluorouridines, more powerful anti-tumor drugs than 5-fluorouridine itself. Notably, the chain length of acyl donors had an obvious effect on the initial rate and the maximum substrate conversion of the regioselective acylation. The acylation of 5-fluorouridine with vinyl laurate was used as a model to explore the influence of various factors on the reaction with respect to the initial rate, the maximum substrate conversion and the regioselectivity. The optimum water activity, the molar ratio of vinyl laurate to 5-fluorouridine, reaction temperature and shaking rate were 0.07, 15/1, 45 degrees C and 200rpm, respectively, under which the maximum substrate conversion and the regioselectivity were as high as 98.4 and >99%, respectively, after a reaction time of around 6h.
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PMID:Novel and highly regioselective route for synthesis of 5-fluorouridine lipophilic ester derivatives by lipozyme TL IM. 1736 51

Comparative studies of lipase-catalyzed hydrolysis of soy oil in solvent-free system were carried out in shaking bath and in ultrasonic bath. A suitable ultrasonic power of 1.64 W cm(-2) was determined to guarantee satisfactory hydrolysis extent and lipase activity. The influence of temperature, pH, enzyme concentration and water/oil ratio was investigated subsequently. Compared with that in shaking bath, optimum temperature and inactivation temperature of lipase in ultrasonic bath were about 5-10 degrees C higher, while pH effect in ultrasonic bath was similar; ultrasound also led to a smooth increase of reaction rate at relatively higher enzyme loading and less use of water to saturate hydrolysis substrate. In optimum conditions, the overall hydrolysis reaction rate in the ultrasonic bath process was above 2-fold than that in the shaking bath process.
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PMID:The effect of ultrasound on lipase-catalyzed hydrolysis of soy oil in solvent-free system. 1799 68

Production of an extracellular lipase from Serratia marcescens ECU1010, which is an industrially important biocatalyst for the stereospecific synthesis of Diltiazem precursor, was carefully optimized in both shake flasks and a fermenter, using Tween-80 as the enzyme inducer. Dextrin and beef extract combined with ammonium sulfate were indicated to be the best carbon and nitrogen sources, respectively. With the increase of Tween-80 from 0 to 10 g l-1, the lipase production was greatly enhanced from merely 250 U l-1 to a maximum of 3,340 U l-1, giving the highest lipase yield of ca 640 U g-1 dry cell mass (DCW), although the maximum biomass (6.0 g DCW l-1) was achieved at 15 g l-1 of Tween-80. When the medium loading in shake flasks was reduced from 20 to 10% (v / v), the lipase production was significantly enhanced. The increase in shaking speed also resulted in an improvement of the lipase production, although the cell growth was slightly repressed, suggesting that the increase of dissolved oxygen (DO) concentration contributed to the enhancements of lipase yield. When the lipase fermentation was carried out in a 5-l fermenter, the lipase production reached a new maximum of 11,060 U l-1 by simply raising the aeration rate from 0.5 to 1.0 vvm, while keeping the dissolved oxygen above 20% saturation via intermittent adjustment of the agitation speed (> or =400 rpm), in the presence of a relatively low concentration (2 g l-1) of Tween-80 to prevent a potential foaming problem, which is easy to occur in the intensively aerated fermenter.
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PMID:Significant improvement of Serratia marcescens lipase fermentation, by optimizing medium, induction, and oxygen supply. 1802 76

Lipase production by Candida rugosa was carried out in submerged fermentation. Plackett-Burman statistical experimental design was applied to evaluate the fermentation medium components. The effect of twelve medium components was studied in sixteen experimental trials. Glucose, olive oil, peptone and FeCl3.6H2O were found to have more significance on lipase production by Candida rugosa. Maximum lipase activity of 3.8 u mL(-1) was obtained at 50 h of fermentation period. The fermentation was carried out at optimized temperature of 30 degrees C, initial pH of 6.8 and shaking speed of 120 r/min. Unstructured kinetic models were used to simulate the experimental data. Logistic model, Luedeking-Piret model and modified Luedeking-Piret model were found suitable to efficiently predict the cell mass, lipase production and glucose consumption respectively with high determination coefficient(R2). From the estimated values of the Luedeking-Piret kinetic model parameters, alpha and beta, it was found that the lipase production by Candida rugosa is growth associated.
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PMID:Evaluation of medium components by Plackett-Burman statistical design for lipase production by Candida rugosa and kinetic modeling. 1858 20

A purified alkaline thermo-tolerant bacterial lipase from Bacillus cereus MTCC 8372 was immobilized on a Poly (MAc-co-DMA-cl-MBAm) hydrogel. The hydrogel showed approximately 94% binding capacity for lipase. The immobilized lipase (2.36 IU) was used to achieve esterification ofmyristic acid and isopropanol in n-heptane at 65 degrees C under continuous shaking. The myristic acid and isopropanol when used at a concentration of 100 mM each in n-heptane resulted in formation of isopropyl myristate (66.0 +/- 0.3 mM) in 15 h. The reaction temperature below or higher than 65 degrees C markedly reduced the formation of isopropyl myristate. Addition of a molecular sieve (3 A x 1.5 mm) to the reaction mixture drastically reduced the ester formation. The hydrogel bound lipase when repetitively used to perform esterification under optimized conditions resulted in 38.0 +/- 0.2 mM isopropyl myristate after the 3rd cycle of esterification.
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PMID:Enzymatic synthesis of isopropyl myristate using immobilized lipase from Bacillus cereus MTCC 8372. 1880 May 97

Our previous work has indicated that enzymatic resolution of glycidyl butyrate are strongly affected by many factors, including concentration of substrate, amount of lipase, the temperature, pH, shaking speed and reaction time. In this study, Plackett-Burman design was undertaken to evaluate the effects of the six factors. By regression analysis, concentration of substrate, amount of lipase and the temperature were found to be important for enzymatic resolution of glycidyl butyrate. In the second phase of the optimization process, a response surfacemethodology (RSM) was used to optimize the above critical factors, and to find out the optimal concentration levels and the relationships between these factors. By solving the quadratic regression model equation using appropriate statistic methods, the optimal parameter of the variables were determined as: 0.499 mol/L glycidyl butyrate, 30.23 mg/g lipase and 29.68 degrees C. In the optimum condition, the value of enantiomeric excess(ee%) was 93.28%. Compared to 84.65% which was the maximum ee% under the non-optimized condition, this study has a significant advancement. The experimental data under various conditions have validated the theoretical values.
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PMID:[Optimization of enzymatic resolution technique of glycidyl butyrate via response surface methodology]. 1880 93

A wide range of fatty acid esters can be synthesized by esterification and transesterification reactions catalyzed by lipases in non-aqueous systems. In the present study, immobilization of a purified alkaline extra-cellular lipase of Bacillus cereus MTCC 8372 by adsorption on diatomaceous earth (celite) for synthesis of ethyl acetate via transesterification route was investigated. B. cereus lipase was deposited on celite (77% protein binding efficiency) by direct binding from aqueous solution. Immobilized lipase was used to synthesis of ethyl acetate from vinyl acetate and ethanol in n -nonane. Various reaction conditions, such as biocatalyst concentration, substrates concentration, choices of solvents ( n -alkanes), incubation time, temperature, molecular sieves (3A x 1.5 mm), and water activity(a w ), were optimized. The immobilized lipase (25 mg/ml) was used to perform transesterification in n -alkane(s) that resulted in approximately 73.7 mM of ethyl acetate at 55 degrees C in n -nonane under shaking (160 rpm) after 15 h, when vinyl acetate and ethanol were used in a equimolar ratio (100 mM each). Addition of molecular sieves (3A x 1.5 mm) as well as effect of water activity of saturated salt solutions (KI, KCl and KNO 3 ) to the transesterification efficiency has inhibitory effect. Batch operational stability tests indicated that immobilized lipase had retained 50% of its original catalytic activity after four consecutive batches of 15 h each.
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PMID:Synthesis of ethyl acetate employing celite-immobilized lipase of Bacillus cereus MTCC 8372. 1978 38


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