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1.
《Biocatalysis and Biotransformation》2013,31(5):237-245
AbstractThe reaction kinetics of Candida antarctica lipase B (CalB) in the commercially available preparation Novozym® 435 (N435) were compared to those of preparations of CalB immobilised on Accurel® MP1000 (porous polypropylene). Two polypropylene preparations were made using enzyme loadings of 0.2% and 2% (w/w). All three preparations were used in hydrolysis as well as transesterification of two substrates, ethyl acrylate and ethyl methacrylate with octanol. Reactions carried out at water activity levels from 0.06 to 0.96 and at octanol concentrations between 25 and 500 mM showed that both water and octanol can inhibit CalB. Pronounced mass transfer limitations were also observed, which were more pronounced for N435 than for the two MP1000 preparations. The MP1000 preparations could thus use the lipase more efficiently in these reactions, achieving a specific activity (per g enzyme) between 5 and 20 times that of N435. To achieve high rates in the transesterification reaction, it is recommended to use low water activity and moderate alcohol concentration. In order to carry out a hydrolysis reaction, an intermediate water activity should be used to balance the effects of water as a limiting substrate and as a competitive inhibitor. 相似文献
2.
Three methods for enzyme modification/immobilization were compared to enhance the catalytic performance of a commercially available lipase, Lipase PS from Pseudomonascepacia, in highly enantioselective transesterification of an agrochemically useful sec-alcohol, (R,?S)-HMPC [=(R,?S)-4-hydroxy-3-methyl-2-(2′-propenyl)-2-cyclopenten-1-one], with vinyl acetate as both acyl donor and reaction medium. The stearic acid-coated lipase showed the highest catalytic activity, with a specific activity improved by 54 times over the native lipase. The microcrystal salt-supported lipase and celite-adsorbed lipase also displayed much better performance as compared with the native lipase. All the three modified lipase preparations showed a similar thermal stability to that of the native enzyme. The enantioselectivity (E-value) was also quite satisfactory in all the cases (E>100 at 30°C), though a trend of slight decline was also observed with the temperature increase in the range of 25–60°C. The optimum aqueous pH, from which the modified lipases were prepared, was 6.0–7.0. A low water activity (aw) of ca. 0.1 was favorable for all the three modified lipases. The stearic acid-coated lipase displayed prominent advantages in catalyzing the transesterification reaction at a very high (R,?S)-HMPC concentration up to 1.0?M. 相似文献
3.
Suk-Chan Park Woo-Jin Chang Sang-Mok Lee Young-Jun Kim Yoon-Mo Koo 《Biotechnology and Bioprocess Engineering》2005,10(1):99-102
Organic solvents are widely used in biotransformation systems. There are many efforts to reduce the consumption of organic
solvents because of their toxicity to the environment and human health. In recent years, several groups have started to explore
novel organic solvents called room temperature ionic liquids in order to substitute conventional organic solvents. In this
work, lipase-catalyzed transesterification in several uni-and bi-phasic systems was studied. Two representative hydrophobic
ionic liquids based on 1-butyl-3-methylimidazolum coupled with hexafluorophosphate ([BMIM][PF6]) and bis[(trifluoromethylsulfonyl) imide] ([BMIM] [Tf2N]) were employed as reaction media for the transesterification ofn-butanol. The commercial lipase, Novozym 435, was used for the transesterification reaction with vinyl acetate as an acyl
donor, The conversion yield was increased around 10% in a water/[BMIM][Tf2N], bi-phasic system compared with that in a water/hexane system. A higher distribution of substrates into the water phase
is believed to enhance the conversion yield in a water/[BMIM][Tf2N] system. Partion coefficients of the substrates in the water/[BMIM][Tf2N] bi-phasic system were higher than three times that found in the water/hexane system, while n-butyl acetate showed a similar
distribution in both systems. Thus, RTILs appear to be a promising substitute of organic solvents in some biotransformation
systems. 相似文献
4.
The methacrylate ester of citronellol was synthesized using various lipases as catalyst. The effect of different reaction parameters such as amount of lipase, solvent, temperature, and acylating agent on the conversion of citronellol to citronellyl methacrylate was studied. Methyl methacrylate, vinyl methacrylate, and 2,3-butanedione mono-oxime methacrylate were used as acylating agents. Porcine pancreatic lipase (PPL), Candida rugosa lipase (CRL), and Pseudomonas cepacia lipase (Amano-PS) were used as biocatalysts. Diisopropyl ether (DIPE) was found to be the most suitable solvent. The stereoselectivity of CRL in transesterification of (+/-)-citronellol was tested for the optimized reaction parameters. 相似文献
5.
《Biocatalysis and Biotransformation》2013,31(6):238-245
AbstractReactions involving tert-alcohols and their esters are generally not catalyzed by lipases. Candida rugosa lipase is one of the few lipases which shows at least limited catalytic activity towards tert-alcohols and their esters. Using transesterification of tributyrin with tertiary butyl and amyl alcohols as a model reaction, it is shown that precipitation of lipase by a tertiary alcohol in the presence of a buffer with optimum concentration enhances the catalytic activity 7 fold as compared to rates obtained with lyophilized powders. Optimization of the ratio of triglyceride to tert-alcohols and medium engineering gave an initial rate which was 41 times higher than that obtained with lyophilized powders. Hence, use of a simple enzyme formulation, coupled with optimization of reaction conditions led to Candida rugosa lipase becoming a useful catalyst for catalyzing transesterification involving tertiary alcohols. 相似文献
6.
Anastasia MacArio Girolamo Giordano Leonardo Setti Attilio Parise Juan M. Campelo José M. Marinas 《Biocatalysis and Biotransformation》2013,31(2-4):328-335
In order to understand the role of the acid–base, electrostatic and covalent interactions between enzyme and support, the catalytic behavior of the Rhizomucor miehei lipase (RML) immobilized on zeolite materials has been studied. The highest lipase activities were obtained when this enzyme, immobilized by adsorption, interacts through acid–base binding forces with the support surface, resulting in activation of the enzyme catalytic center. Due to the interest in biodiesel production by mild enzymatic transesterification, this heterogeneous biocatalyst has been used in transesterification of fatty acids contained in olive oil. The results show a high oleic acid conversion for several reaction cycles with a higher total biodiesel productivity compared to that using the free enzyme. 相似文献
7.
Carlos F. Torres Luis Vzquez Francisco J. Seorns Guillermo Reglero 《Process Biochemistry》2009,44(9):1025-1031
Lipase-catalyzed transesterification of 1-O-octadecyl glycerol (batyl alcohol) with ethyl butyrate has been studied. The effect of vacuum on the rate of both transesterification and distillation of ethyl butyrate has also been investigated and at different reaction conditions, more than 85% of 1-O-octadecyl glycerol was consumed in only 5 min giving rise to the monoester. Then the monoester is again acylated to produce the diesterified product. In addition, the transesterification reactions were effected in solvent free reaction medium and it has been scaled-up to produce up to ca. 500 g of 2,3-dibutyroil-1-O-alkylglycerols in three consecutive cycles reutilizing the same batch of lipase. An efficient evaporation of ethanol was necessary to significantly reduce the reaction times of the transesterification reaction. Finally, a kinetics model describing both the rate of transesterification and the rate of inactivation of the immobilized lipase has been developed. The results indicate that the operational stability of the immobilized lipase confined into the mesh baskets (according to the value of kd attained), was very high and that provides a half-life of the lipase higher than 1500 h.The present procedure is intended to be used for the synthesis of homogeneous alkylglycerols with biological activities and/or precursors of structured alkylglycerols. 相似文献
8.
Toshiyuki Furutani Ronghui Su Hiroshi Ooshima Jyoji Kato 《Enzyme and microbial technology》1995,17(12):1067-1072
We investigated lipase-catalyzed hydrolysis in water and dioxane—water with a simple colorimetric method. We screened 24 lipases for the ability to hydrolyze p-nitrophenyl esters as chromogenic substrates. Their hydrolytic activities were varied by adding dioxane. Most of the lipases showed high activity in hydrolysis in water, but some showed activity in 50% dioxane—water several tens times higher than those in water. Moreover, several lipases with hydrolytic abilities in 50% dioxane—water also catalyzed the transesterification of p-nitrophenol using fatty acid vinyl esters. We found it possible that a useful lipase for transesterification can be selected by measuring the hydrolysis activity of p-nitrophenyl ester in 50% dioxane—water. 相似文献
9.
Kyung Hwa Lee Chang-Ho Park Eun Yeol Lee 《Bioprocess and biosystems engineering》2010,33(9):1059-1065
Glycerol carbonate was synthesized from renewable glycerol and dimethyl carbonate using lipase in solvent-free reaction system
in which excess dimethyl carbonate played as the reaction medium. A variety of lipases have been tested for their abilities
to catalyze transesterification reaction, and Candida antartica lipase B and Novozyme 435 exhibited higher catalytic activities. The silica-coated glycerol with a 1:1 ratio was supplied
to prevent two-phase formation between hydrophobic dimethyl carbonate and hydrophilic glycerol. Glycerol carbonate was successfully
synthesized with more than 90% conversion from dimethyl carbonate and glycerol with a molar ratio of 10 using Novozyme 435-catalyzed
transesterification at 70 °C. The Novozyme 435 [5% (w/w) and 20% (w/w)] and silica gel were more than four times recycled
with good stability in a repeated batch operation for the solvent-free synthesis of glycerol carbonate. 相似文献
10.
Highly active lipase and protease complexes were prepared by non-covalent modification with stearic acid. The protein content and yield of the modified enzyme complexes depended on the enzymes' source. The increase in the transesterification activity of the modified enzymes was 15 fold for Candida rugosa lipase and porcine pancreatic lipase, with preservation of the enantioselectivity. Pseudomonas sp. lipase which showed no activity in its crude form, exhibited an activity of 38 mol/h·mg protein in the modified form. © Rapid Science Ltd. 1998 相似文献
11.
Achmadin Luthfi Machsun Misri Gozan Mohammad Nasikin Siswa Setyahadi Young Je Yoo 《Biotechnology and Bioprocess Engineering》2010,15(6):911-916
Transesterification is a principal chemical reaction that occurs in biodiesel production. We developed a novel biocatalytic
membrane microreactor (BMM) for continuous transesterification by utilizing an asymmetric membrane as an enzyme-carrier for
immobilization. The BMM was developed by pressure driven filtration of lipase from Pseudomonas fluorescens, which is suitable for highly efficient biocatalytic transesterification. Lipase solution was allowed to permeate through
an asymmetric membrane with NMWL 300 kDa composed of polyethersulfone. The performances of BMM were studied in biodiesel synthesis
via transesterification of triolein with methanol. Transesterification was carried out by passing a solution of triolein and
methanol through the asymmetric membrane. The degree of triolein conversion using this microreactor was ca. 80% with a reaction
time of 19 min. The BMM system displayed good stability, with no activity decay over a period of 12 day with continuous operation.
Results from triolein transesterification clearly demonstrate the potential of an asymmetric membrane as an enzyme carrier
material. Enzyme activity (mmol/h·glipase) was approximately 3 fold higher than that of native free lipase. 相似文献
12.
Penicillium sp.脂肪酶的发酵及催化生成生物柴油的研究 总被引:5,自引:2,他引:5
目的:为了提高脂肪酶的产量及更好地应用脂肪酶。方法:采用单因子实验与均匀设计相结合的方法,对青霉Penicil- lium sp.TS414发酵生产脂肪酶的条件进行了优化。结果:在实验优化后的最适产酶培养基中,碳源为1.4%蔗糖,氮源为7.0%豆饼粉,起始pH8.0。均匀设计优化后的产酶水平(315.1U/mL)比优化前(101.5U/mL)提高了约2倍。Penicillium sp.TS414脂肪酶能够有效地催化大豆油转酯化合成脂肪酸甲酯(生物柴油),反应72h后,脂肪酸甲酯的最终得率在96%左右。结论:Penicillium sp.TS414产生的脂肪酶在生物柴油的工业化生产方面,具有潜在的应用前景。 相似文献
13.
Xiao Wang Xiaohong Wang Yanling Xu Jie Kang Ying Zhang 《Biocatalysis and Biotransformation》2018,36(4):332-339
Cinnamyl acetate as an important fragrance ingredient could be synthesized by lipase-catalysed transesterification in organic systems, but enzyme proteins tended to denature and inactivate for no water lubrication. To improve the non-aqueous stability of lipases, absorbent cotton was taken as an alternative “water” phase to stabilize enzyme proteins. In a mass ratio of 1:1, Pseudomonas fluorescens lipase was immobilized on cotton fibres by physical absorption in a column glass bottle, forming a facile cotton-lipase bioreactor in which the transesterification between cinnamyl alcohol and vinyl acetate processed efficiently. From the molar conversions after reaction for 2?h at 37?°C and 160?rpm, the ability of cotton-lipase to transform substrate was more than 5-folds of native lipase. And even in static state and at 4?°C, the conversion of reaction catalysed by cotton-PFL had 11-fold increase relative to native lipase after 8?h. Recycles showed that the cotton-lipase had an extra-long half-life of activity (t1/2?=?693?h) and a negligible decay rate in the ability to transform substrate (Dr?=?0.08% h?1). All these showed that this lipase had been effectively activated and stabilized by cotton fibres for the numerous hydroxyl groups and fluffy structure. 相似文献
14.
The lipase from Pseudomonas fragi 22.39 B catalyzed the transesterification in ester and alcohol mixtures without any other solvent. Activated esters, such as vinyl and phenyl esters, were excellent acyl donors for the reaction, and the activity was enhanced by increasing the carbon number of the fatty acid fraction of the esters. Primary alcohols were esterified faster than secondary ones in this reaction system, while tertiary alcohols such as alpha-terpineol did not react at all. The lipase exhibited stereoselectivity in the esterification of alcohols such as 2-octanol. 相似文献
15.
Mirosława Szczęsna-Antczak Łukasz Stańczyk Agnieszka Borowska Tadeusz Antczak 《Biocatalysis and Biotransformation》2016,34(6):253-264
The objective of presented study was to maximize yields of 2-methylbutyl esters, derived by transesterification reactions mediated by sn-1,3-specific lipases, through engineering of reaction medium. Effects of water and diethylamine (DEA) concentrations on the efficiency of plant oils 2-methylbutanolysis, catalyzed by either mycelium-bound Mucor circinelloides lipase (powder) or commercial immobilized lipase Lipozyme TL IM, were determined. Water content monitoring in reaction mixtures enabled to optimize the initial water content in terms of preventing the dehydration of enzyme’s microenvironment and increasing 2-methylbutyl esters yields. These yields were found to be increased by addition of either suitable amounts of water (0.5–1.5%) or diethylamine (10–30?mM) to the mixture of substrates. The presented results suggest that at low concentrations, diethylamine molecules contribute to retaining water in the microenvironment of enzyme that gives rise to increased transesterification yields and significantly reduced amounts of residual mono- and 1,2-diacyl-glycerols. 相似文献
16.
Biodiesel has gained widespread importance in recent years as an alternative, renewable liquid transportation fuel. It is derived from natural triglycerides in the presence of an alcohol and an alkali catalyst via a transesterification reaction. To date, transesterification based on the use of chemical catalysts has been predominant for biodiesel production at the industrial scale due to its high conversion efficiency at reasonable cost. Recently, biocatalytic transesterification has received considerable attention due to its favorable conversion rate and relatively simple downstream processing demands for the recovery of by-products and purification of biodiesel. Biocatalysis of the transesterification reaction using commercially purified lipase represents a major cost constraint. However, more cost-effective techniques based on the immobilization of both extracellular and intracellular lipases on support materials facilitate the reusability of the catalyst. Other variables, including the presence of alcohol, glycerol and the activity of water can profoundly affect lipase activity and stability during the reaction. This review evaluates the current status for lipase biocatalyst-mediated production of biodiesel, and identifies the key parameters affecting lipase activity and stability. Pioneer studies on reactor-based lipase conversion of triglycerides are presented. 相似文献
17.
18.
The Rhizopus oryzae lipase containing prosequence was expressed in Pichia pastoris. Recombinant lipase subunit showed a molecular mass of 32 kDa. The maximum activity of recombinant lipase obtained from Mut(s) recombinant was 90 IU/ml. The enzyme was stable in broad ranges of temperatures and pH, with the optimal temperature at 35 °C and pH 7.0. The crude recombinant R. oryzae lipase can be directly used for the transesterification of plant oils at high-water content of 60-100% (w/w) based on oil weight. The addition of 80% water to the transesterification systems resulted in the yield of methyl ester of 95%, 94% and 92% after 72 h using soybean oil, Jatropha curcas seed raw oil and Pistacia chinensis seed raw oil as raw material, respectively. These results indicate that the recombinant lipase is an effective biocatalyst for enzymatic biodiesel production. 相似文献
19.
Lipase-catalyzed transesterification of rapeseed oils for biodiesel production with a novel organic solvent as the reaction medium 总被引:15,自引:0,他引:15
Lilin Li Wei Du Dehua Liu Li Wang Zebo Li 《Journal of Molecular Catalysis .B, Enzymatic》2006,43(1-4):58-62
tert-Butanol, as a novel reaction medium, has been adopted for lipase-catalyzed transesterification of rapeseed oil for biodiesel production, with which both the negative effects caused by excessive methanol and by-product glycerol could be eliminated. Combined use of Lipozyme TL IM and Novozym 435 was proposed further to catalyze the methanolysis and the highest biodiesel yield of 95% could be achieved under the optimum conditions (tert-butanol/oil volume ratio 1:1; methanol/oil molar ratio 4:1; 3% Lipozyme TL IM and 1% Novozym 435 based on the oil weight; temperature 35 °C; 130 rpm, 12 h). There was no obvious loss in lipase activity even after being repeatedly used for 200 cycles with tert-butanol as the reaction medium. Furthermore, waste oil was also explored for biodiesel production and it has been found that lipase also showed good stability in this novel system. 相似文献
20.
Triantafyllou AO Wehtje E Adlercreutz P Mattiasson B 《Biotechnology and bioengineering》1997,54(1):67-76
The catalytic activities of lyophilized powders of alpha-chymotrypsin and Candida antarctica lipase were found to increase 4- to 8-fold with increasing amounts of either buffer salts or potassium chloride in the enzyme preparation. Increasing amounts of sorbitol in the chymotrypsin preparation produced a modest increase in activity. The additives are basically thought to serve as immobilization matrices, the sorbitol being inferior because of its poor mechanical properties.Besides their role as supports, the buffer species were indispensable for the transesterification activity of chymotrypsin because they prevented perturbations of the pH during the course of the reaction. Hence, increasing amounts of buffer species yielded a 100-fold increase in transesterification activity. Effects of pH changes were not as predominant in the peptide synthesis and the lipase-catalyzed reactions.Immobilization of the protease on celite resulted in a remarkable improvement of transesterification activity as compared to the suspended protease, even in the absence of buffer species. Immobilization of the lipase caused a small improvement of activity. The activity of the immobilized enzymes was further enhanced 3-4 times by including increasing amounts of buffer salts in the preparation.The inclusion of increasing amounts of sodium phosphate or sorbitol to chymotrypsin rendered the catalyst more labile against thermal inactivation. The denaturation temperature decreased with 7 degrees C at the highest content of sodium phosphate, as compared to the temperature obtained for the denaturation of the pure protein. The apparent enthalpy of denaturation increased with increasing contents of the additives. The enhancement of hydration level and flexibility of the macromolecule upon addition of the compounds partly provides the explanation for the observed results. (c) 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 54: 67-76, 1997. 相似文献