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1.
对催化合成L-抗坏血酸棕榈酸酯反应的脂肪酶(NOVO435、MML、LIPOLASE、PPL)和反应介质进行比较,得出最佳酶种为NOVO435,最佳介质为叔戊醇;同时对影响合成L抗坏血酸棕榈酸酯反应的初速度的因素(转速、温度、水分含量、酶浓度和底物浓度)进行了探讨,确定了最适反应条件:转速为200r/min,温度为55℃,水分含量为0,酶浓度为12.5%。  相似文献   

2.
生物法合成维生素C棕榈酸酯   总被引:7,自引:0,他引:7  
研究了不同的脂肪酶在有机溶剂体系中催化合成L-维生素C棕榈酸酯的反应。针对维生素C在有机溶剂中溶解度较低这一问题,对催化合成维生素C棕榈酸酯反应的脂肪酶和反应介质进行比较,同时对影响合成维生素C棕榈酸酯反应的因素(温度、底物浓度、底物摩尔比、反应时间和酶量等)进行探讨,优化了反应条件:在10mL的丙酮中,1.094g棕榈酸与0.107g维生素C在酶量为20%(W/W, 固定化酶/维生素C)的固定化脂肪酶催化下,初始含0.4nm分子筛20%,温度为60℃,转速为200r/min,反应48h转化率可以达到80%,产物维生素C棕榈酸酯的浓度可达20g/L。  相似文献   

3.
应用RNA印迹分析和亚硝酸盐含量测定检查脂多糖(LPS)对大鼠血管平滑肌细胞(VSMC)一氧化氮合酶(NOS)基因表达及NO合成的影响,用3H-TdR参入实验观察LPS对细胞DNA合成的影响.结果表明,LPS在诱导VSMCiNOSmRNA表达和促进NO合成的同时,抑制VSMCDNA合成.证明LPS的作用与其浓度和作用时间有关  相似文献   

4.
应用RNA迷分析和亚硝酸盐含量测定检查脂多糖(LPS)对大鼠血管平滑肌细胞(VSMC)一氧化氮合酶(NOS)基因表达及NO合成的影响,用T3H-TdR参入实验观察LPS对细胞DNA合成的影响,结果表明,LPSD 诱导VSMCiNOSmRNA表达和促进NO合成的同时,抑制VSMCDNA合成,证明LPS的作用与其浓度和作用时间有关。  相似文献   

5.
脂多糖对离体培养大鼠血管平滑肌细胞增殖的影响   总被引:2,自引:0,他引:2  
Li J  Lin SX  Li Y  Zhao HL  Jia B 《生理学报》1999,51(1):14-18
本研究观察到10-7~10-5kg/L脂多糖(lipopolysacharide,LPS)可显著促进血管平滑肌细胞(VSMC)的增殖及DNA的合成(P<005)。5×10-4~10-3kg/LLPS却抑制VSMC的增殖及DNA的合成,降低其活力(P<001),并呈时间依赖效应。一氧化氮合酶抑制剂NNitroLArginine(LNNA)可拮抗LPS的抑制作用。大剂量LPS作用组VSMC上清液中一氧化氮(NO)代谢产物NO-3和NO-2的含量与对照组相比显著增加(P<001),48h组比24h组增加91%,72h组比48h组增加45%;同时,诱导性一氧化氮合酶(inductivenitricoxidesynthase,iNOS)免疫组化染色呈阳性。结果表明,低浓度LPS促进VSMC增殖和DNA合成,而高浓度LPS却明显抑制VSMC增殖和DNA合成,降低其活力。这种抑制作用可能与LPS诱导VSMC产生的NO有关。  相似文献   

6.
中缝大核在刺激视上核镇痛中的作用   总被引:1,自引:0,他引:1  
运用核团灌流液的放免测定和高压液相色谱法以及核团内注射拮抗剂,观察了化学刺激下丘脑视上核(SON)对中缝大核(NRM)灌流液内催产素(OT)、精氨酸加压素(AVP)和5-羟色胺(5-HT)含量的影响以及NRM内注射AVP、5-HT或OT受体拮抗剂对痛阈(PT)的影响。结果表明:SON内注射L-谷氨酸(L-Glu)10μg后动物痛阈明显升高,NRM灌流液中OT和5-HT的含量明显高于对照组水平,AVP的含量仅有一过性增加。NRM内注射oT或5-HT拮抗剂可逆转化学刺激SON引起的镇痛作用;而AVP的V_(1/2)受体拮抗剂也轻度抑制这种镇痛作用,但V_1拮抗剂对此作用无影响。以上结果提示:在刺激SON镇痛中,OT起着重要作用,L-Glu刺激SON的OT细胞释放OT,作用于NRM细胞的OT受体和V_2受体而产生镇痛作用,5-HT在此过程中也发挥重要作用。  相似文献   

7.
L-NNA及NO供体对延髓腹外侧头端区神经元自发放电的影响   总被引:3,自引:1,他引:2  
在麻醉大鼠观察了静注NO合成酶抑制剂N-硝基左旋精氨酸(L-NNA)和NO供体──硝普钠(SNP)和SIN-I对血压、心率和延髓腹外侧头端区(RVLM)神经元自发放电活动的影响,旨在探讨L-arg:NO通路对动脉血压调节的中枢作用部位。所得结果如下:(1)静注L-NNA后,平均动脉压(MAP)升高,心率(HR)加快,11个RVLM神经元自发放电频率增加。这些变化发生于给药后5min,持续时间达30min以上。(2)静注SNP后,MAP降低,HR加快,23个RVLM神经元自发放电频率降低,且有剂量依赖性。SNP作用发生快,持续时间短。为了排除脑缺血的影响,还特意向一侧颈动脉内注射相同剂量SNP,结果引起MAP轻度降低,而HR无明显改变,但RVLM神经元自发放电频率仍显著降低。(3)静注另一NO供体SIN-I后,MAP降低,11个RVLM神经元自发放电频率降低.与SNP的效应基本一致。以上结果提示,RVLM是L-arg:NO通路实现动脉血压调节的一个中枢作用部位。  相似文献   

8.
曲霉N1—14‘胞质酶活性与产L—苹果酸能力的关系   总被引:3,自引:0,他引:3  
L-苹果酸(LMA)高产突变株曲霉N1-14’在高产酸状态下,其胞质中催化CO2固定反应的酶有四种:丙酮酸羧化酶(PC)、磷酸烯醇丙酮羧化酶(PEPC)、磷酸烯醇丙酮酸羧化激酶(PCK)和苹果酸酶(ME);除ME之外,三种羧化酶的活性与LMA产生速率呈较好的线性正相关关系;苹果酸脱氢酶(MDH)活性比PC等酶高2 ̄3个数量级;琥珀酸脱氢酶(SDH)活力则明显低,几种酶只有SDH与发酵醪中LMA含量  相似文献   

9.
以N‘-苄氧羰工保护的L-赖氨酸(L-Lys(Z)-OH)为原料,经过混合酸活化,与重氮甲烷反应合成重氮酮,再经Wolff重排,合成了具有光学活性的L-7-(N-苄氧羰基)氨基-3-(N-叔丁氧羰基)氨基-正庚酸。  相似文献   

10.
在KC1介质中牛脑V-型质子转运ATP酶复合体活力温度的Arrhenius图在33℃附近呈现明显的折点,同样做其N-[1-芘]马来酰亚胺(N-[1-P]M)的荧光-温度的Arrhenius图,发现其折点温度也为33℃,当加入100μmol/L NEM(N-ethylmaleimide),ATP酶复合体活力部分被抑制后的Arrhenius图折点下降为27℃,加入0.75-0.85mol/L尿素则活力  相似文献   

11.
The enzymatic hydrolysis of a mixture of lutein diesters from Marigold flower (Tagetes erecta) was performed both in organic solvents and supercritical CO(2) (SC-CO(2)) using two commercial lipases: lipase B from Candida antarctica (Novozym 435) and the lipase from Mucor miehei (Lipozyme RM IM). Both lipases showed an unexpected dependence of initial reaction rate with the initial water activity (a(wi)) in hexane, with the highest rates of hydrolysis taking place at the lowest a(wi) of the biocatalyst particles. The same result was observed using isooctane, toluene, or SC-CO(2). It is proposed that an increase in a(wi) generates a hydrophilic microenvironment that prevents efficient partitioning of the highly hydrophobic lutein diesters to the enzyme. The critical role of water in this system has not been reported for other hydrolytic reactions in low water media. Calculations of water available for hydrolysis from isotherm analysis, Karl-Fischer titration, and substrate conversion at a(wi) = 0.13, indicate that the extent of reaction is not limited by the amount of available water. Accordingly, the enzyme that holds the largest amount of water after prehydration at the same a(wi) (0.13) will yield the greatest substrate conversion and concentration of the free lutein product. The highest conversion occurred in SC-CO(2), which opens up new opportunities to develop a combined extraction-reaction process for the environmentally benign synthesis of lutein, an important nutraceutical compound.  相似文献   

12.
Immobilization of lipases involves many levels of complications relating to the structure of the active site and its interactions with the immobilization support. Interaction of the so called hydrophobic ‘lid’ with the support has been reported to affect synthetic activity of an immobilized lipase. In this work we evaluate and compare the synthetic activity of lipases from different sources immobilized on different kinds of supports with varying hydrophobicity. Humicola lanuginosa lipase, Candida antarctica lipase B and Rhizomucor miehei lipase were physically adsorbed onto two types of hydrophobic carriers, namely hydrophilic carriers with conjugated hydrophobic ligands, and supports with base matrix hydrophobicity. The prepared immobilized enzymes were used for acylation of n-butanol with oleic acid as acyl donor in iso-octane with variable water content (0–2.8%, v/v) as reaction medium. Enzyme activity and effect of water on the activity of the immobilized derivatives were compared with those of respective soluble lipases and a commercial immobilized lipase Novozyme 435. Both R. miehei and H. lanuginosa immobilized lipases showed maximum activity at 1.39% (v/v) added water concentration. Sepabeads, a methacrylate based hydrophilic support with conjugated octadecyl chain showed highest immobilized esterification (synthetic) activity for all three enzymes, and of the three R. miehei lipase displayed maximum esterification activity comparable to the commercial enzyme.  相似文献   

13.
Previously isolated and characterized Pseudomonas lipases were immobilized in a low‐cost MP‐1000 support by a re‐loading procedure that allowed a high activity per weight of support. Immobilized LipA, LipC, and LipCmut lipases, and commercial Novozym® 435 were tested for fatty acid methyl ester (FAMEs) synthesis using conventional and alternative feedstocks. Triolein and degummed soybean oils were used as model substrates, whereas waste cooking oil and M. circinelloides oil were assayed as alternative, low cost feedstocks, whose free fatty acid (FFA), and acylglyceride profile was characterized. The reaction conditions for FAMEs synthesis were initially established using degummed soybean oil, setting up the best water and methanol concentrations for optimum conversion. These conditions were further applied to the alternative feedstocks and the four lipases. The results revealed that Pseudomonas lipases were unable to use the FFAs, displaying a moderate FAMEs synthesis, whereas a 44% FAMEs production was obtained when M. circinelloides oil was used as a substrate in the reaction catalysed by Novozym® 435, used under the conditions established for degummed soybean oil. However, when Novozym® 435 was tested under previously described optimal conditions for this lipase, promising values of 85 and 76% FAMEs synthesis were obtained for waste cooking oil and M. circinelloides oil, respectively, which might result in promising, nonfood, alternative feedstocks for enzymatic biodiesel production. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 33:1209–1217, 2017  相似文献   

14.
Optimization of lipase-catalyzed biodiesel by response surface methodology   总被引:18,自引:0,他引:18  
Biodiesel prepared by catalyzed mild transesterification has become of much current interest for bioenergy. The ability of a commercial immobilized lipase (Novo Industries--Bagsvaerd, Denmark) from Rhizomucor miehei (Lipozyme IM-77) to catalyze the transesterification of soybean oil and methanol was investigated in this study. Response surface methodology and 5-level-5-factor central composite rotatable design were employed to evaluate the effects on reaction time, temperature, enzyme amount, molar ratio of methanol to soybean oil, and added water content on percentage weight conversion to soybean oil methyl ester by transesterification. Based on ridge max analysis, the optimum synthesis conditions giving 92.2% weight conversion were: reaction time 6.3 h, temperature 36.5 degrees C, enzyme amount 0.9 BAUN (Batch Acidolysis Units NOVO), substrate molar ratio 3.4:1, and added water 5.8%.  相似文献   

15.
This paper describes in detail the selection and optimization of immobilized lipases for enhanced regioselective acylation of glucose into glucose monolaurate (GlcML). Initially, nature of biocatalyst, immobilization approach, reaction media, glucose, and lauric acid concentration were screened out. Finally, lipases from Rhizopus arrhizus immobilized on dead mycelia were investigated under various reaction conditions (Temperature, shaking speed, enzyme dose, and water content) following a fully rotatable central composite design (FRCCD) to optimize the activity of lipases. The immobilized lipases-based biocatalysts in the presence of polar solvents (tertiary alcohols) and higher concentrations of substrates i.e. glucose and lauric acid (100 and 300?mmol?L?1, respectively) offered conversion rate of 1.5 mmolmin?1?L?1. Moreover, optimization of reaction conditions revealed that 162.5 lipase units/100mL at 31.25?°C, 3% water content, and 105?RPM shaking speed enhanced the conversion rate by 0.5 mmolmin?1?L?1 rendering the reaction more economical. Hence, lipases-based immobilized biocatalysts may provide an intelligent and green choice for commercial scale synthesis of GlcML for food and pharmaceutical industries.  相似文献   

16.
Ethanolysis of borage oil catalyzed by two commercial lipases (from Pseudomonas cepacia and Candida antarctica) was studied using two different methodologies. Multiresponse models derived from a generalized Michaelis-Menten mechanism were utilized to describe the rates of formation of ethyl esters of the primary fatty acids present in the precursor oil. The relative rate constants determined for each of the fatty acid residues indicated that both lipases discriminate against release of gamma-linolenic acid residues under the reaction conditions studied. However, both lipases also released some of the residues located at the sn-2 position, indicating that for the experimental conditions studied, both lipases are nonspecific. Moreover, inactivation of Novozym 435 was rapid. Because the half-life of this enzyme (ca. 2.2 h) is comparable to the half-life of the reaction, the intrinsic reaction rate and enzyme deactivation must both be considered in modeling the kinetics.  相似文献   

17.
脂肪酶协同催化猪油合成生物柴油工艺研究   总被引:1,自引:0,他引:1       下载免费PDF全文
探讨了以乙酸甲酯为酰基受体两种脂肪酶协同催化猪油转酯合成生物柴油的工艺条件。首先利用单因子试验确定2种固定化脂肪酶Novozym435、Lipozyme TLIM单独作为催化剂时的最佳酶用量为40%,反应温度为50℃,乙酸甲酯用量为14(相对于油的摩尔比)。在此基础上,采用3因素5水平和3个中心点的中心组分旋转设计法研究了上述2种脂肪酶协同使用时脂肪酶用量(g/g)、混合酶的配比(%/%)以及乙酸甲酯用量诸因素共同作用对转酯反应转化率的影响。优化后的反应条件为:总酶用量为40%,混合酶配比为50/50,乙酸甲酯用量为14,在该条件下甲酯得率可达97.6%,比同质量的Novozym435、Lipozyme TLIM的催化活性分别高出7.6%、22.3%。表明脂肪酶协同催化猪油合成生物柴油工艺可以较好地提高甲酯得率,并且节约生产成本。  相似文献   

18.
Enzymatic ring-opening polymerization of epsilon-caprolactone by various lipases was investigated in toluene at various temperatures. The determination of molecular weight and structural identification was carried out with gel permeation chromatography and proton NMR, respectively. Among the various lipases employed, an immobilized lipase from Candida antartica B (Novozym 435) showed the highest catalytic activity. The polymerization of epsilon-caprolactone by Novozym 435 showed an optimal temperature of 65 degrees C and an optimum toluene content of 50/50 v/v of toluene and epsilon-caprolactone. As lipases can degrade polyesters, a maximum in the molecular weight with time was obtained due to the competition of ring opening polymerization and degradation by specific chain end scission. The optimum temperature, toluene content, and the variation of molecular weight with time are consistent with earlier observations. A comprehensive model based on continuous distribution kinetics was developed to model these phenomena. The model accounts for simultaneous polymerization, degradation and enzyme deactivation and provides a technique to determine the rate coefficients for these processes. The dependence of these rate coefficients with temperature and monomer concentration is also discussed.  相似文献   

19.
Penicillium expansum lipase (PEL) was used to catalyze biodiesel production from corn oil in [BMIm][PF6]1 (an ionic liquid, IL) and tert-butanol. Both systems were optimized in terms of MeOH/oil molar ratio, reaction temperature, enzyme loading, solvent volume, and water content. The high conversion obtained in the IL (86%) as compared to that in tert-butanol (52%) demonstrates that the IL is a superior solvent for PEL-catalyzed biodiesel production. Poor yields were obtained in a series of hydrophilic ILs. Addition of salt hydrates affected biodiesel production predominantly through the specific ion (Hofmeister) effect. The impact of methanol on both activity and stability of PEL in the IL and in hexane was investigated, in comparison to the results obtained by two commonly used lipases, Novozym 435 and Lipozyme TLIM. The results substantiate that while different lipases show different resistance to methanol in different reaction systems, PEL is tolerant to methanol in both systems.  相似文献   

20.
In order to examine the industrial potential to indirectly isolate phytosterols from deodoriser distillates (DODs), enzymatic transesterification of an industrial rapeseed and soybean oil DOD mixture with bioethanol was investigated using commercial lipases and a few newly immobilised preparations of lipases. The lipases from different sources and differing preparation forms were evaluated, in terms of thermostability, enzyme efficiency, and toleration of ethanol. Lipozyme 435 and Lipozyme NS-40044 TLL were found to be most effective biocatalysts in catalysing ethanolysis of glycerides and steryl esters from DODs. The optimum conditions are 10% enzyme load (wt% of DODs), ethanol/DODs of 3.0:1.0 (mol/mol), water content 0.125% (based on the weight of total mixture), and reaction at 30 °C for 5 h. The results demonstrated that >95% sterols can be recovered as free form (>85% sterol esters were liberated as free sterols within 4 h). With this process, the system was simplified as fatty acid ethyl esters and free sterol as major components, where free sterols can be recovered via solvent extraction or molecular distillation. Furthermore, a reuse study of enzyme in consecutive batch reactions demonstrated an excellent operation stability and reusability of Lipozyme 435 and Lipozyme NS-40044 TLL with the developed process. This work indicated that the industrially refined waste DODs can be directly subjected to an enzymatic process for high efficacy recovery of phytosterol without any pre-process, driven by robust lipase preparations.  相似文献   

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