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排序方式: 共有96条查询结果,搜索用时 15 毫秒
1.
Volkan Kseli Zakir M. O. Rzaev Erhan Pikin 《Journal of polymer science. Part A, Polymer chemistry》2003,41(11):1580-1593
Stimuli‐responsive poly[(N‐isopropylacrylamide‐co‐maleic anhydride)‐g‐poly(ethylene oxide)]/poly(ethylene imine) macrobranched macrocomplexes were synthesized by (1) the radical copolymerization of N‐isopropylacrylamide and maleic anhydride with α,α′‐azobisisobutyronitrile as an initiator in 1,4‐dioxane at 65 °C under a nitrogen atmosphere, (2) the polyesterification (grafting) of prepared poly(N‐isopropylacrylamide‐co‐maleic anhydride) containing less than 20 mol % anhydride units with α‐hydroxy‐ω‐methoxy‐poly(ethylene oxide)s having different number‐average molecular weights (Mn = 4000, 10,000, or 20,000), and (3) the incorporation of macrobranched copolymers with poly(ethylene imine) (Mn = 60,000). The composition and structure of the synthesized copolymer systems were determined by Fourier transform infrared, 1H and 13C NMR spectroscopy, and chemical and elemental analyses. The important properties of the copolymer systems (e.g., the viscosity, thermal and pH sensitivities, and lower critical solution temperature behavior) changed with increases in the molecular weight, composition, and length of the macrobranched hydrophobic domains. These copolymers with reactive anhydride and carboxylic groups were used for the stabilization of penicillin G acylase (PGA). The conjugation of the enzyme with the copolymers significantly increased the thermal stability of PGA (three times at 45 °C and two times at 65 °C). © 2003 Wiley Periodicals, Inc. J Polym Sci Part A: Polym Chem 41: 1580–1593, 2003 相似文献
2.
The effects of five polyethylene glycol (PEG) compounds of different molecular weight on the thermal stability of penicillin
G acylase (PGA) obtained from a mutant ofEscherichia coli ATCC 11105 have been investigated. The molecular weights of PEG compounds were 400, 4000, 6000, 10,000, and 15,000. The thermal
inactivation mechanisms of both native and PEG-containing PGA were considered to obey first order inactivation kinetics during
prolonged heat treatments. Optimal concentrations of PEGs at molecular weights of 400,4000, 6000,10,000, and 15,000 were found
to be 250,150,150,100, and 50 mM, respectively. The greatest enhancement of thermostability was observed with PEG 4000 and
PEG 6000, as a nearly 20-fold increase above 50°C. PGA showed almost the same temperature activity profile and optimal temperature
values both in the presence and absence of PEG. The addition of PEGs did not cause any change in the optimal temperature value
of PGA, but the parametersV
m
,K
m
, the activation energy, and thek
cat
values of enzyme were markedly decreased because of the mixed inhibition by PEG compounds. The type of inhibition was found
to be hyperbolic uncompetitive. 相似文献
3.
青霉素酰化酶在甲基丙烯酸缩水甘油酯共聚物上的固定化 总被引:6,自引:0,他引:6
用共价键合法将青霉素酰化酶固定化在珠状多孔的甲基丙烯酸缩水甘油酯(GM)共聚物上,研究了固定化反应时间、温度、pH值和酶液用量对固定化青霉素酰化酶的表观活性、表观偶联效率、活性回收及稳定性的影响.将GM共聚物载体加入到磷酸缓冲液(0.1mol/L,pH10.8)与青霉素酰化酶液(每克干载体用酶液1ml)的混合溶液中,在30℃下反应72h,单位质量(干重)固定化酶的表观活性为348U/g,表观偶联效率为66.7%,活性回收为31.7%. 相似文献
4.
5.
A simple colorimetric method for the assay of penicillin G salt and penicillamine by oxidation with iodate 总被引:1,自引:0,他引:1
A simple colorimetric procedure is described for determination of penicillin G salt and penicillamine. It is based on oxidation with potassium iodate at room temperature and measurement of the liberated iodine at 520 nm after extraction with carbon tetrachloride. Compared with other procedures, this method proved to be more rapid, highly reproducible and reasonably accurate. The relative standard deviation did not exceed 0.9% and 0.4% for penicillin and penicillamine, respectively. The procedure has been successfully applied to pharmaceutical preparations containing either of the two compounds. 相似文献
6.
流动注射化学发光法测定青霉素G钾 总被引:1,自引:0,他引:1
在甲醛的存在下,酸性KMnO4与青霉素G钾能够产生很强的化学发光,从而建立了KMnO4-甲醛-青霉素G钾化学发光体系来测定青霉素G钾.青霉素G钾的测定线性范围为2.0×10-7~1.0×10-5 g/mL,方法的检出限为1.4×10-7 g/mL,对4.0×10-7 g/mL的青霉素G钾进行11次平行测定,相对标准偏差为1.0%,用此法测定青霉素G钾取得了较好的结果. 相似文献
7.
Illanes A Wilson L Caballero E Fernández-Lafuente R Guisán JM 《Applied biochemistry and biotechnology》2006,133(3):189-202
Crosslinked enzyme aggregates (CLEAs) of a partially purified penicillin acylase from a recombinant Escherichia coli strain have been produced as a novel type of biocatalysts well endowed to perform in organic media. Different protein precipitants
were studied and glutaraldehyde was used as the crosslinking agent. Precipitation curves were obtained for all precipitants
to determine the concentrations at which all the protein precipitated out of the solution. The effect of the glutaraldehyde-to-protein
ratio was studied with respect to process recovery and the specific activity and stability of the biocatalyst. Recovery of
penicillin acylase activity was moderately high, about 50%; major losses of enzyme activity were produced at the precipitation
step. Specific activities of all CLEAs were very high, which is one of the advantages of using nonsupported biocatalysts.
Ammonium sulfate and tert-butyl alcohol were the best precipitants at a glutaraldehyde-protein mass ratio of 2 and were selected to perform the kinetically
controlled synthesis of ampicillin in 60% (v/v) ethylene glycol medium. At comparable conversion yields, volumetric and specific
antibiotic productivity were much higher for CLEAs than for carrier-bound penicillin acylases. 相似文献
8.
9.
Poly[(glycidyl methacrylate)-co-(glycerol monomethacrylate)]-grafted magnetic microspheres were prepared by graft random copolymerization via ATRP from polymer microspheres with dispersed Fe(3)O(4) nanoparticles. Penicillin G acylase (PGA) was immobilized onto the polymer brush-grafted magnetic microspheres. The immobilized PGA prepared with initial glycidyl methacrylate/glycerol monomethacrylate ratios of 40/60 to 60/40 possessed higher catalytic activity than that prepared with higher proportions of glycidyl methacrylate in the initial monomer mixture. The immobilized PGA showed high thermal stability and enhanced tolerability to the pH variance. 相似文献
10.
在稀HCl介质中,K3[Fe(CN)6]与阿莫西林(AMO)、氨苄西林(AMP)、氯唑西林钠(CLO)、羧苄西林钠(CAR)和青霉素钠(BEN)等抗生素药物在加热条件下反应生成结合产物,会导致溶液的共振瑞利散射(RRS)强度急剧增强,并产生新的RRS光谱,5种反应产物的最大散射峰均位于330 nm附近。在一定的浓度范围内,不同的反应体系散射强度(∆I)与药物浓度成正比,反应具有很高的灵敏度,K3[Fe(CN)6]对5种药物的检出限分别在4.61至5.62 ng·mL-1之间。本文研究了RRS的光谱特征和适当的反应条件,并讨论了反应机理和散射增强的原因,还考察了共存物质的影响,表明方法具有较好的选择性,可用于胶囊、片剂和人血清及尿液中青霉素类药物的测定。 相似文献