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21.
介体型乳酸脱氢酶生物传感器的研制及应用 总被引:3,自引:0,他引:3
本报道了能对丙酮酸产生良好响应的电流型乳酸脱氢酶生物传感器。该传感器以耐尔兰A修饰浸石墨电极为基体电极,将酶直接固化在蚕丝蛋白膜上。在PH7.4的NaH2PO4-NaOH介质中,当2.4×10^-4mol/L的辅酶I(NADH)存在下,该传感器的响应电流与丙酮酸浓度在3.2×10^-5mol/L范围内有良好的线性关系。响应时间为60s.本讨论了影响传感器响应的各种因素,用此传感器测定了人血清中 相似文献
22.
Nils Siegbahn Mats-Olle Maånsson Klaus Mosbach 《Applied biochemistry and biotechnology》1987,12(2):91-105
A soluble, bifunctional enzyme complex has been prepared by crosslinking lactate dehydrogenase and alcohol dehydrogenase with
glutaraldehyde. The crosslinking was performed on a solid phase while the active sites of alcohol dehydrogenase and lactate
dehydrogenase were held adjacent to one another with the aid of a bis-NAD analog. Subsequently, the enzyme complex was released
from the solid phase. The soluble enzyme complex was then purified by using NAD-Sepharose as an affinity adsorbent. Based
on gel filtration experiments, the complex was estimated to consist of one of each dehydrogenase.
By using a third enzyme, lipoamide dehydrogenase, which competes with lactate dehydrogenase for NADH produced by alcohol dehydrogenase,
the effect of site-to-site orientation was studied. It was found that about 83% of the NADH produced by alcohol dehydrogenase
was oxidized by site-to-site oriented lactate dehydrogenase compared to a figure of only about 61% obtained in an identical
system of separate enzymes. This indicates that given two alternative routes, the preference for the one to lactate dehydrogenase
over the one to lipoamide dehydrogenase is enhanced when lactate dehydrogenase and alcohol dehydrogenase are site-to-site
oriented. 相似文献
23.
Fumihiko Hasumi Yasumitsu Miyamoto Ichiro Okura 《Applied biochemistry and biotechnology》1995,55(1):1-4
Glutamate synthesis by reductive amination of 2-oxoglutarate was performed by the combination of NADH regeneration system
and glutamate dehydrogenase (GluDH). The conversion of 2-oxoglutamate to glutamate was 98% after 3 h, and the turnover number
of NAD+was 17. 相似文献
24.
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26.
Isobaric vapor–liquid equilibrium (VLE) data of the reactive quaternary system ethanol (1) + water (2) + ethyl lactate (3) + lactic acid (4) have been determined experimentally. Additionally, the reaction equilibrium constant was calculated for each VLE experimental data. The experimental VLE data were correlated using the UNIQUAC equation to describe the chemical and phase equilibria simultaneously. For some of the non-reactive binary systems, UNIQUAC binary interaction parameters were obtained from the literature. The rest of the binary UNIQUAC parameters were obtained by correlating the experimental quaternary VLE data obtained in this work. A maximum pressure azeotrope at high water concentration for the binary reactive system ethyl lactate + water has been calculated. 相似文献
27.
介体型乙醇生物传感器的研制及应用 总被引:1,自引:0,他引:1
本文报道了电流型乙醇生物传感器的研制与应用。该传感器以健合型耐尔蓝修饰浸蜡石墨电极为基体电极,将乙醇脱氢酶及NAD^+固定在人造丝网上,成为一种无试剂的乙醇生物传感器。在pH8.8的Tris/HCl介质中,该传感器的响应电流与乙醇浓度在0.10-1.0mmol/l范围内有良好的线性关系。 相似文献
28.
Fumihiko Hasuni Katsunori Fukuoka Shuichi Adachi Yasumitsu Miyamoto Ichiro Okura 《Applied biochemistry and biotechnology》1996,56(3):341-344
Alanine synthesis by reductive amination of pyruvate was performed by the combination of NADH regeneration system and alanine
dehydrogenase (AlaDH). The conversion of pyruvate to alanine was 99% after 1 h. Leucine synthesis was also carried out by
the combination of NADH regeneration system and leucine dehydrogenase (LeuDH). The conversion of 4-methyl-2-oxovalerate to
leucine was 60% after 1.5 h. 相似文献
29.
含离子液体[bmim]Cl的反应介质中马肝醇脱氢酶的催化特性 总被引:2,自引:0,他引:2
研究了马肝醇脱氢酶(HLADH)在含离子液体1-丁基-3-甲基咪唑氯酸盐([bmim]Cl)的反应介质中的催化特性. 以乙醇为底物时,该酶在[bmim]Cl含量≤0.15 g/ml的体系中的活力高于在不含离子液体的体系中的活力; 离子液体浓度过高(>0.15 g/ml)对酶活性有明显的抑制作用. 反应温度和pH对含离子液体的反应介质中酶活力的影响规律与不含离子液体时的规律相似. 与不含离子液体的反应介质相比, HLADH在含0.05 g/ml [bmim]Cl的体系中催化乙醇氧化的活化能下降,酶反应的Vmax和Km均升高. 反应体系中低浓度(≤0.1 g/ml)的离子液体能提高酶的热稳定性,但高浓度(>0.1 g/ml)的离子液体可降低酶的热稳定性. 紫外二阶导数光谱显示,在含不同浓度离子液体的反应介质中酶分子构象的变化有较大的差异. 相似文献
30.
Francisco M. Gírio Fátima Pelica M. T. Amaral-Collaço 《Applied biochemistry and biotechnology》1996,56(1):79-87
The xylitol dehydrogenase (EC 1.1.1.9) from xylose-grown cells ofDebaryomyces hansenii was partially purified in two Chromatographic steps, and characterization studies were carried out in order to inves tigate
the role of the xylitol dehydrogenase-catalyzed step in the regu lation of D-xylose metabolism. The enzyme was most active
at pH 9.0–9.5, and exhibited a broad polyol specificity. The Michaelis con stants for xylitol and NAD+ were 16.5 and 0.55 mM, respectively. Ca2+, Mg2+, and Mn2+ did not affect the enzyme activity. Conversely, Zn2+, Cd2+, and Co2+ strongly inhibited the enzyme activity. It was concluded that NAD+-xylitol dehydrogenase from D.hansenii has similarities with other xylose-fermenting yeasts in respect to optimal pH, substrate specificity, and Km value for xylitol, and therefore should be named L-iditol:NAD+-5-oxidoreductase (EC 1.1.1.14). The reason D.hansenii is a good xylitol producer is not because of its value of Km for xylitol, which is low enough to assure its fast oxidation by NAD+ xylitol dehydrogenase. However, a higher Km value of xylitol dehydro genase for NAD+ compared to theK
m
values of other xylose-ferment ing yeasts may be responsible for the higher xylitol yields. 相似文献