• Korean journal of applied entomology
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• v.34 no.3
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• pp.181-190
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• 1995

Malate dehydrogenase in the mosquito ovary after a blood meal, Aedes aegypti, was purified and characterized. MDH purification steps involved DEAE-Sepharose, S-Sepharose and Cibacron blue affinity chromatography. The purified MDH was 70,000 daltons in molecular weight and was a homodimer consisting of tow identical subunits. Optimal activity of purified MDH was obtained pH 9.0-9.2 in malate-oxaloacetate reaction and pH 9.8-10.2, in oxaloactate-malate reaction. With obtained pH 9.0-92 in malate-oxaloacetate reaction and pH 9.8-10.2, in oxaloactate-malate reaction. With malate as substrate, purified mitochondrial MDH (1.28$\times$${10}^{-4}$ M) had lower Km value than cytoplasmic MDH (8.92x${10}^{-3}$ M). MDH activity was inhibited by citrate, $\alpha$-ketoglutarate, and ATP. Inhibition of MDH activity by ATP and citrate was less in malate-oxaloacetate reaction and in oxaloacetate-malate reaction. MDH activity was completely inhibited by ATP in oxaloacetate-malate reaction and not inhibited by citrate in malate-oxaloacetate reaction. Temporal activity change of MDH is similar to that of isocitrate dehydrogenase in the ovary after blood feeding; their activities in the ovary began to rise at 18 hours after a blood meal, and reached at the maximal level at 48 hours.

• KSBB Journal
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• v.9 no.3
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• pp.319-324
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• 1994

A biosensor for the measurement of malate has been constructed by the sodium-alginate immobilized bundle sheath cell tissue of corn leaf containing malate dehydrogenase (decarboxylating) (EC 1. 1. 1. 40) on the CO2 gas-sensing electrode. The proposed tissue sensor had the linear in the range of malate concentration $5.5{\times}10^{-5}M∼2.5{\times}10^{-2}M$ with a slope of 53.5 mV/decade in 0.02M Tris-HCl buffer solution at optimum pH 8.0, and $25^{\circ}C$. A response time was 16∼18min. The present L-malate sensing tissue sensor is stable for more than one week. At pH 7.4, Km value was $0.6{\times}10^{-5}M$. The various kinds of salt did not effect the signal of malate tissue biosensor as the inhibitor. We can measure the malate by the CO2 electrode at the pH=8.0. Thus, the proposed tissue sensor will be useful for the measurement of malate.

• Korean Journal of Food Science and Technology
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• v.16 no.1
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• pp.90-94
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• 1984

We deduced a possible metabolic pathway of L-malate in a malo-alcoholic yeast, Schizosaccharomyces japonicus var. japonicus St-3. The malic enzyme (EC 1.1.1.40) prepared from the microorganism was about four times as active as that of malate dehydrogenase (EC 1.1.1.37). And Km values of malic enzyme and malate dehydrogenase for malate were found to be 3.125 mM and 4.761 mM, respectively, which referred to the fact that the affinity of malic enzyme for the substrate was greater than that of malate dehydrogenase. We also found that pyruvate was produced with disappearing malate in malo-alcoholic fermentation, and that the addition of $Mn^{2+}$ activated malic enzyme activity. Based on these results obtained we have deduced a main pathway of malate${\rightarrow}$pyruvate${\rightarrow}$acetaldehyde${\rightarrow}$ethanol for the utilization of L-malate by this malo-alcoholic yeast strain.

• Preventive Nutrition and Food Science
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• v.4 no.1
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• pp.79-83
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• 1999

A potentiometric biosensor employing a CO3-2 ion-selective electrode(ISE) and malic enzyme immobilization in al flow injection analysis (FIA) system was constructed. Analytical parameters were optimized for L-malate determination . The CO3-2 -ISE-FIA system was composed of a pump, an injector, a malic enzyme (EC1.1.1.40) reactor, a CO3-2 ion-selective electrode, a pH/mV meter and a recorder. Cofactor NADP was also injected with substrate for theenzyme reaction into the system. Optimized analytical parameters for L-malate determination in the CO3-2 ISE-FIA system were as follows ; flow rate, 14.5ml/hr ; sample injection volume, 100ul; enzyme loading in the reactor, 20 units ; length of the enzyme reactor , 7 cm ; tubing length form the enzyme reactor to the detector as a geometric factor in FIA, 15 cm . The response time for measuring the entire L-malate concentration range (10-2 ~10-5 mol/L ; 4 injections )was <15minutes . In this CO3-2 -ISE-FIA system, the potential differences due to th eformation of CO3-2 by the reaction of malic enzyme on L-malate were correlated to L-malate concentration in the range of 10-2 ~10-5mol/L ; the detection limit was 10-5 mol/L. This potentionmetric CO3-2 ISE--FIA system was found to be useful for L-malate measurement.

• Journal of Microbiology and Biotechnology
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• v.7 no.6
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• pp.435-437
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• 1997

The role of $Ca^{2+}$ in making functional malate synthase in Corynebacterium glutamicum was investigated using the cloned DNA coding for the enzyme. Introduction of cloned aceB into C. glutamicum overexpressed malate synthase as judged by SDS-PAGE. However, the increase in enzyme activity of the expressed malate synthase did not match the level of overexpression observed in SDS-PAGE. Addition of $Ca^{2+}$ to the growth medium specifically increased the activity. The malate synthase could be stained with ruthenium red in a $Ca^{2+}$-specific manner. This agrees with the previous observation which reported a potential $Ca^{2+}$-binding domain in the N-terminal region of the protein.

• Korean Journal of Medicinal Crop Science
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• v.16 no.4
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• pp.261-267
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• 2008

Malate dehydrogenase is a ubiquitous enzyme in plants, involving in a range of metabolic processes depending on its subcellular location. A malate dehydrogenase (PgMDH) cDNA was isolated and characterized from the root of Panax ginseng C. A. Meyer. The deduced amino acid sequence of PgMDH showed high similarity with the NAD-dependent mitochondrial malate dehydrogenase from Glycinemax (P17783), Eucalyptus gunnii (P46487), and Lycopersicon esculentum (AAU29198). And the segment of a malate dehydrogenase gene was amplified through RT-PCR. The expression of PgMDH was increased after treatments of chilling, salt, UV, cadmium or copper treatment.

• Journal of Animal Science and Technology
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• v.51 no.6
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• pp.511-520
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• 2009

The purpose of this study was to investigate effects of increased levels of eugenol, thymol and malate on pH and the concentrations of VFA, lactate and ammonia-N during in vitro ruminal incubation. One Hanwoo beef steer (741 kg) fitted with a rumen cannula was used and fed 0.5 kg/day rice straw and 10 kg/day corn-based concentrate (ratio of concentrate to rice straw = 95 : 5 on DM basis). Three different doses of thymol, eugenol and malate were used. Treatments of the experiment were as follows: Treatments of thymol were control (1g D-glucose/40ml), T1 (1g D-glucose + 40 mg thymol/40 ml), T2 (1g D-glucose + 50 mg thymol/40 ml) and T3 (1g D-glucose + 60 mg thymol/40 ml). Treatments of eugenol were control (1g D-glucose/40 ml), E1 (1g D-glucose + 55 mg eugenol/40 ml), E2 (1g D-glucose + 65 mg eugenol/40 ml) and E3 (1g D-glucose + 75 mg eugenol/40 ml). Treatments of malate were control (1g D-glucose/40ml), M1 (1g D-glucose + 25 mg malate/40ml), M2 (1g D-glucose + 50 mg malate/40 ml) and M3 (1g D-glucose + 100 mg malate/40 ml). The results of this study showed that eugenol and thymol have improved stability of the ruminal fermentation by decreasing lactic acid concentration and increasing ruminal pH. However, it inhibited the production of total VFA, acetate and propionate. Malate also improved stability of the ruminal fermentation by decreasing lactic acid concentration and increasing ruminal pH, but it had a very little effect on ruminal lactate concentrations and pH. On the other hand, malate did not decrease the concentrations of total VFA, acetate and propionate. Therefore, at the low ruminal pH expected in high-concentrate diets, thymol, eugenol, and malate are potentially useful in Hanwoo finishing diets. Further studies are necessary for determining the effectiveness of these additives on in vivo rumen fermentation and animal performance in Hanwoo finishing steers.

• Asian-Australasian Journal of Animal Sciences
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• v.19 no.3
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• pp.368-375
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• 2006

Four rumen-fistulated dairy steers were randomly assigned according to a $4{\times}4$ Latin square design to investigate effects of supplementation levels of sodium dl-malate in concentrates on rumen ecology, ruminal fermentation, nitrogen balance, feed intake and digestibility of nutrients and ruminal microbial protein synthesis. The dietary treatments were cassava concentrate-based, containing sodium dl-malate supplementation at 0, 9, 18 and 27 g/hd/d with urea-treated rice straw (UTS) fed ad libitum. The experiment was conducted for four periods, each period lasting 21 days. Ruminal pH increased with incremental addition of malate (p<0.05). Additionally, molar proportions of propionate were higher in supplemented groups and was highest at 18 g/hd/d of malate supplement (p<0.05). Microbial protein synthesis tended to be higher in dairy steers receiving sodium dl-malate supplements and also was the highest at 18 g/hd/d. Variable bacterial populations, such as amylolytic, proteolytic and cellulolytic species were increased (p<0.05). Furthermore, protozoal populations were decreased significantly (p<0.05), while fungal zoospores were dramatically increased in dairy steers receiving sodium dl-malate supplement (p<0.05). These results suggested that supplementation of concentrate containing a high level of cassava chip at 18 g/hd/d with UTS in dairy steers could improve rumen fermentation efficiency and rumen microbial protein synthesis.

• International Journal of Industrial Entomology and Biomaterials
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• v.18 no.2
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• pp.91-95
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• 2009

The presence of considerable amount of enzymes of TCA cycle isocitrate dehydrogenase (ICDH-NADP+, EC1.1.1.42), $\alpha$-ketogluterate dehydrogenase ($\alpha$-KGD, EC1.2.4.2) and malate dehydrogenase (MDH, EC1.1.1.37) in fresh control and in vitro starved adult Isoparorchis hypselobagri establish the functional TCA cycle in this fluke. The major metabolic end products are pyruvate, lactate, oxaloacetate and malate. The ratio of oxaloacetate/malate assess that oxaloacetate is reduced to malate and in this fluke the reverse TCA cycle is active. The pyruvate/lactate ratio shows pyruvate is reduced to lactate and the fluke is homolactate farmenters.

• Journal of Plant Biology
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• v.22 no.3
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• pp.55-57
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• 1979

These studies were undertaken to determine the $CO^2$fixation patterns following the chloroplast development in maize leaves. At the early stage of chloroplast development $^{14}C$ was incorporated into aspartate (41%) and malate (22%) respectively. Whereas the incorporation of $^{14}C$ into malate was higher than that of aspartate as chloroplast developed. Activity of NADPH-dependent malate dehydrogenase was increased throughout chloroplast development, but that of aspartate transaminase was not. Much incorporation of $^{14}C$ into aspartate at the early stage of chloroplast development and into malate at later stage of chloroplast development lead us to conclude that NADPH-dependent malate dehydrogenase activity is closely associated with chloroplast development, but activity of aspartate transaminase is not.