• The Korea Journal of Herbology
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• v.22 no.4
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• pp.29-34
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• 2007

Objective : Kyenegum(Galli Stomachichum Corium) has been popularly used long as the digestive. The purpose of this study was to investigate the enzymatic characteristic of Kyenegum crude enzyme. Methods : To evaluate of the enzymatic characteristic of Kyenegum, we examined the activity of Kyenegum crude enzyme from optimum solvent, optimum temperature and pH of crude Kyenegum extract. Futhermore, we examined the effects of NaCI and acidity of crude Kyenegum extract. Results : The Kyenegum was composed with crude protein about 20%, crude lipid 2%. The optimum Kyenegum dry condition, optimum extract solvent, optimum temperature and optimum pH were $4{\sim}6$ hours at $60^{\circ}C$, commercial apple vinegar, $50^{\circ}C$ and 2.0. Conclusion : The result suggests that the Kyenegum crude enzyme extract very strong enzyme in temperature, NaCl and acidity, respectively.

• The Korea Journal of Herbology
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• v.22 no.4
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• pp.21-28
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• 2007

Objectives : Kyenegum has been popularly used long as the digestive. The purpose of this study was to investigate the purification and characteristics of protease obtained from Kyenegum crude enzyme. Methods : Kyenegum protease was purified by precipitation with ammonium sulfate followed by SP-Spharose ion exchange chromatography. The molecular weight of Kyenegum protease was estimated by SDS-PAGE electrophoresis. Results : Kyenegum protease was 3,087 units/mg protein specific activity, 14.5 purification fold and 9.8 % recovery. The molecular weight of protease was estimated to be 18 kDa. The isoelectric point was pI 8.97 and values of Km and Vmax of its were 48 mg/mL and 2 units/min, respectively. Conclusion : The result suggests that the protease obtained from Kyenegum has excellent stability of temperature, acid and collagen substrate specificity.

• Korean Journal of Pharmacognosy
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• v.32 no.3 s.126
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• pp.212-218
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• 2001

The water extracts of 82 Korean medicinal herbs were prepared and were examined for the binding affinity on the glycine binding site of NMDA (N-methyl-D-aspartate) receptor prepared by the synaptic membranes from the forebrains of male Sprague-Dawley rats. Among the tested, the extracts of Dioscoreae Rhizoma, Hoveniae Semen cum Fructus, Astragali Radix, Armeniacae Semen, Huttuynia cordata Herba, Acanthopanacis Cortex, Aurantii nobilis Pericarpium, Phellinus linteus, Amomi Fructus, Artemisiae capillaris Herba, Polyporus, Agastachis Herba and of Galli Stomachichum Corium were found to exhibit significant competitions with $[^3H]-MDL$ 105,519 for the glycine specific binding site of NMDA receptor in a dose dependent manner, respectively.