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Rhizopus japonicus 의 효소에 의한 인삼 사포닌의 선택적 전환
김상달,서정훈 한국균학회 1986 韓國菌學會誌 Vol.14 No.3
The enzyme produced by a strain of Rhizopus japonicus was able to covert selectively ginsenoside Rb₁ which was the most abundant ginseng saponin, into ginsenoside Rd which was known to be superior to ginsenoside Rb₁ pharmaceutically. This specific conversion of ginsenoside Rb₁ without any change of other ginsenoside patterns was confirmed by thin layer chromatography and high performance liquid chromatograpy quantitatively. The amount of ginsenoside Rd was increased to 4.8 and 34.7 folds by enzymatic conversion of ginsenoside Rb₁ in total saponin and ginsenoside Rb group saponin, respectively. The increased amount of ginsenoside Rd corresponded to total amount of released glucose and decreased amount of ginsenoside Rb₁ accurately.
Monasucs 속 균주가 생성하는 Alkaline Protease 에 관한 연구
김상달,서정훈 한국농화학회 1972 Applied Biological Chemistry (Appl Biol Chem) Vol.15 No.1
The alkaline protease was isolated from the culture material of monascus sp. on wheat bran culture. The crude purification of this enzyme was extracted with distilled water and precipitated with ammonium sulfate of 0.5 saturation. And, the activity of this enzyme was determined very strongly by folin's colorimetric method. The optimal pH of this enzyme was ranging from pli 10 to 12 and the optimal temperature was 50℃. The pH stability was ranging from pH 5 to 12 and the enzyme activity was not inactivated by heat treatment in lower temperature than 40℃. The enzyme was protected from heat denature by the treatment of Pb^(++), Ba^(++), Co^(++), Zn^(++), and Cu^(++), but was inactivated with Hg^(++), Fe^(++) strongly. Moreover, one of these metal ions, the copper ion, has a strung protective activity on enzyme heat denature. And, it was not effected by treatment of EDTA.