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오성훈,오평수,Oh, Sung-Hoon,O, Pyong-Su 한국미생물 · 생명공학회 1991 한국미생물·생명공학회지 Vol.19 No.2
Mutation experiments were performed to select the mutant of Aspergillus niger 55, which had lost almost all the ability to produce transglucosidases but retained that of high productivity of raw meal saccharifying enzyme, by means of successive induction with N-methyl-N'-nitro-N-nitrosoguanidine(MNNG), ultraviolet(UV) light, and ${\gamma}$-rays. Also, we used the mutant enrichment techniques, such as liquid culture-filtration procedure and differential heat sensitivity of conidia, in order to increase the possibility of obtaining a mutant. The glucoamylase productivity of mutant PFST-38 was 11 times higher than that of the parent strain. The mutant PFST-38 was morphologically identical to the parent strain, except for the size of conidia, the tendency to form conidia and the lenght of conidiophore. Asp. niger mutant PFST-38 apeared to be useful for the submerged production of the raw corn meal saccharifying enzyme.
김무성,오평수,Kim, Moo-Sung,O, Pyong-Su 한국미생물 · 생명공학회 1991 한국미생물·생명공학회지 Vol.19 No.2
A bacterial strain NO. 32 which produced thermostable ${\alpha}$-amylase was isolated from soil and identified to genus of Bacillus. To enhance ${\alpha}$-amylase productivity, a successive mutation of Bacillus sp. No. 32 was attempted with treatment of N-methyl-N'-nitro-N-nitrosoguanidine (NTG). The resulting mutant, Bacillus sp. No. 32H417, which is risistant to refampicin and deficient in spore formation, produced about 90-fold high level of ${\alpha}$-amylase when compared with parental strain. The properties of the enzyme for thermostability were investigated. The optimal temperature and pH for enzyme reaction were 95$^{\circ}C$ and pH6.5, respectively, in the presence of 0.3mM $Ca^{2+}$ as an effective stabilizer.
Isolation of Neutral Protease Hyperproducing Bacillus sp. KN103N and Some Properties of the Enzyme
김홍립,오평수,Kim, Hong-Rip,O, Pyong-Su 한국미생물 · 생명공학회 1991 한국미생물·생명공학회지 Vol.19 No.2
A bacterial strain KN, which highly produced a protease, was isolated from several soil samples and identified to to belong to the genus Bacillus. We selected mutant strain Bacillus sp. KN103N, which was hyperproducer of protease and was resistant to D-cyclowerine, from the strain KN by several steps of mutagenesis. Neutral protease productivity of mutant strain KN103N was about 55 times as much as that of the original strain KN. The optimum pH and temperature for the enzyme activity were 7.0 and 50$^{\circ}C$, respectively and the enzyme was relatively stable at pH6.0~8.0 and below 40$^{\circ}C$. The enzyme was inactivated by EDTA, but not by DFP. These results indicate that the enzyme from Bacillus sp. KN103N was a neutral (metallo-) protease.