DC Field | Value | Language |
---|---|---|
dc.contributor.advisor | Byun, Si-Myung | - |
dc.contributor.advisor | 변시명 | - |
dc.contributor.author | Lim, Moon-Young | - |
dc.contributor.author | 임문영 | - |
dc.date.accessioned | 2011-12-12T08:50:53Z | - |
dc.date.available | 2011-12-12T08:50:53Z | - |
dc.date.issued | 1979 | - |
dc.identifier.uri | http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=62415&flag=dissertation | - |
dc.identifier.uri | http://hdl.handle.net/10203/27824 | - |
dc.description | 학위논문 (석사) - 한국과학기술원 : 생물공학과, 1979.2, [ [iii], 81 p. ] | - |
dc.description.abstract | In order to develop a program to obtain the high activity and high purity of penicillin acylase, mutation and affinity chromatographic technique were studied using $\mbox{\underline{Bacillus}}$ $\mbox{\underline{megaterium}}$ ATCC 14945. An extracellular penicillin acylase (EC 3.5.1.11) from the medium of $\mbox{\underline{B}}$. $\mbox{\underline{megaterium}}$ culture was partially purified overall 446 folds by means of adsorption on celite, followed by an affinity chromatography using a Sepharose-1,6-diaminohexyl-penicillin V column. The partially purified enzyme of a specific activity of 1521 U/mg protein on benzylpenicillin showed 3 bands by 7\% polyacrylamide gel electrophoresis. The enzyme was inhibited by both reaction products, phenylacetic acid and 6-aminopenicillanic acid. Phenylacetic acid inhibited the enzyme competitively and 6-aminopenicillanic acid noncompetitively and inhibition constants were 45 mM and 26 mM, respectively Michaelis constant of the enzyme on benzylpenicillin was 4.5mM. The enzyme showed the maximum activity at 45$^\circ$C and pH8.7. The activation energy calculated by Arrhenius`` method was 4.57 cal/mole. The enzyme productivity was improved by control of fermentation conditions. When the cells were fermented with 20\% inoculum in reciprocal shaker at 250 rpm the enzyme productivity was 36.5 U/ml which was higher productivity compared with that of routine fermentation conditions, 5\% inoculum in rotary shaker at 250 rpm, of 15 U/ml. The strain of $\mbox{\underline{B}}$. $\mbox{\underline{magaterium}}$ ATCC 14945 was improved by mutation with UV irradiation followed by methylmethanesulfonate treatment. Two strains of mutant showed higher productivity of 44 U/ml and 56.6 u/ml, respectively, when they were fermented with 20\% inoculum in reciprocal shaker at 250 rpm. | eng |
dc.language | eng | - |
dc.publisher | 한국과학기술원 | - |
dc.subject | 단백질 분리. | - |
dc.title | (A) study on penicillin acylase from bacillus megaterium | - |
dc.title.alternative | Bacillus megaterium 의 penicillin acylase에 관한 연구 | - |
dc.type | Thesis(Master) | - |
dc.identifier.CNRN | 62415/325007 | - |
dc.description.department | 한국과학기술원 : 생물공학과, | - |
dc.identifier.uid | 000771123 | - |
dc.contributor.localauthor | Byun, Si-Myung | - |
dc.contributor.localauthor | 변시명 | - |
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