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Micrococcus sp . LL3 가 생성하는 intracellular aminopeptidase 의 특성 및 정제
이시경(Si Kyung Lee),주현규(Hyun Kyu Joo) 한국응용생명화학회 1993 Applied Biological Chemistry (Appl Biol Chem) Vol.36 No.6
This paper describes the purification and partial characteristics of aminopeptidase from Microccus sp. LL3 to utilize the microorganism as a potential agent for industrial application for the purpose of shortening ripening period of cheddar cheese. The optimal temperature and pH for enzyme activity were 35℃ and 7.0, respectively for L-leucine -p-nitroanilide as substrate. The enzyme remained stable for 10 minutes up to 50℃. The activity of aminopeptidase was stimulated by Mg^(++) ion but strongly inhibited by Hg^(++), metal complexing reagents, ethylenediaminetetraacetate (EDTA) and 1,10-phenanthroline. The enzyme was thought to be metallopeptidase. This enzyme had a broad substrate specificity, but was inactive on peptide with arginine as N-terminal amino acid. An intracellular aminopeptidase from Micrococcus sp. LL3 was purified by chromatography on DEAE-Sephacel and filtration on Sepacryl S-300. The enzyme has a molecular weight of 43,500.
전통식품 ( 청국장 ) 으로 부터 fibrin 용해 세균의 분리 동정
허석,이시경,주현규 ( Seok Heo,Si Kyung Lee,Hyun Kyu Joo ) 한국응용생명화학회 1998 Applied Biological Chemistry (Appl Biol Chem) Vol.41 No.2
In this study, the bacteria which could hydrolyze the fibrin produced through the blood coagulation mechanism in the human body, were isolated from Chungkookjang. The KCK-7 strain was selected among the isolated bacteria as the best strain for fibrinolytic activity. It was spore forming and Gram positive. C_(15-0) anteisa fatty acid and C_(15-0) iso fatty acid were 40.85% and 19.47%, respectively as major component among its cellular fatty acid composition. It showed the similarity of 63.6%, compared with standard strain. It was thus identified to be Bacillus subtilis according to Bergey`s manual of systematic bacteriology and its fatty acid profiles af Gas chromatography. The optimum culture temperature and pH were 37℃ and 8 for the production of fibrinolytic enzyme by Bacillus subtilis KCK-7.
CaCO3 가 Bacillus subtilis 에 의한 청국장메주 발효에 미치는 영향
이강무(Kang Moo Lee),이시경(Si Kyung Lee),주현규(Hyung Kyu Joo) 한국응용생명화학회 1994 Applied Biological Chemistry (Appl Biol Chem) Vol.37 No.6
This study was carried out to investigate the effect of CaCO₃ on the Chungkook-jang Meju fermentation. B. subtilis was cultured on the Meju added 0, 0.01, 0.1, 1% CaCO₃, respectively, and the chemical composition, protease activity, amino acid and vitamin B complex were examined with fermentation time. The inner temperature of the CaCO₃ treatments during fermentation was increased as compared with the control group. Titratable acidity in Meju decreased as CaCO₃ cocentration increased. And protease activity and amino-nitrogen content were however high in same order. The content of amino acid was on the increase in every treatments, it made no difference between CaCO₃, treatments and the control. Vitamin B complex content in the CaCO₃ treatments was increased than in the control. The 0.01% added treatment showed the highest amount of vitamin B complex content in all the treatments.