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KMID : 0665220030160020152
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Korean Journal of Food and Nutrition
2003 Volume.16 No. 2 p.152 ~ p.157
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Enzymatic Properties of Serratia marcescens Pretense
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Choi Byung-Bum
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Abstract
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Serratia marcescens ATCC 25419 protease was purified to homogeneity by ammonium sulfate treatment, and DEAE-cellulose anion exchange chromatography. The specific activity of the enzyme was increased 448-fold during purification with an overall yield of 43.0%. Metal reactivation on the purified protease from S. marcescens was studied. S. marcescens protease was a metalloenzyme to be completely inhibited its activity by EDTA and the enzyme outstandingly inhibited by Hg, Fe, Cu, but the activity was increased approximately 20% by Co. The reactivation of the apoenzyme was effective with Mn, Co, Zn in pH range from 6 to 8. Among metalloenzymes prepared to the addition of Mn, Co, Zn to restore the degree of activity of native enzyme, Zn-enzyme was similar to the native enzyme in respects with enzyme activity, alkali-inactivation, thermo-stability.
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KEYWORD
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protease, reactivation, purification, Serratia marcescens
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