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SCOPUS 학술저널

난각막 분해를 위한 Bacillus licheniformis 로 부터 Keratinase 의 정제 및 특성

The egg shell membrane degrading isolated from soil was identified as Bacillus licheniformis by 16S rDNA identification method. A keratinase was isolated from the Bacillus licheniformis culture. DEAE-cellulose ion-exchange and Sephadex G-75 gel chromatograhies were used to purify the enzyme. The specific activity was increased 17.3-fold by the purification procedures. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis and Sephadex G-75 chromatography indicated that the purified keratinase was monomeric and had a molecular weight of 65 kDa. The enzyme showed optimum activity at pH 9.0, and was stable above pH 9.0. The optimum temperature was 50℃ and the enzyme was stable in the temperature ranges from 20℃ to 50℃. By the addition of 1mM and 10 mM FeSO4, the activities of the enzyme were increased to 111±4.6% and 133±3.79%, respectively. The keratinase was an alkaline serine protease because it was inhibited only by phenylmethylsulfonylfluorice (PMSF).

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