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KMID : 1024620020220030259
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Food Science of Animal Resources
2002 Volume.22 No. 3 p.259 ~ p.266
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Purification and Characterization of a Keratinase from Bacillus licheniformis Strain for Degradation of Egg Shell Membrane
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Jeon Tae-Woog
Park K. M.
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Abstract
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The egg shell membrane degrading isolated from soil was identified as Bacillus licheniformis by 16S rDNA identification method. A keratinase was isolated from the Baciilu licheniformis culture. DEAE-cellulose ion-exchange and Sephadex C-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 50t. By the addition of 1 mM and 10 mM FeSO4, the activities of the enzyme were increased to 1114.6% and 1333.79%, respectively. The keratinase was an alkaline serine pretense because it was inhibited only by phenylmethylsulfonylfluorice (PMSF).
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KEYWORD
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egg shell membrane, keratinase, Bacillus licheniformis
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