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

• 발행기관: 한국축산식품학회
• 저자명: 전태욱 박기문
• 간행물 정보: 『Food Science of Animal Resources』Korean Journal for Food Science of Animal Resources 제22권 제3호, 259~266쪽, 전체 8쪽
• 주제분류: 농수해양 > 식품과학
• 파일형태: PDF
• 발행일자: 2002.09.30

영문 초록

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).