Microbiology and Biotechnology Letters (한국미생물·생명공학회지)

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Characteristics and Action Pattern of Alikaline Lipase from Serratia liquefaciens AL-11

Serratia liquefaciens AL-11이 생산하는 Alkaline Lipase의 특성 및 작용양상

  • Choi, Cheong (Department of Food Science and Technology, Yeungnam University) ;
  • Kim, Tae-Wan (Department of Food Science and Technology, Yeungnam University) ;
  • Ahn, Bong-Jeon (Department of Cosmetic Engineering, Dongkook Jr. College) ;
  • Kim, Yung-Hwal (Department of Clinical Pathology, Taegu Health Jr. College) ;
  • Son, Jun-Ho (Department of Food Science and Technology, Yeungnam University) ;
  • Kim, Sung (Department of Food Science and Technology, Yeungnam University) ;
  • Choi, Hee-Jin (Department of Food Science and Technology, Yeungnam University)
  • 최청 (영남대학교 자연자원대학 식품가공학과) ;
  • 김태완 (영남대학교 자연자원대학 식품가공학과) ;
  • 안봉전 (동국전문대 향장공업과) ;
  • 김영활 (보건전문대 임상병리과) ;
  • 손준호 (영남대학교 자연자원대학 식품가공학과) ;
  • 김성 (영남대학교 자연자원대학 식품가공학과) ;
  • 최희진 (영남대학교 자연자원대학 식품가공학과)
  • Published : 1996.02.01
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Abstract

The optimum temperature and pH for the enzyme activity were 45$^{\circ}C$ and 10.0, respectively. The enzyme was stable in a pH range of 5 to 10, and 62% of its activity was lost on heat treatment of 60$^{\circ}C$ for 20 min. The activity of the purified enzyme was inhibited by $Fe^{2+},\;Zn^{2+}\;and\;Pb^{2+}$, and slightly activated by $Mn^{2+}\;and\;Ca^{2+}$. ${\gamma}$-Chloromercuribenzoic acid, 2,4-dinitrophenol and $H_{2}O_{2}$ did not show inhibitroy effect on the lipolytic activity of the alkaline lipase but ethylenediaminetetraacetic acid inhibited the enzyem activity. This suggested that the enzyme have metal group in its active site. Sodium salts of bile acids stimulated the enzyme activity. Analysis of hydrolyzates of olive oil after the reaction revealed that Serratia liquefaciens AL-11 produced non-specific lipolytic enzyme.

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