Purification and characterization of Protease from Kyenegum

계내금(鷄內金) 단백질 분해 효소의 정제와 특성

  • Kim, Do-Wan (Dep. of Oriental Medicine Process, Kundong University) ;
  • Jo, Hye-Sim (Dep. of Food Science and Technology, Keimyung University) ;
  • Jeong, Yong-Jin (Dep. of Food Science and Technology, Keimyung University) ;
  • Kim, Kwang-Soo (Dep. of Food and Nutrition, Yeungnam University)
  • 김도완 (건동대학교 한약재개발학과) ;
  • 조혜심 (계명대학교 식품가공학과) ;
  • 정용진 (계명대학교 식품가공학과) ;
  • 김광수 (영남대학교 식품영양학과)
  • Published : 2007.12.31

Abstract

Objectives : Kyenegum has been popularly used long as the digestive. The purpose of this study was to investigate the purification and characteristics of protease obtained from Kyenegum crude enzyme. Methods : Kyenegum protease was purified by precipitation with ammonium sulfate followed by SP-Spharose ion exchange chromatography. The molecular weight of Kyenegum protease was estimated by SDS-PAGE electrophoresis. Results : Kyenegum protease was 3,087 units/mg protein specific activity, 14.5 purification fold and 9.8 % recovery. The molecular weight of protease was estimated to be 18 kDa. The isoelectric point was pI 8.97 and values of Km and Vmax of its were 48 mg/mL and 2 units/min, respectively. Conclusion : The result suggests that the protease obtained from Kyenegum has excellent stability of temperature, acid and collagen substrate specificity.

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