고온성 알콜발효 효모의 Alcohol Dehydrogenase의 특성

  • Yea, Sang-Soo (Department of Microbiology, College of Natural Sciences, Kyungpook National University) ;
  • Lim, Si-Kyu (Department of Microbiology, College of Natural Sciences, Kyungpook National University) ;
  • Sohn, Ho-Yong (Department of Microbiology, College of Natural Sciences, Kyungpook National University) ;
  • Jin, Ing-Nyul (Department of Microbiology, College of Natural Sciences, Kyungpook National University) ;
  • Rhee, In-Koo (Department of Agricultural Chemistry, College of Agriculture, Kyungpook National University) ;
  • Kim, Young-Ho (Department of Microbiology, College of Natural Sciences, Kyungpook National University) ;
  • Seu, Jung-Hwn (Department of Microbiology, College of Natural Sciences, Kyungpook National University) ;
  • Park, Wan (Department of Microbiology, College of Natural Sciences, Kyungpook National University)
  • 예상수 (경북대학교 자연과학대학 미생물학과) ;
  • 임시규 (경북대학교 자연과학대학 미생물학과) ;
  • 손호용 (경북대학교 자연과학대학 미생물학과) ;
  • 진익렬 (경북대학교 자연과학대학 미생물학과) ;
  • 이인구 (경북대학교 농과대학 농화학과) ;
  • 김영호 (경북대학교 자연과학대학 미생물학과) ;
  • 서정훈 (경북대학교 자연과학대학 미생물학과) ;
  • 박완 (경북대학교 자연과학대학 미생물학과)
  • Published : 1997.08.01

Abstract

The characteristics of alcohol dehydrogenase (ADH, EC 1.1.1.1, alcohol:NAD oxidoreductase) of thermotolerant alcohol-producing yeasts, Saccharomyces cerevisiae RA-74-2 and Kluyveromyces marxianus RA-912, were compared with that of mesophilic S. cerevisiae D, an industrial strain. Under anaerobic culture condition, both S. cerevisiae RA-74-2 and D had similar level of ADH activity at 30$\circ$C, and the activity of S. cerevisiae RA-74-2 at 37$\circ$C was the same level at 30$\circ$C. However, the level of ADH activity of S. cerevisiae D at 37$\circ$C decreased about 70% of that at 30$\circ$C. The level of enzyme activity of K. marxianus RA-912, which showed lower alcohol productivity than S. cerevisiae RA-74-2 and D, was about 43% of those strains at 30$\circ$C, and decreased somewhat at 37$\circ$C. The results showed a good correlation between the alcohol productivities and the level of ADH activities of these strains grown at 30$\circ$C and 37$\circ$C. And the higher heat stability of ADH of S. cerevisiae RA-74-2 than that of S. cerevisiae D seemed to reflect the ability of high temperature fermentation. Despite of its fermentation ability even at 45$\circ$C, however, the ADH of K. marxianus RA-912 showed lower heat stability than that of S. cerevisiae D. Both S. cerevisiae RA-74-2 and D showed similar patterns of two bands of ADH isozyme, and the low band of S. cerevisiae RA-74-2 moved slightly faster than that of S. cerevisiae D. The staining intensity of the bands of S. cerevisiae D at 37$\circ$C was weaker than those at 30$\circ$C. However, S. cerevisiae RA-74-2 showed no differences in total intensity of the bands of 30$\circ$C and 37$\circ$C. As the patterns of cellular proteins and ADH isozyme of K. marxianus RA-912 were different from S. cerevisiae RA-74-2 and D, K. marxianus might have its own characteristic ADH system.

Keywords

High temperature fermentation;ADH;Isozyme;S. cerevisiae;K.marxianus