Journal of Life Science

Korean Society of Life Science (한국생명과학회)
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Purification and Some Properties of an Extracellular Pectinase from Bacillus sp. BS-214

  • Jeon, Beong-Sam (Institute of Molecular and Cellular Biosciences, The Univetsity of Tokyo, Yayoi, Bunkyo-ku, Tokyo113-8657, Japan) ;
  • Song, Jae-Young (Dept. of Microbiology, College of Medicine, Gyeongsang National University, Chinju 660-750) ;
  • Lee, Gang-Deog (Dept. of Genetic Engineering Research Institute, Gyeongsang National University, Chinju 660-701) ;
  • Kim, Beom-Kyu (Dept. of Genetic Engineering Research Institute, Gyeongsang National University, Chinju 660-701) ;
  • Cha, Jae-Young (Faculty of Natural Resources and Life Science, Dong-A University, Pusan 604-714) ;
  • Lee, Young-Choon (Corresponding author, Faculty of Natural Resources and Life Science, Dong-A University, Pusan 604-714)
  • Published : 2000.04.01
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Abstract

Pectinase was isolated from culture medium of Bacillus sp. BS-214 and purified 105-fold with 3.4% yield by ammonium sulfate precipitation, gel filteration using Sephadex G-75 and DEAE-cellulose followed by gel filteration through Sephadex G-100. The molecular weight of the purified enzyme was estimated to be about 43 kDa on SDS-PAGE and by gel filtration, indicating that the enzyme is a monomer. the optium pH and temperature of the enzyme were 9.0 and 55$^{\circ}C$, respectively. the enzyme was stable at 60$^{\circ}C$ for 30min and in a pH range from 7.5 to 10.5 for 12 h ant 4$^{\circ}C$. The enzyme activity was highly enhanced by Ca2+, and also K+, Li+ and Na+showed a positive effect, while stongly inhibited by Zn2+ and Hg2+.

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