• Title/Summary/Keyword: Candida sp. BT001

Search Result 2, Processing Time 0.014 seconds

Direct Fermentation of D-Xylose to Ethanol by Candida sp. BT001

  • LEE, SANG-HYEOB;WON-GI BANG
    • Journal of Microbiology and Biotechnology
    • /
    • v.4 no.1
    • /
    • pp.56-62
    • /
    • 1994
  • A yeast strain, BT001, which can directly ferment D-xylose to ethanol was isolated from forest soils, and then identified as Candida sp. Cultural conditions for the optimum ethanol production, along with the effects of aeration on cell growth and ethanol production were investigated. Aeration stimulated the cell growth and the volumetric rate of ethanol production, but decreased the ethanol yield. Optimum temperature and initial pH for the ethanol production were $33{\circ}^C$ and 6.0, respectively. In a shake flask culture, this strain produced 52.3 g ethanol per liter from 12%(w/v) D-xylose after incubation for 96 hours. Ethanol yield was 0.436 g per g D-xylose consumed. This corresponds to 85.8% of theoretical yield. Also, this yeast strain produced ethanol from D-galactose, D-glucose and D-mannose, but not from L-arabinose and L-rhamnose. Among these sugars, D-glucose was the fastest in being converted to ethanol sugars.

  • PDF

Purification of xylose reductase from Candida sp. BT001 and characterization of its properties (Candida sp. BT001의 xylose reductase의 정제 및 성질)

  • Hwang, In-Gyun;Lee, Sang-Hyub;Lee, Wang-Sik;Bang, Won-Gi
    • Applied Biological Chemistry
    • /
    • v.36 no.3
    • /
    • pp.178-183
    • /
    • 1993
  • Xylose reductase (alditol: $NADP^+$ 1-oxidoreductase, EC 1.1.1.21) from the xylose-fermenting yeast, Candida sp. BT001, was purified via salt fractionation, ion-exchange, gel filtration and affinity chromatography, and its properties were characterized. The enzyme from the yeast was active with both NADPH and NADH as coenzyme. The xylose reductase activity with NADH was approximately 51% of that with NADPH and the specific activities of purified enzyme with NADPH and NADH were 11.78 U/mg and 6.01 U/mg, respectively. Molecular weight of the purified enzyme was 31,000 on SDS-PAGE and 61,000 on gel filtration. The Km for D-xylose, NADPH, and NADH was $94.2{\times}10^{-3}M,\;0.011{\times}10^{-3}M\;and \;0.032{\times}10^{-3}M$, respectively. The purified xylose reductase had relatively higher substrate affinity for L-arabinose than other aldoses tested. The optimal pH was 6.2 and the optimal reaction temperature was $45^{\circ}C$. The thermal stability of the enzyme was for 20 minutes at $30^{\circ}C$.

  • PDF