Purification and some properties of extracellular invertase B from Zymomonas mobilis |
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Authors: | Patrick J O'Mullan Theodore Chase Jr Douglas E Eveleigh |
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Institution: | (1) Department of Biochemistry and Microbiology, Cook College, Rutgers University, P. O. Box 231, 08903 New Brunswick, NJ, USA |
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Abstract: | Zymomonas mobilis is a Gram-negative ethanologen that can ferment glucose, fructose, and sucrose. Three enzymes that hydrolyze sucrose were found in a zymogram of electrophoretically separated proteins of Z. mobilis CP4. Two were invertase,, Inv A and Inv B; the latter was studied. Inv B is extracellular and accounts for at least 60% of the saccharolytic activity found in the culture broth of Z. mobilis CP4. The enzyme was purified 51-fold in 17% yield from culture broth of Z. mobilis grown on sucrose. It is a -fructosidase, monomeric with a molecular mass of 47 kDa and pI of 4.3. Its K
m for sucrose is 86 mm, and it has high catalytic activity (V
max = 1800 mol product/min per milligram protein). The purification and some properties of Inv B are presented.
Correspondence to: D. E. Eveleigh |
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