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. 1995 Apr;59(4):632-7.
doi: 10.1271/bbb.59.632.

Purification and characterization of extracellular alginate lyase from Enterobacter cloacae M-1

Y Nibu  1 , T Satoh, Y Nishi, T Takeuchi, K Murata, I Kusakabe
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Free article

Purification and characterization of extracellular alginate lyase from Enterobacter cloacae M-1

Y Nibu et al. Biosci Biotechnol Biochem. 1995 Apr.
Free article

Abstract

An alginate lyase from the culture supernatant of Enterobacter cloacae M-1 was purified by ammonium sulfate precipitation, cation-exchange chromatography (SP-Toyopearl), and gel filtration (Ultrogel AcA44). The final preparation thus obtained showed a single band on SDS-PAGE. The purified enzyme had the molecular weight of 38,000 and 32,000 by SDS-PAGE and gel filtration, respectively. The pI of the enzyme was 8.9. The optimum pH and temperature for the enzyme reaction were around 7.8 and 30 degrees C, respectively. The enzyme was unstable on heating. EDTA completely inhibited the enzyme activity, but the activity was completely restored by the treatment with CaCl2. The enzyme was specific for poly-guluronate and produced several kinds of unsaturated oligomers from the gluluronate. This suggested that the enzyme could be classified as an endo poly-guluronate lyase.

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