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Partial purification and properties of an invertase from Pseudomonas fluorescens

BUGBEE, W. M. 1984. Partial purification and properties of an invertase from P.S~U~O~O~~.S~~U O~~.TC~~.S. Can. J. Microbiol. 30: 1326- 1329. An intracellular P-fructofuranosidase was extracted from a sugar beet root isolate of P.seudomonns~7uoresc.ens. The enzyme was partially purified using Sephacryl 200 gel and anion-exchange column chromatography. The enzyme's molecular weight was estimated at 35 400 on a calibrated column of Sephacryl 200 gel. Two protein bands with molecular weights of 19 000 and 21 000 were evident after polyacrylamide gel electrophoresis in sodium dodecyl sulfate. The isoelectric point was pH 4.18. The K,,, of the enzyme was estimated at 90 rnM for sucrose. The optimum pH for activity was 6.5 when measured in a phosphate buffer.