✦ LIBER ✦

Purification and properties of an extracellular levansucrase from Erwinia herbicola NRRL B-1678

✍ Scribed by Gregory L. Cote; Syed H. Imam

Publisher: Elsevier Science
Year: 1989
Tongue: English
Weight: 592 KB
Volume: 190
Category: Article
ISSN: 0008-6215
DOI: 10.1016/0008-6215(89)84132-1

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✦ Synopsis

Levansucrase (EC 2.4.1.10) was purified approximately 40-fold from the extracellular culture fluid of Erwiniu herbicolu NRRL B-1678. The purified enzyme in its native form occurred as an aggregate. Poly(acrylamide) gel electrophoresis in the presence of sodium dodecyl sulfate showed an active monomer having a molecular weight of 48,000. The enzyme had a K,,, for sucrose of 28mM and a pH optimum of 6.0, and was stable from -18 to t-52". It was free from cy-D-glucosidase, amylase, and glucansucrase activities, but exhibited considerable P-Dfructofuranosidase activity.

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