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Biosynthesis of alginate: Purification and characterisation of mannuronan C-5-epimerase from azotobacter vinelandii

✍ Scribed by Gudmund Skj»k-Bræk; Bjørn Larsen

Book ID
102991087
Publisher
Elsevier Science
Year
1985
Tongue
English
Weight
594 KB
Volume
139
Category
Article
ISSN
0008-6215

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✦ Synopsis

A mannuronan C-5-epimerase from the soil bacterium Azotobacter vinelundii has been highly purified and characterised. The enzyme is a single polypeptide chain with a mobility in gradient and SDS electrophoresis corresponding to a mol. wt. of 122,000; it has a p1 of 4, highest activity at pH 7.0, and an absolute requirement for Ca2+. The K,,, has been estimated for two different calcium concentrations, using [5-3H]alginate as substrate. A rapid purification procedure based on fast protein liquid chromatography on MonoQ (HO-) resin is described.

📜 SIMILAR VOLUMES

Mannuronan C-5-Epimerases and Their Appl
Mannuronan C-5-Epimerases and Their Application for in Vitro and in Vivo Design of New Alginates Useful in Biotechnology
✍ Helga Ertesvåg; Hilde Kristin Høidal; Hilde Schjerven; Britt Iren Glærum Svanem; 📂 Article 📅 1999 🏛 Elsevier Science 🌐 English ⚖ 224 KB

The industrially important polysaccharide alginate is a linear copolymer of ;-D-mannuronic acid (M) and :-L-guluronic acid (G). It is produced commercially by extraction from brown seaweeds, although some of the bacteria belonging to the genera Azotobacter and Pseudomonas also synthesize alginates.