Purification and characterisation of a bifunctional alginate lyase from novel Isoptericola halotolerans CGMCC 5336
•This study was the first report on the alginate lyase from Isoptericola genus.•The lyase was purified through simple steps with specific activity of 8409.19U/ml.•This alginate lyase was a monomer with molecular mass of 28kDa.•The enzyme showed excellent thermostability and a broad pH range for acti...
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Veröffentlicht in: | Carbohydrate polymers 2013-11, Vol.98 (2), p.1476-1482 |
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Sprache: | eng |
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Zusammenfassung: | •This study was the first report on the alginate lyase from Isoptericola genus.•The lyase was purified through simple steps with specific activity of 8409.19U/ml.•This alginate lyase was a monomer with molecular mass of 28kDa.•The enzyme showed excellent thermostability and a broad pH range for activity.•The lyase had substrate specificity for polyguluronate and polymannuronate.
A novel halophilic alginate-degrading microorganism was isolated from rotten seaweed and identified as Isoptericola halotolerans CGMCC5336. The lyase from the strain was purified to homogeneity by combining of ammonium sulfate fractionation and anion-exchange chromatography with a specific activity of 8409.19U/ml and a recovery of 25.07%. This enzyme was a monomer with a molecular mass of approximately 28kDa. The optimal temperature and pH were 50°C and pH 7.0, respectively. The lyase maintained stability at neutral pH (7.0–8.0) and temperatures below 50°C. Metal ions including Na+, Mg2+, Mn2+, and Ca2+ notably increased the activity of the enzyme. With sodium alginate as the substrate, the Km and Vmax were 0.26mg/ml and 1.31mg/ml min, respectively. The alginate lyase had substrate specificity for polyguluronate and polymannuronate units in alginate molecules, indicating its bifunctionality. These excellent characteristics demonstrated the potential applications in alginate oligosaccharides production with low polymerisation degrees. |
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ISSN: | 0144-8617 1879-1344 |
DOI: | 10.1016/j.carbpol.2013.07.050 |