Heterologous expression of an alginate lyase from Streptomyces sp. ALG-5 in Escherichia coli and its use for preparation of the magnetic nanoparticle-immobilized enzymes
- First Online:
- 417 Downloads
The marine alginate lyase from Streptomyces sp. ALG-5, which specifically degrades poly-G block of alginate, was functionally expressed as a His-tagged form with an Escherichia coli expression system. The recombinant alginate lyase expressed with pColdI at 15 °C exhibited the highest alginate-degrading activity. The recombinant alginate lyase was efficiently immobilized onto two types of magnetic nanoparticles, superparamagnetic iron oxide nanoparticle, and hybrid magnetic silica nanoparticle, based on the affinity between His-tag and Ni2+ that displayed on the surfaces of nanoparticles. An alginate oligosaccharide mixture consisting of dimer and trimer was prepared by the immobilized alginate lyase. The immobilized enzymes were re-used repeatedly more than 10 times after magnetic separation.
KeywordsImmobilization Alginate lyase Alginate oligosaccharide Streptomyces sp. ALG-5
- 3.Zhang Z, Yu G, Guan H, Zhao X, Du Y, Jiang X (2004) Preparation and structure elucidation of alginate oligosaccharides degraded by alginate lyase from Vibrio sp. 510. Carbohydr Res 258:187–197Google Scholar
- 15.Choi D, Ryu B-Y, Piao YL, Choi S-K, Jo B-W, Shin W-S, Cho H (2008) Studies on saccharification from alginate using Stenotrophomonas maltophilia. J Ind Eng Chem 14:182–186Google Scholar