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 |
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| Authors: | Jung Won Shin Sung Hee Choi Dong Eun Kim Hee Sook Kim Jae-Hwa Lee In Su Lee Eun Yeol Lee |
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| Affiliation: | (1) Department of Chemical Engineering, Industrial Liaison Research Center, Kyung Hee University, Gyeonggi-do, 446-701, Republic of Korea;(2) Department of Food Science and Biotechnology, Kyungsung University, Pusan, 608-736, Republic of Korea;(3) Department of Bioscience and Biotechnology, Silla University, Pusan, 617-736, Republic of Korea;(4) Department of Applied Chemistry, Kyung Hee University, Gyeonggi-do, 446-701, Republic of Korea; |
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| Abstract: | 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. |
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