| 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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MedLine Citation:
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PMID: 20640446 Owner: NLM Status: In-Process |
Abstract/OtherAbstract:
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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 Ni(2+) 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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Authors:
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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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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-07-17 |
Journal Detail:
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Title: Bioprocess and biosystems engineering Volume: 34 ISSN: 1615-7605 ISO Abbreviation: Bioprocess Biosyst Eng Publication Date: 2011 Jan |
Date Detail:
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Created Date: 2011-01-03 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101088505 Medline TA: Bioprocess Biosyst Eng Country: Germany |
Other Details:
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Languages: eng Pagination: 113-9 Citation Subset: IM |
Affiliation:
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Department of Chemical Engineering, Industrial Liaison Research Center, Kyung Hee University, Gyeonggi-do 446-701, Republic of Korea. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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