| Stabilization of invertase by molecular engineering. | |
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MedLine Citation:
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PMID: 19918887 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Extracellular invertase (EC 3.2.1.26) of Saccharomyces cerevisiae was stabilized against thermal denaturation by intermolecular and intramolecular crosslinking of the surface nucleophilic functional groups with diisocyanate homobifunctional reagents (O==C==N(CH(2))(n)N==C==O) of various lengths (n = 4, 6, 8). Crosslinking with 1,4-diisocyanatobutane (n = 4) proved most effective in enhancing thermostability. Stability was improved dramatically by crosslinking 0.5 mg/mL of protein with 30 mumol/mL of the reagent. Molecular engineering by crosslinking reduced the first-order thermal denaturation constant at 60 degrees C from 1.567 min(-1) (for the native enzyme) to 0.437 min(-1) (for the stabilized enzyme). Similarly, the best crosslinking treatment increased the activation energy for denaturation from 391 kJ mol(-1) (for the native protein) to 466 kJ mol(-1) (for the stabilized enzyme). Crosslinking was confirmed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. |
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Authors:
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Pattamawadee Tananchai; Yusuf Chisti |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Biotechnology progress Volume: 26 ISSN: 1520-6033 ISO Abbreviation: Biotechnol. Prog. Publication Date: 2010 Jan-Feb |
Date Detail:
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Created Date: 2010-02-15 Completed Date: 2010-05-24 Revised Date: 2011-05-26 |
Medline Journal Info:
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Nlm Unique ID: 8506292 Medline TA: Biotechnol Prog Country: United States |
Other Details:
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Languages: eng Pagination: 111-7 Citation Subset: IM |
Affiliation:
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School of Engineering, Massey University, Palmerston North, New Zealand. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Chemical Engineering* Cross-Linking Reagents / chemistry*, pharmacology Electrophoresis, Polyacrylamide Gel Enzyme Stability / drug effects Hot Temperature Protein Denaturation / drug effects Saccharomyces cerevisiae / enzymology beta-Fructofuranosidase / chemistry*, metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Cross-Linking Reagents; EC 3.2.1.26/beta-Fructofuranosidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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