| Molecular cloning and characterization of trehalose biosynthesis genes from hyperthermophilic archaebacterium Metallosphaera hakonesis. | |
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MedLine Citation:
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PMID: 18051363 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The trehalose (alpha-D-glucopyranosyl-[1,1]-alpha-D-glucopyranose) biosynthesis genes MhMTS and MhMTH, encoding a maltooligosyltrehalose synthase (MhMTS) and a maltooligosyltrehalose trehalohydrolase (MhMTH), respectively, have been cloned from the hyperthermophilic archaebacterium Metallosphaera hakonesis. The ORF of MhMTS is 2,142 bp long, and encodes 713 amino acid residues constituting a 83.8 kDa protein. MhMTH is 1,677 bp long, and encodes 558 amino acid residues constituting a 63.7 kDa protein. The deduced amino acid sequences of MhMTS and MhMTH contain four regions highly conserved for MTSs and three for MTHs that are known to constitute substrate-binding sites of starch-hydrolyzing enzymes. Recombinant proteins obtained by expressing the MhMTS and MhMTH genes in E. coli catalyzed a sequential reaction converting maltooligosaccharides to produce trehalose. Optimum pH of the MhMTS/MhMTH enzyme reaction was around 5.0 and optimum temperature was around 70 degrees C. Trehalose-producing activity of the MhMTS/ MhMTH was notably stable, retaining 80% of the activity after preincubation of the enzyme mixture at 70 degrees C for 48 h, but was gradually abolished by incubating at above 85 degrees C. Addition of thermostable 4-alpha-glucanotransferase increased the yield of trehalose production from maltopentaose by 10%. The substrate specificity of the MhMTS/MhMTH-catalyzed reaction was extended to soluble starch, the most abundant maltodextrin in nature. |
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Authors:
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Ju-Seok Seo; Ju Hee An; Moo-Yeol Baik; Cheon Seok Park; Jong-Joo Cheong; Tae Wha Moon; Kwan Hwa Park; Yang Do Choi; Chung Ho Kim |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of microbiology and biotechnology Volume: 17 ISSN: 1017-7825 ISO Abbreviation: J. Microbiol. Biotechnol. Publication Date: 2007 Jan |
Date Detail:
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Created Date: 2007-12-05 Completed Date: 2008-01-22 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 9431852 Medline TA: J Microbiol Biotechnol Country: Korea (South) |
Other Details:
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Languages: eng Pagination: 123-9 Citation Subset: IM |
Affiliation:
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Department of Agricultural Biotechnology and Center for Agricultural Biomaterials, Seoul National University, Seoul 151-921, Korea. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Base Sequence Cloning, Molecular DNA Primers / genetics DNA, Archaeal / genetics Enzyme Stability Escherichia coli / genetics Genes, Archaeal* Glucosidases / genetics, metabolism Glucosyltransferases / genetics, metabolism Glycogen Debranching Enzyme System / genetics, metabolism Hot Temperature Recombinant Proteins / genetics, metabolism Starch / metabolism Substrate Specificity Sulfolobaceae / enzymology, genetics*, metabolism* Thermotoga maritima / enzymology, genetics Trehalose / biosynthesis*, genetics |
| Chemical | |
Reg. No./Substance:
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0/DNA Primers; 0/DNA, Archaeal; 0/Glycogen Debranching Enzyme System; 0/Recombinant Proteins; 9005-25-8/Starch; 99-20-7/Trehalose; EC 2.4.1.-/Glucosyltransferases; EC 2.4.1.-/maltooligosyl trehalose synthase; EC 2.4.1.25/4 alpha-glucanotransferase; EC 3.2.1.-/Glucosidases; EC 3.2.1.141/maltooligosyl trehalose trehalohydrolase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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