Production of trehalose by intramolecular transglucosylation of maltose catalysed by a new enzyme from Thermus thermophilus HB-8
Thermus thermophilus HB-8 is a source of trehalose synthase (GTase), which catalyses conversion of maltose into trehalose. Specific activity of maltose transglucosylation by cell-free extracts of the bacteria was about 0.1 U mg −1 protein and precipitation at 28% saturation of ammonium sulphate caus...
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| Veröffentlicht in: | Food chemistry 2006-05, Vol.96 (1), p.8-13 |
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| creator | Zdziebło, Anna Synowiecki, Józef |
| description | Thermus thermophilus HB-8 is a source of trehalose synthase (GTase), which catalyses conversion of maltose into trehalose. Specific activity of maltose transglucosylation by cell-free extracts of the bacteria was about 0.1
U
mg
−1 protein and precipitation at 28% saturation of ammonium sulphate caused 3.5-fold enzyme purification. The optimum temperature for conversion of maltose into trehalose was 65
°C with about 27% of maximum activity at 85
°C. The highest GTase productivity was achieved at cultivation temperature over 60
°C and at NaCl concentration range of 0.1–0.5% (w/v). However, larger concentrations of sodium chloride in the growth media caused a remarkable decrease of GTase synthesis. The results, of ammonium sulphate fractionation and activity towards maltotriose (0.028
U
mg
−1), maltotetraose (0.16
U
mg
−1) and GlcαpNp (0.27
U
mg
−1), show that trehalose synthase and α-glucosidase activities reside in separate protein fractions of cell-free extracts from
T. thermophilus cells. |
| doi_str_mv | 10.1016/j.foodchem.2005.01.048 |
| format | Article |
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U
mg
−1 protein and precipitation at 28% saturation of ammonium sulphate caused 3.5-fold enzyme purification. The optimum temperature for conversion of maltose into trehalose was 65
°C with about 27% of maximum activity at 85
°C. The highest GTase productivity was achieved at cultivation temperature over 60
°C and at NaCl concentration range of 0.1–0.5% (w/v). However, larger concentrations of sodium chloride in the growth media caused a remarkable decrease of GTase synthesis. The results, of ammonium sulphate fractionation and activity towards maltotriose (0.028
U
mg
−1), maltotetraose (0.16
U
mg
−1) and GlcαpNp (0.27
U
mg
−1), show that trehalose synthase and α-glucosidase activities reside in separate protein fractions of cell-free extracts from
T. thermophilus cells.</description><identifier>ISSN: 0308-8146</identifier><identifier>EISSN: 1873-7072</identifier><identifier>DOI: 10.1016/j.foodchem.2005.01.048</identifier><identifier>CODEN: FOCHDJ</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>alpha-glucosidase ; Biological and medical sciences ; bioreactors ; enzymatic reactions ; enzyme activity ; enzyme substrates ; Food industries ; Fundamental and applied biological sciences. Psychology ; Intramolecular transglucosylation ; isomerases ; maltose ; maltotetraose ; maltotriose ; reducing sugars ; sodium chloride ; temperature ; Thermus thermophilus ; trehalose ; Trehalose synthase ; α-Glucosidase</subject><ispartof>Food chemistry, 2006-05, Vol.96 (1), p.8-13</ispartof><rights>2005 Elsevier Ltd</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.foodchem.2005.01.048$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17514257$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Zdziebło, Anna</creatorcontrib><creatorcontrib>Synowiecki, Józef</creatorcontrib><title>Production of trehalose by intramolecular transglucosylation of maltose catalysed by a new enzyme from Thermus thermophilus HB-8</title><title>Food chemistry</title><description>Thermus thermophilus HB-8 is a source of trehalose synthase (GTase), which catalyses conversion of maltose into trehalose. Specific activity of maltose transglucosylation by cell-free extracts of the bacteria was about 0.1
U
mg
−1 protein and precipitation at 28% saturation of ammonium sulphate caused 3.5-fold enzyme purification. The optimum temperature for conversion of maltose into trehalose was 65
°C with about 27% of maximum activity at 85
°C. The highest GTase productivity was achieved at cultivation temperature over 60
°C and at NaCl concentration range of 0.1–0.5% (w/v). However, larger concentrations of sodium chloride in the growth media caused a remarkable decrease of GTase synthesis. The results, of ammonium sulphate fractionation and activity towards maltotriose (0.028
U
mg
−1), maltotetraose (0.16
U
mg
−1) and GlcαpNp (0.27
U
mg
−1), show that trehalose synthase and α-glucosidase activities reside in separate protein fractions of cell-free extracts from
T. thermophilus cells.</description><subject>alpha-glucosidase</subject><subject>Biological and medical sciences</subject><subject>bioreactors</subject><subject>enzymatic reactions</subject><subject>enzyme activity</subject><subject>enzyme substrates</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Intramolecular transglucosylation</subject><subject>isomerases</subject><subject>maltose</subject><subject>maltotetraose</subject><subject>maltotriose</subject><subject>reducing sugars</subject><subject>sodium chloride</subject><subject>temperature</subject><subject>Thermus thermophilus</subject><subject>trehalose</subject><subject>Trehalose synthase</subject><subject>α-Glucosidase</subject><issn>0308-8146</issn><issn>1873-7072</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><recordid>eNo1kUFv1DAQhSMEEkvhL0AucEs6tpPYvgEV0EqVQKI9W7POuOuVEy92AgonfjqJtj2NRvO9J715RfGWQc2AdZfH2sXY2wMNNQdoa2A1NOpZsWNKikqC5M-LHQhQlWJN97J4lfMRADgwtSv-_Uixn-3k41hGV06JDhhipnK_lH6cEg4xkJ0DpvWGY34Is415CfikGDBMG29xwrBk6jclliP9KWn8uwxUuhSH8u5AaZhzOW0zng4-rMv150q9Ll44DJnePM6L4v7rl7ur6-r2-7ebq0-3FXEtp0qQViD3jWyF5Q3ruG6Rc-JCcr2XnZZOdqik0-A6aVG2veq51U5I3VEDKC6KD2ffU4q_ZsqTGXy2FAKOFOdsmBbAQPEVfP8IYrYY3Jra-mxOyQ-YFsNkyxreypV7d-YcRoMPaWXuf65P3WwaprVYiY9ngtZcvz0lk62n0VLvE9nJ9NEbBmYr0RzNU4lmK9EAM2uJ4j-gdZMQ</recordid><startdate>20060501</startdate><enddate>20060501</enddate><creator>Zdziebło, Anna</creator><creator>Synowiecki, Józef</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><scope>7QL</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20060501</creationdate><title>Production of trehalose by intramolecular transglucosylation of maltose catalysed by a new enzyme from Thermus thermophilus HB-8</title><author>Zdziebło, Anna ; Synowiecki, Józef</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e297t-3e9807b4753c2416295a22e23729b7697f76a87f90f67ca75d8d2c9f3796e40a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>alpha-glucosidase</topic><topic>Biological and medical sciences</topic><topic>bioreactors</topic><topic>enzymatic reactions</topic><topic>enzyme activity</topic><topic>enzyme substrates</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Intramolecular transglucosylation</topic><topic>isomerases</topic><topic>maltose</topic><topic>maltotetraose</topic><topic>maltotriose</topic><topic>reducing sugars</topic><topic>sodium chloride</topic><topic>temperature</topic><topic>Thermus thermophilus</topic><topic>trehalose</topic><topic>Trehalose synthase</topic><topic>α-Glucosidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zdziebło, Anna</creatorcontrib><creatorcontrib>Synowiecki, Józef</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zdziebło, Anna</au><au>Synowiecki, Józef</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Production of trehalose by intramolecular transglucosylation of maltose catalysed by a new enzyme from Thermus thermophilus HB-8</atitle><jtitle>Food chemistry</jtitle><date>2006-05-01</date><risdate>2006</risdate><volume>96</volume><issue>1</issue><spage>8</spage><epage>13</epage><pages>8-13</pages><issn>0308-8146</issn><eissn>1873-7072</eissn><coden>FOCHDJ</coden><abstract>Thermus thermophilus HB-8 is a source of trehalose synthase (GTase), which catalyses conversion of maltose into trehalose. Specific activity of maltose transglucosylation by cell-free extracts of the bacteria was about 0.1
U
mg
−1 protein and precipitation at 28% saturation of ammonium sulphate caused 3.5-fold enzyme purification. The optimum temperature for conversion of maltose into trehalose was 65
°C with about 27% of maximum activity at 85
°C. The highest GTase productivity was achieved at cultivation temperature over 60
°C and at NaCl concentration range of 0.1–0.5% (w/v). However, larger concentrations of sodium chloride in the growth media caused a remarkable decrease of GTase synthesis. The results, of ammonium sulphate fractionation and activity towards maltotriose (0.028
U
mg
−1), maltotetraose (0.16
U
mg
−1) and GlcαpNp (0.27
U
mg
−1), show that trehalose synthase and α-glucosidase activities reside in separate protein fractions of cell-free extracts from
T. thermophilus cells.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><doi>10.1016/j.foodchem.2005.01.048</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Food chemistry, 2006-05, Vol.96 (1), p.8-13 |
| issn | 0308-8146 1873-7072 |
| language | eng |
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| source | Elsevier ScienceDirect Journals |
| subjects | alpha-glucosidase Biological and medical sciences bioreactors enzymatic reactions enzyme activity enzyme substrates Food industries Fundamental and applied biological sciences. Psychology Intramolecular transglucosylation isomerases maltose maltotetraose maltotriose reducing sugars sodium chloride temperature Thermus thermophilus trehalose Trehalose synthase α-Glucosidase |
| title | Production of trehalose by intramolecular transglucosylation of maltose catalysed by a new enzyme from Thermus thermophilus HB-8 |
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