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DC Field | Value | Language |
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dc.contributor.author | Liang, Likun | - |
dc.contributor.author | Chi, Zhenming | - |
dc.contributor.author | Gao, Lingmei | - |
dc.contributor.author | Ma, Liyan | - |
dc.date.accessioned | 2015-01-16T10:42:38Z | - |
dc.date.available | 2015-01-16T10:42:38Z | - |
dc.date.issued | 2006-10 | - |
dc.identifier.issn | 0975-0959 (Online); 0301-1208 (Print) | - |
dc.identifier.uri | http://hdl.handle.net/123456789/30374 | - |
dc.description | 289-294 | en_US |
dc.description.abstract | Mutant A11, a mutant of Saccharomycopsis fibuligera Sdu with low acid and neutral trehalase was found to accumulate over 18% (w/w) trehalose from starch in its cells. In this study, trehalose-6-phosphate synthase (Tps1) was purified to homogeneity from this mutant, with a 30-fold increase in the specific enzyme activity, as compared to the concentrated cell-free extract, from initial cells. The molecular mass of the purified enzyme as determined by SDS-PAGE was 66 kDa. The optimum pH and temperature of the purified enzyme were 6.6 and 37°C, respectively. The enzyme was activated by Ca2+, K+ and Mg2+, with K+ showing the highest activation at 35 mM. On the other hand, Mn2+, Cu2+, Fe3+, Hg2+ and Co2+ inhibited the enzyme. The enzyme was also strongly inhibited by protease inhibitors such as iodoacetic acid, EOTA and PMSF. | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | NISCAIR-CSIR, India | en_US |
dc.rights | ![]() | en_US |
dc.source | IJBB Vol.43(5) [October 2006] | en_US |
dc.subject | Saccharouiycopsis fibuligera | en_US |
dc.subject | Trehalose-6-phopshate synthase | en_US |
dc.subject | Enzyme purification | en_US |
dc.subject | Characterization of Tps1 | en_US |
dc.title | Purification and characterization of trehalose-6-phosphate synthase from Saccharomycopsis fibuligera A11 | en_US |
dc.type | Article | en_US |
Appears in Collections: | IJBB Vol.43(5) [October 2006] |
Files in This Item:
File | Description | Size | Format | |
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IJBB 43(5) 289-294.pdf | 1.39 MB | Adobe PDF | View/Open |
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