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dc.contributor.authorLiang, Likun-
dc.contributor.authorChi, Zhenming-
dc.contributor.authorGao, Lingmei-
dc.contributor.authorMa, Liyan-
dc.identifier.issn0975-0959 (Online); 0301-1208 (Print)-
dc.description.abstractMutant 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.publisherNISCAIR-CSIR, Indiaen_US
dc.rights CC Attribution-Noncommercial-No Derivative Works 2.5 Indiaen_US
dc.sourceIJBB Vol.43(5) [October 2006]en_US
dc.subjectSaccharouiycopsis fibuligeraen_US
dc.subjectTrehalose-6-phopshate synthaseen_US
dc.subjectEnzyme purificationen_US
dc.subjectCharacterization of Tps1en_US
dc.titlePurification and characterization of trehalose-6-phosphate synthase from Saccharomycopsis fibuligera A11 en_US
Appears in Collections:IJBB Vol.43(5) [October 2006]

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