Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/30374
Title: Purification and characterization of trehalose-6-phosphate synthase from Saccharomycopsis fibuligera A11
Authors: Liang, Likun
Chi, Zhenming
Gao, Lingmei
Ma, Liyan
Keywords: Saccharouiycopsis fibuligera;Trehalose-6-phopshate synthase;Enzyme purification;Characterization of Tps1
Issue Date: Oct-2006
Publisher: NISCAIR-CSIR, India
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.
Page(s): 289-294
URI: http://hdl.handle.net/123456789/30374
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.43(5) [October 2006]

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