Purification and characterization of trehalose-6-phosphate synthase from Saccharomycopsis fibuligera A11.
Indian J Biochem Biophys
;
2006 Oct; 43(5): 289-94
Artigo
em Inglês
| IMSEAR
| ID: sea-27074
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 degrees 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, EDTA and PMSF.
Texto completo:
DisponíveL
Índice:
IMSEAR (Sudeste Asiático)
Assunto principal:
Inibidores de Proteases
/
Saccharomycopsis
/
Temperatura
/
Trealose
/
Sistema Livre de Células
/
Cromatografia em Gel
/
Cromatografia por Troca Iônica
/
Ácido Edético
/
Ácido Iodoacético
/
Glucosiltransferases
Idioma:
Inglês
Revista:
Indian J Biochem Biophys
Ano de publicação:
2006
Tipo de documento:
Artigo
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