Increased thermal stability of the enzyme content in permeabilized whole cells from the fission yeast Schizosaccharomyces pombe by exogenous trehalose and other compounds.
Cells of the fission yeast Schizosaccharomyces pombe were permeabilized by treatment with toluene-ethanol. The permeabilized cells lost the bulk of the internal trehalose pool while most of the alkaline phosphatase, invertase, alpha-glucosidase, or neutral trehalase activities located inside the cells remained unaffected. This system was used as an in situ assay to determine the involvement of trehalose in enzyme protection during thermal treatments. The addition of trehalose to suspensions of permeabilized cells resulted in a sugar-dependent thermoprotection of the internal marker enzymes. This approach demonstrates that in whole cells of the fission yeast trehalose plays a physiological role as a protective molecule against thermal denaturation of cellular enzymes.
Fernández
J
J
Department of Genetics and Microbiology, Facultad de Biología, University of Murcia, Spain.
Soto
T
T
Vicente-Soler
J
J
Cansado
J
J
Gacto
M
M
D000469:Alkaline Phosphatase / Q000378:metabolism; D002463:Cell Membrane Permeability; D004795:Enzyme Stability / Q000187:drug effects*; D005656:Fungal Proteins / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism; D006358:Hot Temperature; D012568:Schizosaccharomyces / Q000201:enzymology*; D014198:Trehalase / Q000378:metabolism; D014199:Trehalose / Q000378:metabolism / Q000494:pharmacology*; D000520:alpha-Glucosidases / Q000378:metabolism; D043324:beta-Fructofuranosidase
D005656:Fungal Proteins; D014199:Trehalose; D000469:Alkaline Phosphatase; D006026:Glycoside Hydrolases; D000520:alpha-Glucosidases; D043324:beta-Fructofuranosidase; D014198:Trehalase