Abstract
The laboratory strain of S. cerevisiae, IM1-8b, showed pectolytic activity in the presence of either glucose, fructose, or sucrose as the carbon source, but not with galactose. The enzyme activity was rapidly lost with shaking. The optimum pH and temperature for activity were 4.5 and 45°C, respectively. The enzyme was an endopolygalacturonase, since it preferentially hydrolysed pectate over pectin and decreased the viscosity of a 5% polygalacturonic solution by about 30% in 30min producing oligogalacturonic acid and digalacturonic acid as end-products.
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References
Alaña, A., Gabilondo, A., Hernando, F., Moragues, M.D., Dominguez, J.B., Llama M.J. & Sierra, J.L. 1989 Pectin lyase production by a Penicillium italicum strain. Applied and Environmental, Microbiology 55, 1612–1616.
Albersheim, P. 1966 Pectin lyase from fungi. Methods in Enzymology 8, 628–631.
Blanco, P., Díaz, A., Sieiro, C & Villa, T.G. 1994 Production and partial characterization of an endopolygalacturonase from Saccharomyces cerevisiae. Canadian Journal of Microbiology 40, 974–977.
Gainvors, A., Frézier, V., Lemaresquier, H., Lequart, C., Aigle, M. & Belarbi, A. 1994. Detection of polygalacturonase, pectinlyase and pectin-esterase activities in a Saccharomyces cerevisiae strain. Yeast 10, 1311–1319.
McKay, A.M. 1990 Degradation of polygalacturonic acid by S. cerevisiae. Letters in Applied Microbiology 11, 41–44.
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Blanco, P., Sieiro, C., Di´az, A. et al. Differences between pectic enzymes produced by laboratory and wild-type strains of Saccharomyces cerevisiae. World Journal of Microbiology and Biotechnology 13, 711–712 (1997). https://doi.org/10.1023/A:1018587425202
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DOI: https://doi.org/10.1023/A:1018587425202