Abstract
Several glycosidases have been isolated from suspensioncultured sycamore (Acer pseudoplatanus) cells. These include an alpha-galactosidase, an alpha-mannosidase, a beta-N-acetyl-glucosaminidase, a beta-glucosidase, and two beta-galactosidases. The pH optimum of each of these enzymes was determined. The pH optima, together with inhibition studies, suggest that each observed glycosidase activity represents a separate enzyme. Three of these enzymes, beta-glucosidase, alpha-galactosidase, and one of the beta-galactosidases, have been shown to be associated with the cell surface. The enzyme activities associated with the cell surface were shown to possess the ability to degrade to a limited extent isolated sycamore cell walls. It was found that the activities of beta-glucosidase and of one of the beta-galactosidases increase as the cells go through a period of growth and decrease as cell growth ceases.