Triglucosylation on the biotransformation of (+)-menthol by cultured cells of Eucalyptus perriniana.

Cultured cells of Eucalyptus perriniana biotransformed (+)-menthol to its gentiobioside and triglucoside [2,6-di-O-(beta-D-glucopyranosyl)-beta-D-glucopyranoside]. The structures of these compounds were determined by means of NMR techniques.     

Immobilization and culture of coffee (Coffea arabica L.) cells on novel culture systems using a basket-shaped unit, “EGSTAR”

Summary A simple and new basket-shaped unit for agitation made of stainless steel (EGSTAR), in which immobilized coffee cells in Ca-alginate gel beads were packed, was placed in a jar fermentor (System-1). This system allowed the plant cells to grow submersed in the unit even at high agitation speed (650 rpm). Only a small amount of cells existed out of the EGSTAR. Most of the purine alkaloids produced were released into the medium. Suspended coffee cells in the jar fermentor were also possibly immobilized onto a polyurethane foam sheet fixed inside the net of the EGSTAR (System-2). The total cells in System-2 biotransformed theobromine to caffeine (77.9%). Other plant cell suspensions were also immobilized as efficiently as were the coffee cells in this system. Thus, System-2 is a simple and convenient system for immobilization of plant cells to produce secondary metabolites. This paper is Part 79 in the series of “Studies on Plant Tissue Cultures”. For Part 78, see Orihara, Y., Furuya, T., Hashimoto, N., Deguchi, Y., Tokoro, K., and Kanisawa, T., (1992)Phytochemistry 31: 827–831.     

Lysosomal sialidase deficiency in sialidosis with partial β-galactosidase deficiency

We analyzed the subcellular localization of sialidases in human lymphocytes from a patient with adult type sialidosis with partial β-galactosidase deficiency and normal controls. Sialidase activities were measured with α,2 → 3 NeuAc-lactitol, 4-methylumbelliferyl-NeuAc and G_M3 ganglioside as substrates. Sialidases in the lysosomes were sonication-labile and hydrolyzed mainly hydrophilic substrates such as NeuAc-lactitol and 4-methylumbelliferyl-NeuAc, but hydrolyzed subsidiarily G_M3 ganglioside. On the other hand, sialidases in the plasma membrane were sonication-stable and hydrolyzed both hydrophilic substrates and G_M3 ganglioside. In sialidosis with partial β-galactosidase deficiency, the sialidases of the lysosomes showed 3–5% activity toward hydrophilic substrates and 25% activity toward G_M3 ganglioside as compared with sialidase activities of the controls. However, there are no differences in the activities of the sialidases in the plasma membrane. These results demonstrate that the essential defect in this disease is the deficiency of a lysosomal sialidase.