PURIFICATION AND CHARACTERIZATION OF TREHALOSE PHOSPHORYLASE FROM CATELLATOSPORA-FERRUGINEA

Trehalose phosphorylase was purified from the cell extracts of Catella tospora ferruginea, The enzyme had an apparent molecular weight of 400 ,000 by gel filtration and 98,000 by SDS-PAGE, suggesting that the enz yme was a tetramer. The enzyme was specific for trehalose in phosphoro lysis acid specific for beta-D-glucose l-phosphate in synthesis. In ad dition to D-glucose, D-xylose and D-fucose were also possible sugar ac cepters during synthesis. Phosphate ions were a key to the activity an d stability of the enzyme, controlling the equilibrium of the reversib le reaction and the heat stability of the enzyme. The enzyme was stron gly inhibited by p-chloromercuribenzoate and pyridoxal phosphate. The enzyme was inactivated by heat or by storage frozen with ammonium chlo ride and lithium chloride.