ENZYMATIC-PROPERTIES OF BETA-MANNANASE FROM POLYPORUS-VERSICOLOR

Substrate specificities and the kinetic parameters, Km and Vmax, of the four multiple enzyme forms of extracellular β-mannanase activity purified from Polyporus versicolor were determined. Although Km values were significantly greater than those encountered in other β-mannanase systems Vmax values were equivalent or much greater, rendering the physiological efficiencies of the β-mannanase comparable to those of other β-mannanases. All enzymes preferred glucomannan as substrate, were highly refractory at low concentrations to n-octylglucopyranoside, sodium deoxylcholate, and sodium dodecylsulfate, and were largely insensitive to methanol, ethanol, acetonitrile, and dimethylsulfoxide. © 1990.