Association of beta-glucosidase with intact cells of Thermoactinomyces.
The location of the B-glucosidase activity in a whole culture broth of the thermophilic organism Thermoactinomyces has been studied. Little beta-glucosidase activity was found in the culture filtrate, while the culture solids contained the major part of the activity of the whole culture broth. The activity does not appear to be adsorbed to the culture solids; rather there is evidence that it is an intracellular soluble enzyme(s). The pH and temperature optima for a crude beta-glucosidase preparation were determined to be pH 6.5 and 50--55 degrees C. Enzyme activity studies indicate that the same enzyme(s) accounts for the beta-glucosidase and the cellobiase activities. The validity of using the filter paper activity of culture filtrates from Thermoactinomyces to predict the total saccharification of cellulosic materials to glucose is discussed.
D002482:Cellulose / Q000378:metabolism; D005947:Glucose / Q000096:biosynthesis; D005959:Glucosidases / Q000378:metabolism*; D008848:Micromonosporaceae / Q000201:enzymology*; D013347:Subcellular Fractions / Q000201:enzymology; D001617:beta-Glucosidase / Q000378:metabolism*
D002482:Cellulose; D005959:Glucosidases; D001617:beta-Glucosidase; D005947:Glucose