Production, localization and glucose repression of beta-glucosidase in Trichoderma longibrachiatum.
Optimal production of beta-glucosidase was obtained by incubating the culture at 27 degrees C in a growth medium that had an initial pH of 5.0 and contained cellobiose. The bulk of the enzyme (70%) was present in a cell-associated state (cell debris and cytosol) while only a small portion (30%) appeared in the culture filtrate. When cellulosic substrates were used, the major portion of the enzyme (70%) appeared in the extracellular fraction. A repression of the enzyme occurred in the presence of glucose. A drop of the pH of the medium during the exponential growth phase coincided with a rapid inactivation of the enzyme. The glucose effect was most likely mediated by adverse effects of low pH on the integrity of the enzyme.
D004794:Enzyme Repression; D005947:Glucose / Q000494:pharmacology*; D005959:Glucosidases / Q000096:biosynthesis*; D007700:Kinetics; D003904:Mitosporic Fungi / Q000201:enzymology*; D014242:Trichoderma / Q000201:enzymology* / Q000254:growth & development; D001617:beta-Glucosidase / Q000096:biosynthesis*
D005959:Glucosidases; D001617:beta-Glucosidase; D005947:Glucose