Extracellular beta-xylosidase (1,4-beta-D-xylan xylohydrolase, EC 3.2.1.37) from culture filtrates of Neurospora crassa was purified to homogeneity by preparative isoelectric focusing followed by gel electrophoresis. The molecular weight of the purified xylosidase was 83,000 D and the K(m) on p-nitrophenyl-beta-D-xyloside was 0.047mM. The homogeneous xylanase (1,4-beta-D-xylan xylanohydrolase, EC 3.2.1.8) and beta-xylosidase showed differences in their mode of action towards xylooligosaccharides. The degree of hydrolysis of D-xylan by xylanase of N. crassa was 18%. Supplementation of beta-xylosidase from the same organism resulted in 48% hydrolysis. The synergistic effect was more pronounced, with the hydrolysis of 68%, when a homogeneous preparation of beta-xylosidase from Sclerotium rolfsii was added to the saccharification system.
Endoglucanase, one part of the multicomponent enzyme cellulase, is an extremely important enzyme
in the textile industry (biopolishing), the pulp and paper industry (de-inking operations and recycling of
used paper), and the detergent industry. One major problem in such applications is the inactivation of the
enzyme at elevated temperatures and pH conditions. We present herein details of the encapsulation of
this enzyme in thermally evaporated fatty amine films and studies of the enzymatic activity of the
biocomposite film under different pH and temperature conditions. Substrate protection of the enzyme by
carboxymethyl cellulose was essential to stabilize the enzyme against inactivation in the lipid matrix. The
optimum operation temperature shifted to higher values relative to that of the free enzyme in solution.
The enhanced stability at high temperatures coupled with significant catalytic activity of the enzyme−lipid biocomposite films at elevated pH conditions indicate immediate application of the biocomposite film
in high temperature−high pH industrial applications.
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