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  • Xylanase activity of an endo-cellulase of carboxymethyl-cellulase type from Irpex lacteus (Polyporus tulipiferae).

Xylanase activity of an endo-cellulase of carboxymethyl-cellulase type from Irpex lacteus (Polyporus tulipiferae).

Journal of biochemistry (1976-05-01)
T Kanda, K Wakabayashi, K Nisizawa
PMID8438
ABSTRACT

An endo-cellulase [EC 3.2.1.4.] of carboxymethyl-cellulase type (F-1) which was fractionated from culture filtrate of Irpex lacetus and purified to electrophoretic and ultracentrifugal homogeneity, was found to show xylanase [EC 3.2.1.8.] activity. The activity was not removed from any of the intermediate fractions during the purification of the initial F-I peak, and the radio of xylanase to cellulase activity remained almost unchanged through the purification processes. The xylanase activity of F-I showed not only the same optiomal pH, heat stability, and pH stability as its cellulase activity, but also the same mobility as the cellulase activity upon cellulose acetate film and starch zone electrophoreses. The overall rates of hydrolysis of mixtures of variouis concentrations of CM-cellulose and xylan by F-1 coincided well with those calculated from the Michaelis-Menten treatment of two substances competing for the same active site of the enzyme. These results indicate that the xylanase activity of F-1 is intrinsic to the cellulase itself.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
β-Galactosidase from Escherichia coli, lyophilized powder, ≥500 units/mg protein
Sigma-Aldrich
β-Glucanase from Trichoderma longibrachiatum
Sigma-Aldrich
β-Glucanase from Aspergillus niger, powder, dark brown, ~1 U/mg