Showing papers on "Xylanase published in 1976"
TL;DR: Results indicate that the xylanase activity of F-1 is intrinsic to the cellulase itself, as well as those calculated from the Michaelis-Menten treatment of two substances competing for the same active site of the enzyme.
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.
38 citations
TL;DR: Xylanase (EC 3.2.1.8) was purified from a crude extracellular enzyme of the wood-rotting fungusTrametes hirsuta by a four-step procedure involving precipitation with ammonium sulphate, gel filtration on Bio-Gel P-10, column chromatography on DEAE-Sephadex A-50 and preparative electrophoresis on polyacrylamide gel.
Abstract: Xylanase (EC 3.2.1.8) was purified from a crude extracellular enzyme of the wood-rotting fungusTrametes hirsuta by a four-step procedure involving precipitation with ammonium sulphate, gel filtration on Bio-Gel P-10, column chromatography on DEAE-Sephadex A-50 and preparative electrophoresis on polyacrylamide gel. The isolated enzyme, electrophoretically homogeneous, was separated from β-xylosidase and other hydrolytic enzymes studied. The analysis of the degradation products of water-soluble (4-0-methylglucurono)-D-xylan from willow by the purified xylanase showed it to be endoxylanase (β-1,4-xylan xylanohydrolase).
11 citations
TL;DR: The xylanase component was not stable, due to proteolytic enzymes in the rumen liquor, but could be purified by a variety of methods to give more-stable enzymes.
9 citations
01 Jan 1976
TL;DR: Some properties of xylanase produced by Pleurotus ostreatus during its gorwth in a rice straw medium were investigated and the activity was inhibited by managanous ion, but was increased by other metalic ions.
Abstract: Some properties of xylanase produced by Pleurotus ostreatus during its gorwth in a rice straw medium were investigated. The results are summarized as follows : 1) The optimum pH of xylanase was 5.0 and the stable pH ranged from 4.5 to 6.0. 2) The optimum temperature for the xylanse was around and the xylanse activity was completely lost in 10 minutes at 3) The activity of xylanse was inhibited by managanous ion, but was increased by other metalic ions. Especially K, Mg and Ca ions considerably increased the activity.
4 citations
TL;DR: A few mutants that were stable and highly productive of enzymes were obtained from Irpex lacteus Fr.
Abstract: A few mutants that were stable and highly productive of enzymes were obtained from Irpex lacteus Fr (KY 2901) on irradiation with ultraviolet light These mutants produced acid proteinases with little differences from that of the parent in connection with a crystal form, molecular weight, isoelectric point and some enzymatic properties such as pH optimum, pH stability and thermostabilityIt was, however, assumed that repetition of UV-irradiation caused some alterations in the net charge of the acid proteinase, because the isoelectric point of the enzyme from a mutant, 3U–39, was higher than that of other strainsMutants selected here exhibited coordinate increase of acid proteinase, α-amylase, β-1: 3-glucanase, xylanase and pectolytic enzymes
2 citations