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Showing papers on "Xylanase published in 1972"


01 Jan 1972
TL;DR: This study of the effect of phenolics and higher aromatic compounds on cellulase and xylanase production by wood-destroying fungi, showed an interference with the induction of enzymes.
Abstract: This study of the effect of phenolics and higher aromatic compounds on cellulase and xylanase production by wood-destroying fungi, showed an interference with the induction of enzymes. The mycelium age also influences the extracellular enzyme production.

16 citations


Journal ArticleDOI
TL;DR: The purified enzyme was stable over a wide pH range and had considerable resistance to thermal inactivation, which explains the enzyme's prolonged activity in water-stored spruce sapwood.
Abstract: SUMMARY: The extracellular polygalacturonate lyase of a Bacillus species isolated from water-stored Sitka spruce (Picea sitchensis) was purified by ammonium sulphate fractionation and CM-cellulose chromatography. Its specific activity increased 59-fold and amylase, protease and xylanase activities were removed. Degradation of the substrate was accompanied by a large decrease in viscosity, suggesting random attack. While calcium and strontium ions activated the enzyme, most divalent cations caused inhibition. Addition of EDTA resulted in complete inactivation. Enzyme activity was higher with acid soluble pectic acid than with sodium polypectate. The purified enzyme was stable over a wide pH range and had considerable resistance to thermal inactivation. This stability explains the enzyme's prolonged activity in water-stored spruce sapwood.

6 citations




Journal ArticleDOI
TL;DR: Bacillus subtilis forms a xylanase complex which does not depend on induction by xylane or xylose in the medium, andMaximal enzyme production was achieved at high but balanced amounts of C/N/P, although growth was strongly reprimed under these conditions.
Abstract: Bacillus subtilis forms a xylanase complex which does not depend on induction by xylane or xylose in the medium. The enzyme production is influenced by the kind of the carbon source, probably due to catabolic repression. The regulation of enzyme formation is complex in nature, because the C/N/P-Relation in the medium, cell mass, and growth phase influence the amount of enzyme in the culture fluid. Maximal enzyme production was achieved at high but balanced amounts of C/N/P, although growth was strongly reprimed under these conditions. A formation of cellulase, aryl-β-xylosidase and aryl-β-glucosidase could not be observed.

2 citations