SUMMARY: The extracellular polygalacturonate lyase of a Bacillus species isolated from water-stored Sitka spruce () 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.


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