Enzymic Dissociation of Zea Shoot Cell Wall Polysaccharides

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Abstract
An endo-(1 .fwdarw. 4)-.beta.-xylanase [(1 .fwdarw. 4)-.beta.-D-xylan 4-xylanohydrolase, (EC 3.2.1.8)] was isolated from a commercial preparation of B. subtilis .alpha.-amylase (Novo Ban 120). The purified xylanase exhibited an optimum activity at pH 5.5, and maximum activity at a temperature of 50.degree. C. The enzyme digests a (1 .fwdarw. 4)-.beta.-D-xylan from larch yielding 4-linked xylobiose and xylotriose as predominant products but does not hydrolyze 4-linked xylotriose and xylobiose. The enzyme also digests a (1 .fwdarw. 3), (1 .fwdarw. 4)-.beta.-D-mixed linkage sequence xylan from Rhodymenia into 4-linked xylobiose and xylotriose and 3,4-mixed linked oligosaccharides having a degree of polymerization of .gtoreq. 4. This enzyme is capable of hydrolyzing sequences of .gtoreq. 4 (1 .fwdarw. 4)-.beta.-D-linked xylose residues.