Cell Wall Metabolism in Ripening Fruit

Abstract
A .beta.-1,4-xylanase has been purified from the mixture of carbohydrate-degrading enzymes found in a commercial preparation from cultures of Trichoderma viride. Purification from the desalted enzyme mixture is accomplished either by preparative isoelectric focusing or in 2-column chromatographic steps. The xylanase has maximal activity at pH 5.0 and a MW of approximately 13,000 daltons. The enzyme loses activity when heated to above 45.degree. C. The xylanase degrades xylans from larch and pear cell walls in an apparently endo-fashion.
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