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PLANT PHYSIOLOGY , Vol 107, Issue 2 331-339, Copyright © 1995 by American Society of Plant Biologists

BIOCHEMISTRY AND ENZYMOLOGY

A [beta]-Glucosidase from Lodgepole Pine Xylem Specific for the Lignin Precursor Coniferin

D. P. Dharmawardhana, B. E. Ellis and J. E. Carlson
Biotechnology Laboratory (D.P.D., J.E.C.), and Department of Plant Sciences (B.E.E.), #237-6174 University Boulevard, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3

Coniferin, the glucoside of the monolignol coniferyl alcohol, accumulates to high levels in gymnosperms during spring-cambial reactivation. A cinnamyl alcohol glucoside/[beta]-glucosidase system is thought to play a key role in lignification by releasing the monolignol aglycones. Investigation of such an enzyme system in the xylem of Pinus contorta var latifolia Engelm. revealed two major [beta]-glucosidases. One efficiently hydrolyzed the native substrate, coniferin, and the other was more active against synthetic glucosides. The coniferin [beta]-glucosidase was purified to apparent homogeneity using anion exchange, hydrophobic interaction, and size-exclusion chromatography. The apparent native molecular weight was estimated to be 60,000. A dominant 28-kD protein and a minor 24-kD protein were detected in the purified preparation following sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Immunological evidence from polyclonal antibodies directed against the synthetic N-terminal peptide of the 24-kD protein suggested that the native protein is a dimer of 28-kD subunit size. The N-terminal sequence showed that coniferin [beta]-glucosidase has high homology to known plant [beta]-glucosidases. Coniferin, syringin, and a synthetic coniferin analog were preferred substrates for the coniferin [beta]-glucosidase. In situ localization using the chromogenic coniferin analog showed the exclusive presence of [beta]-glucosidase activity in the differentiating xylem, similar to peroxidase activity.


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