Coumaroyl Esterase

The degradation of plant cell walls requires fra/is-p-coumaroyl esterase, an important enzyme in the digestion of forages and dietary fiber. The trans-p-coumaric acid released by enzymatic hydrolysis was assayed by reversed-phase HPLC. 

The trans-a- and rrans-/3-anomers of the substrate, 0-[5-0-(trans-p-coumaroyl)-a-L-arabinofuranosyl] -(1 — 3)- 0-/3- D-xylopyranosyl-( 1— 4)-d-xylopyranose, were separated from each other and from the product, trans-p-coumaric acid, by chromatography on a Resolve C)8 column (3.9 mm X 150 mm). The mobile phase consisted of a 10 mM NaOH solution titrated to pH 3.0 with formic acid. Methanol was added to this solution to give a final concentration of 21% (v/v). The flow rate was 2 mL/min. The absorbance of the elute was monitored at 313 nm. 

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Bomeman, W. S., Ljungdahl, L. G., Hartley, R. D., and Akin, D. E., Isolation and characterization of p-coumaroyl esterase from the anaerobic fungus Neocallimastix strain MC-2. Appl Environ Microbiol 1991, 57 (8), 2337-44. 

Castanares, A., and Wood, T. M., Purification and characterization of a feruloyl/p-coumaroyl esterase from solid-state cultures of the aerobic fungus Penicillium pinophilum. Biochem Soc Trans 1992, 20 (3), 275S. 

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