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1-O-trans-Cinnamoyl-β-ᴅ -glucopyranose: Alcohol Cinnamoyltransferase Activity in Fruits of Cape Gooseberry (Physalis peruviana L.)

Stefan Latza, Ralf G. Berger
1997 Zeitschrift für Naturforschung C - A Journal of Biosciences  
Methyl and ethyl cinnamate are aroma volatiles frequently occurring in fruits. Evidence was obtained that the enzymatic transfer of cinnamic acid to endogenous alcohols present in fruits (methanol, ethanol, 1-propanol) depended on energy-rich 1-O-glycosyl esters of cinnamic acid which served as acyl donor molecules. A putative 1-O-trans-cinnamoyl-β-ᴅ-gluco-pyranose; alcohol cinnamoyltransferase from cape gooseberry (Physalis peruviana L.) was active towards 1-O-trans-cinnamoyl-β-ᴅ-glucopyranose
more » ... l-β-ᴅ-glucopyranose and 1-O-trans-cinnamoyl-β-ᴅ-gentiobiose. The enzyme was purified 290-fold by a protocol including ammonium sulphate precipi­tation, solubilization by Triton X-100, gel permeation and affinity chromatography on concanavalin A. The acidic glycoprotein (pI = 4.8) most probably is membrane bound. The distribution of alcohol cinnamoyltransferase activity in gel chromatography fractions suggests a native Mr of 75,000. For 1-O-trans-cinnamoyl-β-ᴅ-glucopyranose, an apparent Km of 69 μm was determined. At pH > 6.0, non-enzymatic transesterification superposes the enzymatic transformation.
doi:10.1515/znc-1997-11-1205 fatcat:bpppff64rfcfrmfwuimuxu4kyi