1-O-tran.s-Cinnainoyl-β-D-glucopyranose

Alcohol Cinnamoyltransferase Activity in Fruits of Cape Gooseberry (Physalis peruviana L.)

verfasst von: Stefan Latza, Ralf G. Berger
Abstract: 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 l-O-trans-cinnamoyl-β-D-gluco-pyranose: alcohol cinnamoyltransferase from cape gooseberry (Physalis peruviana L.) was active towards l-O-trans-cinnamoyl-β-D-glucopyranose and l-O-trans-cinnamoyl-β-D-gentio-biose. The enzyme was purified 290-fold by a protocol including ammonium sulphate precipitation, solubilization by Triton X-100, gel permeation and affinity chromatography on conca-navalin 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 M_rof 75,000. For l-O-trans-cinnamoyl-β-D-glucopyranose, an apparent K_mof 69 was determined. At pH > 6.0, non-enzymatic transesterification superposes the enzymatic transformation.
Organisationseinheit(en): Institut für Lebensmittelchemie
Typ: Artikel
Journal: Zeitschrift für Naturforschung - Section C Journal of Biosciences
Band: 52
Seiten: 747-755
Anzahl der Seiten: 9
ISSN: 0939-5075
Publikationsdatum: 12.1997
Publikationsstatus: Veröffentlicht
Peer-reviewed: Ja
ASJC Scopus Sachgebiete: Allgemeine Biochemie, Genetik und Molekularbiologie
Elektronische Version(en): https://doi.org/10.1515/znc-1997-11-1205 (Zugang: Offen)

BibTeX

@article{362cae9ca9204ce8a312603bc9ef0fc8,
title = "1-O-tran.s-Cinnainoyl-β-D-glucopyranose: Alcohol Cinnamoyltransferase Activity in Fruits of Cape Gooseberry (Physalis peruviana L.)",
abstract = "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 l-O-trans-cinnamoyl-β-D-gluco-pyranose: alcohol cinnamoyltransferase from cape gooseberry (Physalis peruviana L.) was active towards l-O-trans-cinnamoyl-β-D-glucopyranose and l-O-trans-cinnamoyl-β-D-gentio-biose. The enzyme was purified 290-fold by a protocol including ammonium sulphate precipitation, solubilization by Triton X-100, gel permeation and affinity chromatography on conca-navalin 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 Mrof 75,000. For l-O-trans-cinnamoyl-β-D-glucopyranose, an apparent Kmof 69 was determined. At pH > 6.0, non-enzymatic transesterification superposes the enzymatic transformation.",
keywords = "Aroma Ester, Flavour Precursor, Glycoconjugate, Methyl Cinnamate, Phenylpropanoid Metabolism",
author = "Stefan Latza and Berger, {Ralf G.}",
year = "1997",
month = dec,
doi = "10.1515/znc-1997-11-1205",
language = "English",
volume = "52",
pages = "747--755",
journal = "Zeitschrift f{\"u}r Naturforschung - Section C Journal of Biosciences",
issn = "0939-5075",
publisher = "Tubingen Verlag Der Zeitschrift Fuer Naturforschung",
number = "11-12",
}