1-O-tran.s-Cinnainoyl-β-D-glucopyranose: Alcohol Cinnamoyltransferase Activity in Fruits of Cape Gooseberry (Physalis peruviana L.)

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autoren

  • Stefan Latza
  • Ralf G. Berger

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OriginalspracheEnglisch
Seiten (von - bis)747-755
Seitenumfang9
FachzeitschriftZeitschrift fur Naturforschung - Section C Journal of Biosciences
Jahrgang52
Ausgabenummer11-12
PublikationsstatusVeröffentlicht - Dez. 1997

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.

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1-O-tran.s-Cinnainoyl-β-D-glucopyranose: Alcohol Cinnamoyltransferase Activity in Fruits of Cape Gooseberry (Physalis peruviana L.). / Latza, Stefan; Berger, Ralf G.
in: Zeitschrift fur Naturforschung - Section C Journal of Biosciences, Jahrgang 52, Nr. 11-12, 12.1997, S. 747-755.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

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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",
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Download

TY - JOUR

T1 - 1-O-tran.s-Cinnainoyl-β-D-glucopyranose

T2 - Alcohol Cinnamoyltransferase Activity in Fruits of Cape Gooseberry (Physalis peruviana L.)

AU - Latza, Stefan

AU - Berger, Ralf G.

PY - 1997/12

Y1 - 1997/12

N2 - 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.

AB - 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.

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KW - Flavour Precursor

KW - Glycoconjugate

KW - Methyl Cinnamate

KW - Phenylpropanoid Metabolism

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