1-O-tran.s-Cinnainoyl-β-D-glucopyranose
Alcohol Cinnamoyltransferase Activity in Fruits of Cape Gooseberry (Physalis peruviana L.)
- authored by
- 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 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.
- Organisation(s)
-
Institute of Food Chemistry
- Type
- Article
- Journal
- Zeitschrift für Naturforschung - Section C Journal of Biosciences
- Volume
- 52
- Pages
- 747-755
- No. of pages
- 9
- ISSN
- 0939-5075
- Publication date
- 12.1997
- Publication status
- Published
- Peer reviewed
- Yes
- ASJC Scopus subject areas
- General Biochemistry,Genetics and Molecular Biology
- Electronic version(s)
-
https://doi.org/10.1515/znc-1997-11-1205 (Access:
Open)
