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Characterisation of two alcohol acyltransferases from kiwifruit (Actinidia spp.) reveals distinct substrate preferences.

Günther, Catrin S. and Chervin, Christian and Marsh, Ken B. and Newcomb, Richard D. and Souleyre, Edwige J.F. Characterisation of two alcohol acyltransferases from kiwifruit (Actinidia spp.) reveals distinct substrate preferences. (2011) Phytochemistry, 72 (8). 700-710. ISSN 0031-9422

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Official URL: http://dx.doi.org/10.1016/j.phytochem.2011.02.026


Volatile esters are key compounds of kiwifruit flavour and are formed by alcohol acyltransferases that belong to the BAHD acyltransferase superfamily. Quantitative RT-PCR was used to screen kiwifruitderived expressed sequence tags with proposed acyltransferase function in order to select ripeningspecific sequences and test their involvement in alcohol acylation. The screening criterion was for at least 10-fold increased transcript accumulation in ripe compared with unripe kiwifruit and in response to ethylene. Recombinant expression in yeast revealed alcohol acyltransferase activity for Actinidia-derived AT1, AT16 and the phylogenetically distinct AT9, using various alcohol and acyl-CoA substrates. Functional characterisation of AT16 and AT9 demonstrated striking differences in their substrate preferences and apparent catalytic efficiencies ðV0 max K�1 m Þ. Thus revealing benzoyl-CoA:alcohol O-acyltransferase activity for AT16 and acetyl-CoA:alcohol O-acyltransferase activity for AT9. Both kiwifruit-derived enzymes displayed higher reaction rates with butanol compared with ethanol, even though ethanol is the main alcohol in ripe fruit. Since ethyl acetate and ethyl benzoate are major esters in ripe kiwifruit, we suggest that fruit characteristic volatile profiles result from a combination of substrate availability and specificity of individual alcohol acyltransferases.

Item Type:Article
Additional Information:Thanks to Elsevier editor. The definitive version is available at http://www.sciencedirect.com. The original PDF of the article can be found at Phytochemistry website : http://www.sciencedirect.com/science/article/pii/S0031942211001166
HAL Id:hal-02648925
Audience (journal):International peer-reviewed journal
Uncontrolled Keywords:
Institution:Université de Toulouse > Institut National Polytechnique de Toulouse - Toulouse INP (FRANCE)
French research institutions > Institut National de la Recherche Agronomique - INRA (FRANCE)
Other partners > The New Zealand Institute for Plant & Food Research (NEW ZEALAND)
Other partners > University of Auckland - UOA (NEW ZEALAND)
Laboratory name:
Deposited On:18 Oct 2011 10:05

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