Please use this identifier to cite or link to this item: https://hdl.handle.net/1959.11/2766
Title: A seed coat cyanohydrin glucosyltransferase is associated with bitterness in almond ('Prunus dulcis') kernels
Contributor(s): Franks, Tricia K (author); Yadollahi, Abbas (author); Wirthensohn, Michelle G (author); Guerin, Jennifer R (author); Kaiser, Brent N (author); Sedgley, Margaret  (author); Ford, Christopher M (author)
Publication Date: 2008
DOI: 10.1071/FP07275
Handle Link: https://hdl.handle.net/1959.11/2766
Abstract: The secondary metabolite amygdalin is a cyanogenic diglucoside that at high concentrations is associated with intense bitterness in seeds of the Rosaceae, including kernels of almond ('Prunus dulcis' (Mill.), syn. 'Prunus amygdalus' D.A. Webb Batsch). Amydalin is a glucoside of prunasin, itself a glucosider of 'R'-mandelonitrile (a cyanohydrin). Here we report the isolation of an almond enzyme (UGT85A19) that stereo-selectively gucosylates 'R'-mandelonitrile to produce prunasin. In a survey of developing kernels from seven bitter and 11 non-bitter genotypes with polyclonal antibody raised to UGT85A19, the enzyme was found to accumulate to higher levels in the bitter types in later development. This differential accumulation of UGT85A19 is associated with more than three-fold greater mandelonitrile glucosyltrajsferase activity in bitter kernels compared with non-bitter types, and transcriptional regulation was demonstrated using quantitative-PCR analysis. UGT85A19 and its encoding transcript were most concentrated in the testa (seed coat) of the kernel compared with the embryo, and prunasin and amygdalin were differentially compartmentalised in these tissues. Prunasin was confined to the testa and amygdalin was confined to the embryo. These results are consisted with the seed coat being an important site of synthesis of prunasin as a precursor of amygdalin accumulation in the kernel. The presence of UGT85A19 in the kernel and other tissues of both bitter and non-bitter types indicates that its expression is unlikely to be a control point for amygdalin accumulation and suggests additional roles for the enzyme in almond metabolism.
Publication Type: Journal Article
Source of Publication: Functional Plant Biology, 35(3), p. 236-246
Publisher: CSIRO Publishing
Place of Publication: Melbourne, Australia
ISSN: 1445-4408
Field of Research (FOR): 070602 Horticultural Crop Improvement (Selection and Breeding)
Socio-Economic Outcome Codes: 820201 Almonds
Peer Reviewed: Yes
HERDC Category Description: C1 Refereed Article in a Scholarly Journal
Other Links: http://nla.gov.au/anbd.bib-an23372255
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