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Metabolic detoxification of capsaicin by UDP‐glycosyltransferase in three Helicoverpa species
Author(s) -
Ahn SeungJoon,
BadenesPérez Francisco R.,
Reichelt Michael,
Svatoš Aleš,
Schneider Bernd,
Gershenzon Jonathan,
Heckel David G.
Publication year - 2011
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.20444
Subject(s) - capsaicin , helicoverpa armigera , generalist and specialist species , biology , midgut , enzyme , biochemistry , malpighian tubule system , helicoverpa zea , helicoverpa , larva , botany , ecology , receptor , habitat , noctuidae
Capsaicin β ‐glucoside was isolated from the feces of Helicoverpa armigera , Helicoverpa assulta , and Helicoverpa zea that fed on capsaicin‐supplemented artificial diet. The chemical structure was identified by NMR spectroscopic analysis as well as by enzymatic hydrolysis. The excretion rates of the glucoside were different among the three species; those in the two generalists, H. armigera and H. zea , were higher than in a specialist, H. assulta . UDP‐glycosyltransferases (UGT) enzyme activities measured from the whole larval homogenate of the three species with capsaicin and UDP‐glucose as substrates were also higher in the two generalists. Compared among five different larval tissues (labial glands, testes from male larvae, midgut, the Malpighian tubules (MT), and fat body) from the three species, the formation of the capsaicin glucoside by one or more UGT is high in the fat body of all the three species as expected, as well as in H. assulta MT. Optimization of the enzyme assay method is also described in detail. Although the lower excretion rate of the unaltered capsaicin in H. assulta indicates higher metabolic capacity toward capsacin than in the other two generalists, the glucosylation per se seems to be insufficient to explain the decrease in capsaicin in the specialist, suggesting that H. assulta might have another important mechanism to deal with capsaicin more specifically. © 2011 Wiley Periodicals, Inc.