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Effect of acetohydroxamic acid (AHA) and salicylhydroxamic acid (SHAM) on the oxidation of o-dihydroxy- and trihydroxyphenols by mushroom tyrosinase
Year:
1999
Source of publication :
Journal of Food Biochemistry
Authors :
Kahn, Varda
;
.
Volume :
23
Co-Authors:
Kahn, V., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, Israel
Facilitators :
From page:
409
To page:
433
(
Total pages:
25
)
Abstract:
Acetohydroxamic acid (AHA) and salicylhydroxamic acid (SHAM) each inhibited the rate of oxidation of different o-dihydroxy- and trihydroxyphenols by tyrosinase when assayed spectrophotometrically or polarographically. SHAM was a much more effective inhibitor than AHA. Spectral changes occurring during the oxidation of different o-dihydroxyphenols by tyrosinase in the presence of AHA or SHAM were different than the spectral changes occurring in their absence. AHA and SHAM also had an effect on the spectrum of the final product(s) formed when different o-dihydroxyphenols were oxidized by the enzyme, suggesting that AHA and SHAM conjugate with the o-quinones formed. A lack of an effect of AHA and SHAM on the spectrum of product(s) formed when trihydroxyphenols were oxidized by tyrosinase suggest that AHA and SHAM do not conjugate with the o-quinones derived from trihydroxyphenols.
Note:
Related Files :
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DOI :
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
20123
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:34
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Scientific Publication
Effect of acetohydroxamic acid (AHA) and salicylhydroxamic acid (SHAM) on the oxidation of o-dihydroxy- and trihydroxyphenols by mushroom tyrosinase
23
Kahn, V., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, Israel
Effect of acetohydroxamic acid (AHA) and salicylhydroxamic acid (SHAM) on the oxidation of o-dihydroxy- and trihydroxyphenols by mushroom tyrosinase
Acetohydroxamic acid (AHA) and salicylhydroxamic acid (SHAM) each inhibited the rate of oxidation of different o-dihydroxy- and trihydroxyphenols by tyrosinase when assayed spectrophotometrically or polarographically. SHAM was a much more effective inhibitor than AHA. Spectral changes occurring during the oxidation of different o-dihydroxyphenols by tyrosinase in the presence of AHA or SHAM were different than the spectral changes occurring in their absence. AHA and SHAM also had an effect on the spectrum of the final product(s) formed when different o-dihydroxyphenols were oxidized by the enzyme, suggesting that AHA and SHAM conjugate with the o-quinones formed. A lack of an effect of AHA and SHAM on the spectrum of product(s) formed when trihydroxyphenols were oxidized by tyrosinase suggest that AHA and SHAM do not conjugate with the o-quinones derived from trihydroxyphenols.
Scientific Publication
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