חיפוש מתקדם
Journal of Food Biochemistry
KAHN, V., Dept. of Food Science, Agriculture Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, Israel
SCHVED, F., Dept. of Food Science, Agriculture Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, Israel
LINDNER, P., Dept. of Food Science, Agriculture Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, Israel
Maltol (3‐hydroxy‐2‐methyl‐4H‐pyran‐4‐one) inhibits the rate of oxidation of different o‐dihydroxyphenols by tyrosinase when assayed spectrophotometrically, but not when assayed polarographically. The spectral changes occurring during the oxidation of different o‐dihydroxyphenols by tyrosinase (or by sodium periodate) in the absence or presence of maltol were different, suggesting that maltol conjugates with the o‐quinones formed. Maltol does not inhibit tyrosinase activity per se but only gives an apparent inhibition probably due to its ability to conjugate with o‐quinones. Copyright © 1993, Wiley Blackwell. All rights reserved
פותח על ידי קלירמאש פתרונות בע"מ -
הספר "אוצר וולקני"
אודות
תנאי שימוש
EFFECT OF MALTOL ON THE OXIDATION OF o‐DIHYDROXYPHENOLS BY MUSHROOM TYROSINASE AND BY SODIUM PERIODATE
17
KAHN, V., Dept. of Food Science, Agriculture Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, Israel
SCHVED, F., Dept. of Food Science, Agriculture Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, Israel
LINDNER, P., Dept. of Food Science, Agriculture Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, Israel
EFFECT OF MALTOL ON THE OXIDATION OF o‐DIHYDROXYPHENOLS BY MUSHROOM TYROSINASE AND BY SODIUM PERIODATE
Maltol (3‐hydroxy‐2‐methyl‐4H‐pyran‐4‐one) inhibits the rate of oxidation of different o‐dihydroxyphenols by tyrosinase when assayed spectrophotometrically, but not when assayed polarographically. The spectral changes occurring during the oxidation of different o‐dihydroxyphenols by tyrosinase (or by sodium periodate) in the absence or presence of maltol were different, suggesting that maltol conjugates with the o‐quinones formed. Maltol does not inhibit tyrosinase activity per se but only gives an apparent inhibition probably due to its ability to conjugate with o‐quinones. Copyright © 1993, Wiley Blackwell. All rights reserved
Scientific Publication
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