Abstract
The gill and skin tissues from several fish species contain active lipoxygenase, which is capable of oxidizing polyunsaturated fatty acids into hydroperoxides. Gill lipoxygenase of rainbow trout exhibited similar reactivities toward arachidonic, eicosapentaenoic, and docosahexaenoic acids, but low reactivity toward linoleic acid. The lipoxygenase exhibited activity from pH 7 to 9 with optimum pH at 7.5. The enzyme was rapidly inactivated at temperatures above 40°C. Stability of gill lipoxygenase was enhanced in the presence of glutathione. Inactivation of lipoxygenase by sulfhydryl-specific reagents suggested that thiol groups were involved in its activity.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 680-685 |
| Number of pages | 6 |
| Journal | Journal of Agricultural and Food Chemistry |
| Volume | 36 |
| Issue number | 4 |
| State | Published - 1988 |
| Externally published | Yes |
ASJC Scopus subject areas
- Agricultural and Biological Sciences (miscellaneous)
- Food Science
- Chemistry (miscellaneous)