Effect of pH on the kinetics of soybean lipoxygenase‐1
The influence of pH on the kinetics of soybean lipoxygenase‐1 was examined. Lipoxygenase‐1 was stable when preincubated in the pH range from 3.2 to 9.2 but was irreversibly denatured at pH 3.0 and below. Double reciprocal plots for undenatured enzyme in the pH range 5.6 to 9.2 showed that the enzyme...
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| Format: | Article |
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Wiley Blackwell
1989
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| Online Access: | http://psasir.upm.edu.my/id/eprint/115827/ |
| _version_ | 1848866871071211520 |
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| author | Asbi, B. Ali Wei, L.S. Steinberg, M.P. |
| author_facet | Asbi, B. Ali Wei, L.S. Steinberg, M.P. |
| author_sort | Asbi, B. Ali |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | The influence of pH on the kinetics of soybean lipoxygenase‐1 was examined. Lipoxygenase‐1 was stable when preincubated in the pH range from 3.2 to 9.2 but was irreversibly denatured at pH 3.0 and below. Double reciprocal plots for undenatured enzyme in the pH range 5.6 to 9.2 showed that the enzyme obeyed Michaelis‐Menten kinetics in this pH range. The Dixon plot (log Vmax/Km vs pH) indicated an active site of the free enzyme to be a histidine residue with a pK of about 7.3. |
| first_indexed | 2025-11-15T14:27:29Z |
| format | Article |
| id | upm-115827 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-15T14:27:29Z |
| publishDate | 1989 |
| publisher | Wiley Blackwell |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-1158272025-03-13T02:44:50Z http://psasir.upm.edu.my/id/eprint/115827/ Effect of pH on the kinetics of soybean lipoxygenase‐1 Asbi, B. Ali Wei, L.S. Steinberg, M.P. The influence of pH on the kinetics of soybean lipoxygenase‐1 was examined. Lipoxygenase‐1 was stable when preincubated in the pH range from 3.2 to 9.2 but was irreversibly denatured at pH 3.0 and below. Double reciprocal plots for undenatured enzyme in the pH range 5.6 to 9.2 showed that the enzyme obeyed Michaelis‐Menten kinetics in this pH range. The Dixon plot (log Vmax/Km vs pH) indicated an active site of the free enzyme to be a histidine residue with a pK of about 7.3. Wiley Blackwell 1989 Article PeerReviewed Asbi, B. Ali and Wei, L.S. and Steinberg, M.P. (1989) Effect of pH on the kinetics of soybean lipoxygenase‐1. Journal of Food Science, 54 (6). pp. 1594-1595. ISSN 0022-1147; eISSN: 1750-3841 https://ift.onlinelibrary.wiley.com/doi/10.1111/j.1365-2621.1989.tb05167.x 10.1111/j.1365-2621.1989.tb05167.x |
| spellingShingle | Asbi, B. Ali Wei, L.S. Steinberg, M.P. Effect of pH on the kinetics of soybean lipoxygenase‐1 |
| title | Effect of pH on the kinetics of soybean lipoxygenase‐1 |
| title_full | Effect of pH on the kinetics of soybean lipoxygenase‐1 |
| title_fullStr | Effect of pH on the kinetics of soybean lipoxygenase‐1 |
| title_full_unstemmed | Effect of pH on the kinetics of soybean lipoxygenase‐1 |
| title_short | Effect of pH on the kinetics of soybean lipoxygenase‐1 |
| title_sort | effect of ph on the kinetics of soybean lipoxygenase‐1 |
| url | http://psasir.upm.edu.my/id/eprint/115827/ http://psasir.upm.edu.my/id/eprint/115827/ http://psasir.upm.edu.my/id/eprint/115827/ |