Recombinant Porcine 12-<i>Lipoxygenase Catalytic Domain</i>: Effect of Inhibitors, Selectivity of Substrates and Specificity of Oxidation Products of Linoleic Acid
<i>Lipoxygenase (LOX)</i> is a major endogenous enzyme for the enzymatic oxidation of lipids during meat storage and meat product manufacturing. In the present work, some characteristics, i.e., effects of inhibitors, selectivity of substrates and specificity of oxidation products, were s...
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MDPI AG
2022-03-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/11/7/980 |
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| author | Jiamei Xu Yu Liu Jingjing Ma Pengpeng Li Zhiming Geng Daoying Wang Muhan Zhang Weimin Xu |
| author_facet | Jiamei Xu Yu Liu Jingjing Ma Pengpeng Li Zhiming Geng Daoying Wang Muhan Zhang Weimin Xu |
| author_sort | Jiamei Xu |
| collection | DOAJ |
| description | <i>Lipoxygenase (LOX)</i> is a major endogenous enzyme for the enzymatic oxidation of lipids during meat storage and meat product manufacturing. In the present work, some characteristics, i.e., effects of inhibitors, selectivity of substrates and specificity of oxidation products, were studied using recombinant porcine 12-<i>lipoxygenase catalytic domain</i> (12-LOXcd). Several familiar inhibitors were found inhibit the activity of recombinant porcine 12-LOXcd;nordihydroguaiaretic acid demonstrated the strongest inhibitory effect. The enzyme could oxygenate common polyunsaturated fatty acids, and showed the highest affinity to linoleic acid (LA), followed by arachidonic acid (AA), linolenic acid (LN) and docosahexaenoic acid (DHA). Under the action of porcine 12-LOXcd, LA was oxidized into four hydroxyoctadecadienoic acid (HODE) isomers, i.e., 13-<i>Z,E</i>-HODE, 13-<i>E,E</i>-HODE, 9-<i>Z,E</i>-HODE and 9-<i>E,E</i>-HODE. Variation of pH not only affected the yield of LA oxidation products, but also the distribution of HODE isomers. These results indicated that endogenous LOX activity and LOX-catalyzed lipid oxidation can be regulated during meat storage and meat product manufacturing. |
| first_indexed | 2024-03-09T11:50:23Z |
| format | Article |
| id | doaj.art-5a0ea9fdc32348de8b3f3e4e94c99897 |
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| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-09T11:50:23Z |
| publishDate | 2022-03-01 |
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| record_format | Article |
| series | Foods |
| spelling | doaj.art-5a0ea9fdc32348de8b3f3e4e94c998972023-11-30T23:15:20ZengMDPI AGFoods2304-81582022-03-0111798010.3390/foods11070980Recombinant Porcine 12-<i>Lipoxygenase Catalytic Domain</i>: Effect of Inhibitors, Selectivity of Substrates and Specificity of Oxidation Products of Linoleic AcidJiamei Xu0Yu Liu1Jingjing Ma2Pengpeng Li3Zhiming Geng4Daoying Wang5Muhan Zhang6Weimin Xu7School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, ChinaInstitute of Agro-Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, ChinaInstitute of Agro-Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, ChinaInstitute of Agro-Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, ChinaInstitute of Agro-Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, ChinaInstitute of Agro-Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China<i>Lipoxygenase (LOX)</i> is a major endogenous enzyme for the enzymatic oxidation of lipids during meat storage and meat product manufacturing. In the present work, some characteristics, i.e., effects of inhibitors, selectivity of substrates and specificity of oxidation products, were studied using recombinant porcine 12-<i>lipoxygenase catalytic domain</i> (12-LOXcd). Several familiar inhibitors were found inhibit the activity of recombinant porcine 12-LOXcd;nordihydroguaiaretic acid demonstrated the strongest inhibitory effect. The enzyme could oxygenate common polyunsaturated fatty acids, and showed the highest affinity to linoleic acid (LA), followed by arachidonic acid (AA), linolenic acid (LN) and docosahexaenoic acid (DHA). Under the action of porcine 12-LOXcd, LA was oxidized into four hydroxyoctadecadienoic acid (HODE) isomers, i.e., 13-<i>Z,E</i>-HODE, 13-<i>E,E</i>-HODE, 9-<i>Z,E</i>-HODE and 9-<i>E,E</i>-HODE. Variation of pH not only affected the yield of LA oxidation products, but also the distribution of HODE isomers. These results indicated that endogenous LOX activity and LOX-catalyzed lipid oxidation can be regulated during meat storage and meat product manufacturing.https://www.mdpi.com/2304-8158/11/7/980<i>Lipoxygenase</i>inhibitorssubstratesoxidation productslinoleic acidporcine |
| spellingShingle | Jiamei Xu Yu Liu Jingjing Ma Pengpeng Li Zhiming Geng Daoying Wang Muhan Zhang Weimin Xu Recombinant Porcine 12-<i>Lipoxygenase Catalytic Domain</i>: Effect of Inhibitors, Selectivity of Substrates and Specificity of Oxidation Products of Linoleic Acid Foods <i>Lipoxygenase</i> inhibitors substrates oxidation products linoleic acid porcine |
| title | Recombinant Porcine 12-<i>Lipoxygenase Catalytic Domain</i>: Effect of Inhibitors, Selectivity of Substrates and Specificity of Oxidation Products of Linoleic Acid |
| title_full | Recombinant Porcine 12-<i>Lipoxygenase Catalytic Domain</i>: Effect of Inhibitors, Selectivity of Substrates and Specificity of Oxidation Products of Linoleic Acid |
| title_fullStr | Recombinant Porcine 12-<i>Lipoxygenase Catalytic Domain</i>: Effect of Inhibitors, Selectivity of Substrates and Specificity of Oxidation Products of Linoleic Acid |
| title_full_unstemmed | Recombinant Porcine 12-<i>Lipoxygenase Catalytic Domain</i>: Effect of Inhibitors, Selectivity of Substrates and Specificity of Oxidation Products of Linoleic Acid |
| title_short | Recombinant Porcine 12-<i>Lipoxygenase Catalytic Domain</i>: Effect of Inhibitors, Selectivity of Substrates and Specificity of Oxidation Products of Linoleic Acid |
| title_sort | recombinant porcine 12 i lipoxygenase catalytic domain i effect of inhibitors selectivity of substrates and specificity of oxidation products of linoleic acid |
| topic | <i>Lipoxygenase</i> inhibitors substrates oxidation products linoleic acid porcine |
| url | https://www.mdpi.com/2304-8158/11/7/980 |
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