| YANG Wenge,XUE Changhu,XU Dalun,FU Xueyan,HE Xiong. 2008. Purification and characterization of lipoxygenase from Entermorpha clathrata. Acta Oceanologica Sinica, (1):92－101 |
| Purification and characterization of lipoxygenase from Entermorpha clathrata |
| Purification and characterization of lipoxygenase from Entermorpha clathrata |
| Received:November 23, 2006 Revised:May 10, 2007 |
| DOI： |
| Key words:Entermorpha clathrata lipoxygenase purification characterization |
| 中文关键词: Entermorpha clathrata lipoxygenase purification characterization |
| 基金项目:The Technology Research and Development Program ("863" Program) of China under contract No.2003AA625030. |
| Author Name | Affiliation | E-mail | | YANG Wenge | College of Food Science and Technology, Ocean University of China, Qingdao 266003, China
Faculty of Life Science and Biotechnology, Ningbo University, Ningbo 315211, China | | | XUE Changhu | College of Food Science and Technology, Ocean University of China, Qingdao 266003, China | xuech@mail.ouc.edu.cn | | XU Dalun | Faculty of Life Science and Biotechnology, Ningbo University, Ningbo 315211, China | | | FU Xueyan | College of Food Science and Technology, Ocean University of China, Qingdao 266003, China | | | HE Xiong | Zhejiang Pharmaceutical College, Ningbo 315100, China | |
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| Abstract: |
| The purification and characterization of lipoxygenase (LOX, EC 1.13.11.12) from the green algae Enteromorpha clathrata were studied. Two components marked LOX-1 and LOX-2 were purified and their molecular masses were estimated to be 102 and 79 ku by SDS-PAGE. Both LOX-1 and LOX-2 were stable over the pH wide range 6.0~10.0 and had the optimum pH of 10.0 and 8.6, at optimum temperature of 30 and 25℃, respectively. Substrate specificities of LOX-1 and LOX-2 were the greatest towards linoleic acid, followed by arachidonic acid and linolenic acid. The Michaelis constant values of LOX-1 and LOX-2 were 0.23 and 0.20 mmol/dm3 with the substrate of linoleic acid. The LOX activities were stimulated greatly by Ca2+ but inhibited by Hg2+ and the antioxidants such as BHA, BHT and TBHQ. The hydroperoxide products of LOX were analysed by HPLC with the substrate of methyl linoleate, and the results showed that LOX-1 formed mainly 9-hydroperoxides while LOX-2 formed both 9-and 13-hydroperoxides at a ratio of 24:76. |
| 中文摘要: |
| The purification and characterization of lipoxygenase (LOX, EC 1.13.11.12) from the green algae Enteromorpha clathrata were studied. Two components marked LOX-1 and LOX-2 were purified and their molecular masses were estimated to be 102 and 79 ku by SDS-PAGE. Both LOX-1 and LOX-2 were stable over the pH wide range 6.0~10.0 and had the optimum pH of 10.0 and 8.6, at optimum temperature of 30 and 25℃, respectively. Substrate specificities of LOX-1 and LOX-2 were the greatest towards linoleic acid, followed by arachidonic acid and linolenic acid. The Michaelis constant values of LOX-1 and LOX-2 were 0.23 and 0.20 mmol/dm3 with the substrate of linoleic acid. The LOX activities were stimulated greatly by Ca2+ but inhibited by Hg2+ and the antioxidants such as BHA, BHT and TBHQ. The hydroperoxide products of LOX were analysed by HPLC with the substrate of methyl linoleate, and the results showed that LOX-1 formed mainly 9-hydroperoxides while LOX-2 formed both 9-and 13-hydroperoxides at a ratio of 24:76. |
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