| 引用本文： |
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刘金磊,苏涛,李典鹏,卢凤来.苦瓜过氧化物酶的提取分离及性质测定[J].广西科学,2007,14(4):407-410. [点击复制]
- LIU Jin-lei,SU Tao,LI Dian-peng,LU Feng-lai.The Extraction of Peroxidase from Momordica charantia and Its Property[J].Guangxi Sciences,2007,14(4):407-410. [点击复制]
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| 摘要: |
| 从苦瓜(Momordica charantia L.)中分离和纯化过氧化物酶(POD),分别测定其最适pH值、最适温度、热稳定性、底物浓度对酶活性的影响。结果表明:苦瓜过氧化物酶以邻苯二胺为底物时λmax=425nm,Km=4.6×10-3,Vmax=0.137unit/s,最适pH值为4.6,最适温度是50℃。在温度为50℃时过氧化物酶的酶活力最大,酶活性较高。在温度为60℃以上时过氧化物酶的失活率升高,在温度为70℃以上时过氧化物酶基本失活。抗坏血酸和半胱胺酸对过氧化物酶有明显的抑制作用,其失活率分别达到94%和92%;Al3+的抑制作用稍弱,过氧化物酶的失活率为69%;EDTA的抑制效果最不明显,过氧化物酶的失活率仅为13%。 |
| 关键词: 过氧化物酶 性质 苦瓜 |
| DOI： |
| 投稿时间：2007-06-08修订日期：2007-06-27 |
| 基金项目: |
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| The Extraction of Peroxidase from Momordica charantia and Its Property |
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LIU Jin-lei1, SU Tao2, LI Dian-peng1, LU Feng-lai1
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| (1.Guangxi Institute of Botany, Guilin, Guangxi, 541006, China;2.Guilin Yibai Lijiang Pharmaceutical Co. Ltd, Guilin, Guangxi, 541006, China) |
| Abstract: |
| Peroxidase was separated and purified from Momordica charantia.Its optimum pH value, optimum temperature, thermal stability and effect of substrate concentration on enzyme activity were determined.The results were showed as follows:With O-phenylenediamine as substrate, λmax=425nm, Km=4.6×103, Vmax=0.137unit/s, optimum pH value 4.6, optimum temperature at 50℃ with high enzyme activity.The inactivation rate of POD raised over 60℃, and the enzyme activity was almost lost above 70℃.Vitamin C and Cysteine had great inhabitation effect on POD activity, the inhibition rate reached 94%and 92% respectively.Al3+ was weaker, with inhibition rate of 69%.EDTA had no significant effect of inhibition, the inhibition rate was only 13%. |
| Key words: POD property Momordica charantia |
