Purification and stability of peroxidase of African oil palm Elaies guineensis.

Sakharov IYu, J Castillo, J C Areza, Galaev IYu
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引用次数: 61

Abstract

In the previous work, after screening tropical plants (43 species) for peroxidase activity, high activity has been detected in leaves of some palms and especially African oil palm Elaeis guineensis. This palm is widely cultivated in Colombia and presents a promising source for the industrial production of peroxidase. The initial enzyme isolation included homogenization and extraction of pigments using aqueous two phase polymer system. Initially, traditional system, formed by polyethyleneglycol/K2HPO4, was used. The replacement of K2HPO4 with (NH4)2SO4 allowed direct application of the salt phase with accumulated peroxidase on a Phenyl-Sepharose column. The final purification was carried out by liquid chromatography on Sephacryl S200 and DEAE-Toyopearl columns. The specific activity of the purified peroxidase measured toward guaiacol was 4300 units per mg of protein. The molecular weight and isoelectric point for palm peroxidase were 57.000 and 3.8, respectively. Palm peroxidase possesses uniquely high thermostability and is more stable in organic solvents than horseradish peroxidase is.

非洲油棕过氧化物酶的纯化及稳定性研究。
在以往的工作中,对热带植物(43种)进行过氧化物酶活性筛选后,在一些棕榈,特别是非洲油棕Elaeis guineensis的叶子中检测到高活性。这种棕榈在哥伦比亚广泛种植,为工业生产过氧化物酶提供了一个有前途的来源。初始酶分离包括均质化和双水相聚合物体系萃取色素。最初采用的是由聚乙二醇/K2HPO4形成的传统体系。用(NH4)2SO4代替K2HPO4,允许在苯基- sepharose色谱柱上直接应用积累过氧化物酶的盐相。采用sepphacryl S200和DEAE-Toyopearl色谱柱进行最终纯化。纯化过氧化物酶对愈创木酚的比活性为每毫克蛋白质4300单位。棕榈过氧化物酶的分子量为57.000,等电点为3.8。棕榈过氧化物酶具有独特的高热稳定性,在有机溶剂中比辣根过氧化物酶更稳定。
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