{"title":"非洲油豆种子脂氧合酶的纯化及其性质——第一部分。","authors":"M N Anokwulu","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Lipoxygenase was extracted from African oil bean seed and purified by ammonium sulphate precipitation, gel filtration on Sephadex G-25 and ion-exchange chromatography on DEAE--cellulose column. The enzyme was purified 79.63 fold and 36% of the enzyme activity was recovered. The molecular weight of the enzyme was 102,000 daltons and the peroxide value was 10.56 x 10(-3) mM. The Vmax was 0.14 OD min-1 while the Km value was 1.92 x 10(-4) M. The enzyme had an optimum pH of 7.0 and optimum temperature of 30 degrees C. While diethyl-dithiocarbamate was the best inhibitor of the enzyme's oxidation of linoleic acid, nordihydroguiaretic acid was the best antioxidant for its oxidation of the fatty acid. African oil bean seed lipoxygenase had high enzyme activity of 86% when compared to soybean lipoxygenase (considered to be the best source of the enzyme). This means that African oil bean seed is a good source of lipoxygenase for biotechnology such as the bleaching of browned yam tubers.</p>","PeriodicalId":9085,"journal":{"name":"Bollettino chimico farmaceutico","volume":"142 9","pages":"410-5"},"PeriodicalIF":0.0000,"publicationDate":"2003-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Purification and some properties of African oil bean seed lipoxygenase--Part 1.\",\"authors\":\"M N Anokwulu\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Lipoxygenase was extracted from African oil bean seed and purified by ammonium sulphate precipitation, gel filtration on Sephadex G-25 and ion-exchange chromatography on DEAE--cellulose column. The enzyme was purified 79.63 fold and 36% of the enzyme activity was recovered. The molecular weight of the enzyme was 102,000 daltons and the peroxide value was 10.56 x 10(-3) mM. The Vmax was 0.14 OD min-1 while the Km value was 1.92 x 10(-4) M. The enzyme had an optimum pH of 7.0 and optimum temperature of 30 degrees C. While diethyl-dithiocarbamate was the best inhibitor of the enzyme's oxidation of linoleic acid, nordihydroguiaretic acid was the best antioxidant for its oxidation of the fatty acid. African oil bean seed lipoxygenase had high enzyme activity of 86% when compared to soybean lipoxygenase (considered to be the best source of the enzyme). This means that African oil bean seed is a good source of lipoxygenase for biotechnology such as the bleaching of browned yam tubers.</p>\",\"PeriodicalId\":9085,\"journal\":{\"name\":\"Bollettino chimico farmaceutico\",\"volume\":\"142 9\",\"pages\":\"410-5\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2003-11-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Bollettino chimico farmaceutico\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bollettino chimico farmaceutico","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
摘要
从非洲油豆种子中提取脂氧合酶,经硫酸铵沉淀、Sephadex G-25凝胶过滤、DEAE-纤维素柱离子交换层析纯化。酶被纯化79.63倍,酶活性恢复36%。酶的分子量为10.2万道尔顿,过氧化值为10.56 × 10(-3) mM, Vmax为0.14 OD min-1, Km值为1.92 × 10(-4) m。酶的最适pH为7.0,最适温度为30℃,二硫代氨基甲酸二乙酯是该酶氧化亚油酸的最佳抑制剂,去二氢脲酸是其氧化脂肪酸的最佳抗氧化剂。非洲油豆种子脂肪加氧酶的酶活性比大豆脂肪加氧酶高86%(被认为是该酶的最佳来源)。这意味着非洲油豆种子是用于生物技术(如褐色薯蓣块茎的漂白)的脂肪加氧酶的良好来源。
Purification and some properties of African oil bean seed lipoxygenase--Part 1.
Lipoxygenase was extracted from African oil bean seed and purified by ammonium sulphate precipitation, gel filtration on Sephadex G-25 and ion-exchange chromatography on DEAE--cellulose column. The enzyme was purified 79.63 fold and 36% of the enzyme activity was recovered. The molecular weight of the enzyme was 102,000 daltons and the peroxide value was 10.56 x 10(-3) mM. The Vmax was 0.14 OD min-1 while the Km value was 1.92 x 10(-4) M. The enzyme had an optimum pH of 7.0 and optimum temperature of 30 degrees C. While diethyl-dithiocarbamate was the best inhibitor of the enzyme's oxidation of linoleic acid, nordihydroguiaretic acid was the best antioxidant for its oxidation of the fatty acid. African oil bean seed lipoxygenase had high enzyme activity of 86% when compared to soybean lipoxygenase (considered to be the best source of the enzyme). This means that African oil bean seed is a good source of lipoxygenase for biotechnology such as the bleaching of browned yam tubers.