甘薯酪氨酸酶的一些理化性质

O. Ilesanmi, Omowumi Funke Adedugbe, D. A. Oyegoke
{"title":"甘薯酪氨酸酶的一些理化性质","authors":"O. Ilesanmi, Omowumi Funke Adedugbe, D. A. Oyegoke","doi":"10.5897/ajb2022.17524","DOIUrl":null,"url":null,"abstract":"Tyrosinase catalyzes formation of browning in plants, foods and vegetables. Sweet potato ( Ipomea batatas ) undergoes browning after harvesting or during post-harvest operations leading to spoilage and loss of economic value. The physico-chemical properties of purified tyrosinase from I. batatas are here described with a view to providing information on the suitability or otherwise of the enzyme for several industrial and biotechnological processes. The enzyme was purified using new approach resulting into final yield and purification fold of 76% and 7.1, respectively. The molecular weight (native) was 48.3 ± 2.5 kDa as estimated on Sephadex G-100. Highest tyrosinase activity was obtained at pH 6.5 while that of temperature was 50  C. Kinetic parameters studies resulted to 2.5 ± 1.2 mM and 451 ± 23.7 units/mg for Michaelis constant ( K m ) and maximum velocity (V max ), respectively. This led to catalytic efficiency, k cat / K m of 1.45 × 10 5 s -1 M -1 . It was concluded that, tyrosinase from I. batatas possesses remarkable properties that could be exploited for biotechnological processes.","PeriodicalId":7414,"journal":{"name":"African Journal of Biotechnology","volume":" ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2022-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":"{\"title\":\"Some physicochemical properties of tyrosinase from sweet potato (Ipomea batatas)\",\"authors\":\"O. Ilesanmi, Omowumi Funke Adedugbe, D. A. Oyegoke\",\"doi\":\"10.5897/ajb2022.17524\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Tyrosinase catalyzes formation of browning in plants, foods and vegetables. Sweet potato ( Ipomea batatas ) undergoes browning after harvesting or during post-harvest operations leading to spoilage and loss of economic value. The physico-chemical properties of purified tyrosinase from I. batatas are here described with a view to providing information on the suitability or otherwise of the enzyme for several industrial and biotechnological processes. The enzyme was purified using new approach resulting into final yield and purification fold of 76% and 7.1, respectively. The molecular weight (native) was 48.3 ± 2.5 kDa as estimated on Sephadex G-100. Highest tyrosinase activity was obtained at pH 6.5 while that of temperature was 50  C. Kinetic parameters studies resulted to 2.5 ± 1.2 mM and 451 ± 23.7 units/mg for Michaelis constant ( K m ) and maximum velocity (V max ), respectively. This led to catalytic efficiency, k cat / K m of 1.45 × 10 5 s -1 M -1 . It was concluded that, tyrosinase from I. batatas possesses remarkable properties that could be exploited for biotechnological processes.\",\"PeriodicalId\":7414,\"journal\":{\"name\":\"African Journal of Biotechnology\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2022-12-31\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"African Journal of Biotechnology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.5897/ajb2022.17524\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"African Journal of Biotechnology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.5897/ajb2022.17524","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 1

摘要

酪氨酸酶催化植物、食物和蔬菜中褐变的形成。红薯(Ipomea batatas)在收获后或收获后操作过程中发生褐变,导致腐败和经济价值损失。本文描述了来自I.batatas的纯化酪氨酸酶的物理化学性质,以期提供关于该酶对几种工业和生物技术工艺的适用性或其他方面的信息。使用新方法纯化该酶,最终产率和纯化倍数分别为76%和7.1。Sephadex G-100分子量为48.3±2.5kDa。当温度为50时,在pH 6.5时获得最高的酪氨酸酶活性 C.动力学参数研究得出米氏常数(K m)和最大速度(V max)分别为2.5±1.2 mM和451±23.7单位/mg。催化效率k cat/k m为1.45×105 s-1 m-1。结果表明,蝙蝠酪氨酸酶具有显著的性质,可用于生物技术研究。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Some physicochemical properties of tyrosinase from sweet potato (Ipomea batatas)
Tyrosinase catalyzes formation of browning in plants, foods and vegetables. Sweet potato ( Ipomea batatas ) undergoes browning after harvesting or during post-harvest operations leading to spoilage and loss of economic value. The physico-chemical properties of purified tyrosinase from I. batatas are here described with a view to providing information on the suitability or otherwise of the enzyme for several industrial and biotechnological processes. The enzyme was purified using new approach resulting into final yield and purification fold of 76% and 7.1, respectively. The molecular weight (native) was 48.3 ± 2.5 kDa as estimated on Sephadex G-100. Highest tyrosinase activity was obtained at pH 6.5 while that of temperature was 50  C. Kinetic parameters studies resulted to 2.5 ± 1.2 mM and 451 ± 23.7 units/mg for Michaelis constant ( K m ) and maximum velocity (V max ), respectively. This led to catalytic efficiency, k cat / K m of 1.45 × 10 5 s -1 M -1 . It was concluded that, tyrosinase from I. batatas possesses remarkable properties that could be exploited for biotechnological processes.
求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
African Journal of Biotechnology
African Journal of Biotechnology 工程技术-生物工程与应用微生物
自引率
0.00%
发文量
15
审稿时长
4.7 months
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信