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首页> 外文期刊>British Biotechnology Journal >Proteomic Quantitative UV Absorption SpectrumAnalysis of Effect of Heat Stress on Protein Extractfrom Cowpea Seed (Vigna unguiculata (L) Walp)
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Proteomic Quantitative UV Absorption SpectrumAnalysis of Effect of Heat Stress on Protein Extractfrom Cowpea Seed (Vigna unguiculata (L) Walp)

机译：蛋白质组学定量紫外吸收光谱分析热胁迫对Cow豆种子蛋白提取的影响

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Aim: Proteomic quantitative UV absorption spectrum analysis was used to study the effect of heat stress on protein extract from cowpea seeds (Vigna unguiculata (L) Walp). Study Design: Protein extracts were obtained from 9 cowpea accessions obtained from GeneBank of International Institute of Tropical Agriculture in January 2014. Each protein extract was divided into four batches out of which three batches were subjected to different temperature treatments and incubation at 37°C, 60°C and 100°C for 1 hour and the remaining one batch served as control. Protein content in each control protein extract and 37°C, 60°C and 100°C treated protein extracts from each of the 9 cowpea samples were determined at 280 nm using bovine serum albumin standard curve. Place and Duration of Study: Biochemistry Unit, Department of Chemical Sciences, Afe Babalola University Ado Ekiti, Nigeria between January 2014 and June 2014.Methodology: A200-A960 UV wavelengths absorption spectrum analysis was carried out on control protein extract and 37°C, 60°C and 100°C treated protein extracts respectively from each of the 9 cowpea samples. In order to establish the relationship between protein extracts (control) and protein extracts heat treated (37°C, 60°C, and 100°C), cluster analysis of optical density (OD) data was carried out using numerical taxonomy and multivariate analysis system. Results: The protein content (control) in Vigna unguiculata (L) Walp was between 8.4 and 10.8 mg/ml (10.5-13.5%) in seed, while protein content (heat treated) in Vigna unguiculata (L) Walp was between 8.9 and 9.5 mg/ml (11.2-11.9%), 8.7-9.5 mg/ml (10.9-11.9%), 9.0 and 11.8 mg/ml (11.3-14.7 %) in heat treatments of 37°C, 60°C, and 100°C respectively. The protein UV absorption spectra of control protein extract and 37°C, 60°C and 100°C treated protein extracts from each cowpea accession were generally different due to differential UV wavelength protein absorption. Cluster analysis of absorbance spectra optical density values revealed five clusters (cluster 1, cluster 2, cluster 3, cluster 4, and cluster 5) among control protein extracts and protein extracts heated at 37°C, 60°C, and 100°C. Cluster1 was made up of protein extracts heated at 37°C and 60°C, while cluster2 and cluster3 constituted closely related protein extracts heated at 37°C and 100°C respectively. Cluster4 was typical of control protein extracts, while cluster5 was made up of distinct protein extracts heated at 100°C. Conclusion: Heating protein extracts at 37°C, 60°C, and 100oC has altered proteomic diversity in different cowpea accessions and this could make protein extraction more difficult with implications on protein properties.
机译：目的：使用蛋白质组学定量紫外吸收光谱分析技术研究热胁迫对cow豆种子（Vigna unguiculata（L）Walp）蛋白质提取物的影响。研究设计：蛋白质提取物是从2014年1月从国际热带农业研究所GeneBank获得的9个cow豆种质中获得的。每种蛋白质提取物分为四批，其中三批经过不同的温度处理并在37°C孵育。在60°C和100°C的温度下放置1小时，其余的一批用作对照。使用牛血清白蛋白标准曲线在280 nm下测定9种cow豆样品中每种对照蛋白提取物以及37°C，60°C和100°C处理的蛋白提取物中的蛋白含量。研究的地点和持续时间：2014年1月至2014年6月，尼日利亚阿菲巴巴拉拉大学化学系生物化学系，研究方法：在对照蛋白提取物和37°C下进行A200-A960紫外波长吸收光谱分析，从9个cow豆样品中分别提取60°C和100°C处理的蛋白质。为了建立蛋白质提取物（对照）和热处理（37°C，60°C和100°C）的蛋白质提取物之间的关系，使用数值分类法和多元分析对光密度（OD）数据进行了聚类分析。系统。结果：Vi豆（Vigna unguiculata（L）Walp）的蛋白质含量（对照）在8.4至10.8 mg / ml（10.5-13.5 ％）之间，而gna豆（Vigna unguiculata（L）Walp）的蛋白质含量（热处理）在8.9之间。在37°C，60°C的热处理中分别为9.5 mg / ml（11.2-11.9 ％），8.7-9.5 mg / ml（10.9-11.9 ％），9.0和11.8 mg / ml（11.3-14.7 ％） C和100°C。对照蛋白提取物与每种cow豆品种的37°C，60°C和100°C处理的蛋白提取物的蛋白UV吸收光谱通常因紫外波长蛋白吸收不同而不同。吸光度光谱光密度值的聚类分析表明，在对照蛋白提取物和加热到37°C，60°C和100°C的蛋白提取物中，有五个簇（簇1，簇2，簇3，簇4和簇5）。 Cluster1由加热至37°C和60°C的蛋白质提取物组成，而cluster2和cluster3分别构成了紧密相关的加热至37°C和100°C的蛋白质提取物。 Cluster4是典型的对照蛋白质提取物，而cluster5由加热至100°C的不同蛋白质提取物组成。结论：在37°C，60°C和100oC加热蛋白质提取物会改变不同cow豆种质的蛋白质组学多样性，这可能会使蛋白质提取更加困难，从而影响蛋白质的特性。

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