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中国精品科技期刊2020
重组藻红蓝蛋白α亚基的稳定性研究[J]. 华体会体育, 2013, (10): 116-119. DOI: 10.13386/j.issn1002-0306.2013.10.037
引用本文: 重组藻红蓝蛋白α亚基的稳定性研究[J]. 华体会体育, 2013, (10): 116-119. DOI: 10.13386/j.issn1002-0306.2013.10.037
Study on the stability ofαsubunit of phycoerythrocyanin[J]. Science and Technology of Food Industry, 2013, (10): 116-119. DOI: 10.13386/j.issn1002-0306.2013.10.037
Citation: Study on the stability ofαsubunit of phycoerythrocyanin[J]. Science and Technology of Food Industry, 2013, (10): 116-119. DOI: 10.13386/j.issn1002-0306.2013.10.037

重组藻红蓝蛋白α亚基的稳定性研究

Study on the stability ofαsubunit of phycoerythrocyanin

  • 摘要: 采用基因重组的方法从大肠杆菌体内获得藻红蓝蛋白a亚基,该蛋白是具有天然活性的红色荧光蛋白。从温度、pH、光照、离子浓度等方面考察该色素蛋白的稳定性影响,同时考察了一些金属离子和小分子对其荧光紫外光谱影响。研究表明,温度低于37℃能较好的保存蛋白;pH在4~9之间蛋白较稳定存在;紫外照射能破坏蛋白结构、避光可以保持蛋白稳定;离子强度对蛋白没有多大影响;碳水化合物影响较小;而多数金属离子对蛋白荧光有猝灭作用等。这些研究都为藻红蓝蛋白作为食品化妆品天然色素的应用研究打下基础。 

     

    Abstract: Theαsubunit of phycoerythrocyanin (α-PEC) extacted from E.coli by using gene recombination technique was a kind of natural red fluorescence protein.The temperature, pH, light, and ion concentration which affected the stability of the protein were studied.Meanwhile, some metal ions and small molecules which impacted the fluorescence or UV spectrum were investigated.That proved that the temperature below 37℃ and pH between 4 and 9 could save protein better.UV radiation could destroy the structure of protein while the dark could maintain it.Ionic strength and carbohydrates had little effect on the protein, however, the majority of metal ions affected the fluorescence quenching of the protein.The work was helpful for the application of the protein used as food and cosmetics natural pigments.

     

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