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中国精品科技期刊2020
丁伟, 张明俐, 史吉平, 柳鹏福, 宋礼华. 表达谷氨酸脱羧酶重组枯草芽孢杆菌的构建及其发酵条件的优化[J]. 食品工业科技, 2015, (23): 194-198. DOI: 10.13386/j.issn1002-0306.2015.23.032
引用本文: 丁伟, 张明俐, 史吉平, 柳鹏福, 宋礼华. 表达谷氨酸脱羧酶重组枯草芽孢杆菌的构建及其发酵条件的优化[J]. 食品工业科技, 2015, (23): 194-198. DOI: 10.13386/j.issn1002-0306.2015.23.032
DING Wei, ZHANG Ming-li, SHI Ji-ping, LIU Peng-fu, SONG Li-hua. Construction of recombinant Bacillus subtilis expressing glutamate decarboxylase and the optimization of fermentation conditions[J]. Science and Technology of Food Industry, 2015, (23): 194-198. DOI: 10.13386/j.issn1002-0306.2015.23.032
Citation: DING Wei, ZHANG Ming-li, SHI Ji-ping, LIU Peng-fu, SONG Li-hua. Construction of recombinant Bacillus subtilis expressing glutamate decarboxylase and the optimization of fermentation conditions[J]. Science and Technology of Food Industry, 2015, (23): 194-198. DOI: 10.13386/j.issn1002-0306.2015.23.032

表达谷氨酸脱羧酶重组枯草芽孢杆菌的构建及其发酵条件的优化

Construction of recombinant Bacillus subtilis expressing glutamate decarboxylase and the optimization of fermentation conditions

  • 摘要: 谷氨酸脱羧酶(GAD)是生物合成γ-氨基丁酸(GABA)的关键酶,本研究通过基因工程构建了一株产GAD的重组枯草芽孢杆菌,并对其产GAD的发酵条件进行优化。分别通过单因素法、正交实验、极差分析和响应面法确定了最佳培养基成分(g/L)及发酵条件为:蔗糖23.5,豆粕10、乙酸铵为8.5、磷酸二氢钾4.1、七水硫酸镁0.5,p H7.0,培养温度37℃。在优化条件下GAD酶活达到0.413 U/m L,与优化前的GAD酶活0.143 U/m L相比,酶活提高了188.8%。本研究有助于后续开发枯草杆菌生产γ-氨基丁酸的工艺,以克服现在γ-氨基丁酸生产工艺中,大肠杆菌安全性的问题和乳酸菌成本过高的问题。 

     

    Abstract: Glutamate decarboxylase( GAD) is a key enzyme involved in the biosynthesis of γ- aminobutyric acid.In this study,a recombinant Bacillus subtilis expressing glutamate decarboxylase was constructed through genetic engineering,and fermentation conditions for production of GAD were optimized by single- factor test,orthogonal test and response surface methodology,and the conditions were as follows,sucrose 23.5,soybean meal 10,ammonium acetate 8.5,potassium dihydrogen phosphate( KH2PO4) 4.1,magnesium sulfate heptahydrate( Mg SO4·7H2O) 0.5,initial p H7.0 and 37℃ of culture temperature. Compared with the initial 0.143 U / m L,GAD activity was incresed by 188.8% and reached 0.413 U / m L under the optimized conditions. This study would contribute to the subsequent development of γ- aminobutyric acid production process in B.subtilis,for the sake of bypassing the safty issue related to Escherichia coli and high cost associated with Lactic acid bacteria during γ-aminobutyric acid production nowadays.

     

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