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中国生物工程杂志

CHINA BIOTECHNOLOGY
中国生物工程杂志  2007, Vol. 27 Issue (10): 34-38    
研究简报     
L-茶氨酸新型酶法制备及其催化工艺优化
李加友 郭丽芸 焦庆才
嘉兴学院生物与化学工程学院 南京大学医药生物技术国家重点实验室 南京大学医药生物技术国家重点实验室
A Novel Biocatalyst and its optimized process for Preparing L-theanine
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摘要:

L-茶氨酸是茶叶中游离氨基酸的主要组成部分,关于其良好的生理活性已有广泛报道。首次报道了来源于Cunnighamella echinulata 9980的L-氨基酰化酶用于高光学纯度的L-茶氨酸的酶法制备。该酶在pH 6.5,底物N-乙酰-DL-茶氨酸浓度为50 mM,且有40 mM CoCl2时催化效果较好。结果表明,在上述条件下,50℃作用12 h得L-茶氨酸22.5 mM,转化率90%。

关键词: L-茶氨酸N-乙酰-DL-茶氨酸CunnighamellaechinulataL-氨基酰化酶光学拆分    
Abstract:

L-theanine ( γ-glutamylethylamide ) is the main free amino acid component of tea and its favorable physiological effects on mammals have been reported. An enzymatic method for optically pure L-theanine production with a new L-aminoacylases-production fungi Cunnighamella echinulata 9980 was developed. The optimum conditions for enzymatic catalysis were at pH 6.5 with 50 mM N-Acyl-DL-theanine and 40 mM CoCl2. After 12-h incubation at 50℃, 22.5 mM L-theanine was obtained, the conversion rate against N-Acyl-L-theanine being 90%. This is the first report that Cunnighamella echinulata and the aminoacylase were applied in preparation of L-theanine.

Key words: L-theanine    N-Acyl-DL-Theanine    Cunnighamella echinulata    L-aminoacylase    optical resolution
收稿日期: 2007-07-17 出版日期: 2007-10-25
通讯作者: 李加友   
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引用本文:

李加友,郭丽芸,焦庆才. L-茶氨酸新型酶法制备及其催化工艺优化[J]. 中国生物工程杂志, 2007, 27(10): 34-38.

. A Novel Biocatalyst and its optimized process for Preparing L-theanine. China Biotechnology, 2007, 27(10): 34-38.

链接本文:

https://manu60.magtech.com.cn/biotech/CN/        https://manu60.magtech.com.cn/biotech/CN/Y2007/V27/I10/34

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