徐红梅,夏仕文,何从林.固定化D-氨基酸氧化酶催化DL-氨基酸去消旋化制备非天然L-氨基酸[J].分子催化,2012,(2):192-196
固定化D-氨基酸氧化酶催化DL-氨基酸去消旋化制备非天然L-氨基酸
Preparation of Non-natural L –amino Acids via Deracemization of DL-Amino Acids Catalyzed by Immobilized D-amino Acid Oxidase
投稿时间:2012-02-14  修订日期:2012-03-14
DOI:
中文关键词:  固定化D-氨基酸氧化酶,过氧化氢酶,氧化脱氨,DL-氨基酸,非天然L-氨基酸
英文关键词:Immobilized D-amino acid oxidase  Catalase  Oxidative deamination  DL-amino acids  Non-natural amino acids
基金项目:重庆市自然科学基金项目
作者单位E-mail
徐红梅 重庆邮电大学 xuhm@cqupt.edu.cn 
夏仕文* 重庆邮电大学 xiasw@cqupt.edu.cn 
何从林 重庆邮电大学 hecl@cqupt.edu.cn 
摘要点击次数: 2005
全文下载次数: 3636
中文摘要:
      在过氧化氢酶和氧气存在下,固定化D-氨基酸氧化酶(D-AAO)对映选择性催化DL-氨基酸中的D-对映体氧化脱氨为相应酮酸,L-对映体保留。研究了D-AAO的底物特异性并对反应条件进行了优化。结果表明:D-AAO具有较宽的底物谱,能够催化疏水性α-氨基酸的D-对映体氧化脱氨。在最优反应条件下,D-AAO催化DL-2-氨基丁酸、DL-2-氨基戊酸去消旋化,L-2-氨基丁酸、L-2-氨基戊酸的收率分别为48%和47%,ee分别为99.5%和99.8%。进一步地,利用Pd-C/HCOONH4催化氧化脱氨过程中产生的亚氨基酸原位还原,有效提高了L-2-氨基丁酸、L-2-氨基戊酸的收率并保持高的光学纯度。
英文摘要:
      The D-enantiomer of DL-amino acid is oxidative deaminated enantioselectively into the corresponding oxo acid by immobilized D-amino acid oxidase (D-AAO) in the presence of catalase and oxygen, and the L-enantiomer is retained. The substrate specificity of D-AAO was studied and the reaction conditions were optimized. The results showed that D-AAO has a broader substrate spectrum and is capable of catalyzing the oxidative deaminzation of hydrophobic D-α-amino acids. Under the optimal conditions, L-2-aminobutyric acid and L-2-aminovaleric acid were obtained in 48% and 47% yield , 99.5% and 99.8% ee respectively. Furthemore, the yields of L-2-aminobutyric acid and L-2-aminovaleric acid were improved and their optically purity were retained through in-situ reduction of imine acids produced during the oxidative deaminization by Pd-C/HCOONH4.
HTML  查看全文  查看/发表评论  下载PDF阅读器