Mathew Sam, Nadarajan Saravanan Prabhu, Chung Taeowan, Park Hyun Ho, Yun Hyungdon
School of Biotechnology, Yeungnam University, Gyeongsan, Gyeongbuk 712-749, South Korea.
Department Bioscience & Biotechnology, Konkuk University, Seoul 143-701, South Korea.
Enzyme Microb Technol. 2016 Jun;87-88:52-60. doi: 10.1016/j.enzmictec.2016.02.013. Epub 2016 Feb 26.
An (S)-ω-transaminase from the thermophilic eubacterium Sphaerobacter thermophilus was expressed and functionally characterized. The enzyme showed good stability at high temperature and in the presence of various substrates. Substrate specificity analysis showed that the enzyme had activity towards a broad range of substrates including amines, β- and γ-amino acids. The purified enzyme showed a specific activity of 3.3U/mg towards rac-β-phenylalanine at 37°C. The applicability of this enzyme as an attractive biocatalyst was demonstrated by synthesizing optically pure β- and γ-amino acids. Among the various beta and gamma amino acids produced via asymmetric synthesis, (S)-4-amino-4-(4-methoxyphenyl)-butanoic acid showed highest analytical yield (82%) with excellent enantiomeric excess (>99%).
对嗜热真细菌嗜热球形杆菌中的一种（S）-ω-转氨酶进行了表达及功能表征。该酶在高温及存在各种底物的情况下表现出良好的稳定性。底物特异性分析表明，该酶对包括胺类、β-和γ-氨基酸在内的多种底物具有活性。纯化后的酶在37°C下对消旋β-苯丙氨酸的比活性为3.3U/mg。通过合成光学纯的β-和γ-氨基酸证明了该酶作为一种有吸引力的生物催化剂的适用性。在通过不对称合成产生的各种β-和γ-氨基酸中，（S）-4-氨基-4-（4-甲氧基苯基）-丁酸的分析产率最高（82%），对映体过量率极佳（>99%）。
