Design and Preparation of Polymer Resin-Supported Proline Catalyst with Industrial Application Potential

2016 ◽  
Vol 1 (9) ◽  
pp. 1933-1937 ◽  
Author(s):  
Mr. Lin Xu ◽  
Mr. Jiejun Huang ◽  
Ming Zhang ◽  
Lei Yu ◽  
Yining Fan
Catalysts ◽  
2020 ◽  
Vol 10 (11) ◽  
pp. 1308
Author(s):  
Lixin Zhai ◽  
Zihao Xie ◽  
Qiaopeng Tian ◽  
Zhengbing Guan ◽  
Yujie Cai ◽  
...  

Aminotransferases are employed as industrial biocatalysts to produce chiral amines with high enantioselectivity and yield. BpTA-1 and BpTA-2 are the only two pyridoxal 5′-phosphate-dependent fold type IV transaminase enzymes in Bacillus altitudinis W3. Herein, we compared the structures and biochemical characteristics of BpTA-1 and BpTA-2 using bioinformatic analysis, circular dichroism spectroscopy, atomic force microscopy and other approaches. BpTA-1 and BpTA-2 are similar overall; both form homodimers and utilize a catalytic lysine. However, there are distinct differences in the substrate cofactor-binding pocket, molecular weight and the proportion of the secondary structure. Both enzymes have the same stereoselectivity but different enzymatic properties. BpTA-2 is more active under partial alkaline and ambient temperature conditions and BpTA-1 is more sensitive to pH and temperature. BpTA-2 as novel enzyme not only fills the building blocks of transaminase but also has broader industrial application potential for (R)-α-phenethylamines than BpTA-1. Structure-function relationships were explored to assess similarities and differences. The findings lay the foundation for modifying these enzymes via protein engineering to enhance their industrial application potential.


2020 ◽  
Vol 31 (5) ◽  
pp. 1078-1082 ◽  
Author(s):  
Chao Chen ◽  
Yitao Cao ◽  
Xixi Wu ◽  
Yuanli Cai ◽  
Jian Liu ◽  
...  

2018 ◽  
Vol 244 (10) ◽  
pp. 1759-1772 ◽  
Author(s):  
Alexander Lauterbach ◽  
Caroline Wilde ◽  
Dave Bertrand ◽  
Jürgen Behr ◽  
Rudi F. Vogel

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