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Monoamine oxidase is a kind of biocatalyst with great potential for application, which can selectively oxidize adesomeofable amine-producing subamine under environmentally friendly conditions.
if a non-selective reducing agent is added to the reaction system, it is possible to catalyze the amine's decyclone to synthesize asingle-frame amines.
, the biocatalytic and green chemical research team led by Zhu Dunming, a researcher at the Tianjin Institute of Industrial Biotechnology of the Chinese Academy of Sciences, and the biocatalyst discovery and transformation research team led by Wu Qiqing, a researcher at Tianjin Institute of Engineering, explored the three-dimensional selective control mechanism of the enzyme and tapped its application potential on the basis of the previous work. The monoamine oxidase (MAO-N) derived from Brevium oxydans IHbacteri-35A is an enzyme engineering modification.
1, through the screening and iterative mutation of CHAO mutant library, obtained a 30 times increased vitality of phenolineeyl, and developed a new way to synthesize D-proline by ethyl proline.
research published online in ChemCatChem.
2, through the monoamine oxidase MAO-N substrate combination pocket and substrate / product entry and exit channel at the same time, to achieve the goal of improving monoamine oxidase activity and regulation of stereoscopic selectivity, for the transformation of other enzymes to provide reference.
research published online in Chemical Science.
3, in order to reveal the key sites affecting CHAO catalytic activity and stereo selectivity, the amino acid residues in the range of 6 s from the active center are selected as the mutation sites, and the diversity of mutant stoctors is constructed.
the constructed mutant bank and 2-replace the tetrahydroquina base bank for multiplication screening, and found that A molecular structure region of CHAO for the oxidation 2-replace sihydroquine activity and stereoscopic selectivity plays an important role.
research published online in ACS Catalysis.
this series of research work has been funded by the National Natural Science Foundation of China, the Chinese Academy of Sciences Youth Promotion Association and the Tianjin Foreign Special thousands of people project.
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