Selenium-contained Materials with Industrial Application Potential

Selenium-catalyzed Oxidation of Alkenes with Industrial Application Potential

Proceedings of The 7th IIAE International Conference on Industrial Application Engineering 2019 ◽

10.12792/iciae2019.049 ◽

2019 ◽

Author(s):

Lei Yu

Keyword(s):

Industrial Application ◽

Application Potential ◽

Catalyzed Oxidation

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Industrial Application Potential of Virtual Reality An Empirical Study of Demands, Barriers, and Drivers

Eurographics - Virtual Environments ’98 ◽

10.1007/978-3-7091-7519-4_31 ◽

1998 ◽

pp. 288-301

Author(s):

Thomas Lechler ◽

Alexandre Saad

Keyword(s):

Virtual Reality ◽

Empirical Study ◽

Industrial Application ◽

Application Potential

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

ChemistrySelect ◽

10.1002/slct.201600404 ◽

2016 ◽

Vol 1 (9) ◽

pp. 1933-1937 ◽

Cited By ~ 5

Author(s):

Mr. Lin Xu ◽

Mr. Jiejun Huang ◽

Ming Zhang ◽

Lei Yu ◽

Yining Fan

Keyword(s):

Industrial Application ◽

Polymer Resin ◽

Application Potential

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Structural and Functional Analysis of the Only Two Pyridoxal 5′-Phosphate-Dependent Fold Type IV Transaminases in Bacillus altitudinis W3

Catalysts ◽

10.3390/catal10111308 ◽

2020 ◽

Vol 10 (11) ◽

pp. 1308

Author(s):

Lixin Zhai ◽

Zihao Xie ◽

Qiaopeng Tian ◽

Zhengbing Guan ◽

Yujie Cai ◽

...

Keyword(s):

Industrial Application ◽

Building Blocks ◽

Bioinformatic Analysis ◽

Binding Pocket ◽

Bacillus Altitudinis ◽

Force Microscopy ◽

Cofactor Binding ◽

Type Iv ◽

Fold Type ◽

Application Potential

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.

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