scholarly journals Selenium-catalyzed Oxidation of Alkenes with Industrial Application Potential

2019 ◽  
Author(s):  
Lei Yu
Keyword(s):  
Industrial Application ◽  
Application Potential ◽  
Catalyzed Oxidation

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
Keyword(s):  
Industrial Application ◽  
Polymer Resin ◽  
Application Potential

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

Catalysts ◽  
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.

Energy saving and environment-friendly element-transfer reactions with industrial application potential

2020 ◽  
Vol 31 (5) ◽  
pp. 1078-1082 ◽  
Author(s):  
Chao Chen ◽  
Yitao Cao ◽  
Xixi Wu ◽  
Yuanli Cai ◽  
Jian Liu ◽  
...  
Keyword(s):  
Energy Saving ◽  
Industrial Application ◽  
Transfer Reactions ◽  
Environment Friendly ◽  
Application Potential ◽  
Element Transfer

Rating of the industrial application potential of yeast strains by molecular characterization

2018 ◽  
Vol 244 (10) ◽  
pp. 1759-1772 ◽  
Author(s):  
Alexander Lauterbach ◽  
Caroline Wilde ◽  
Dave Bertrand ◽  
Jürgen Behr ◽  
Rudi F. Vogel
Keyword(s):  
Molecular Characterization ◽  
Industrial Application ◽  
Yeast Strains ◽  
Application Potential

Renilla Bioluminescence: A Morphologic Approach to the Location of Photocytes

1974 ◽  
Vol 32 ◽  
pp. 208-209
Author(s):  
Ben O. Spurlock ◽  
Milton J. Cormier
Keyword(s):  
Excited State ◽  
Ground State ◽  
Molecular Basis ◽  
Light Emission ◽  
Chemical Basis ◽  
Electronic Excited State ◽  
Colonial Form ◽  
The Common ◽  
Eighteenth And Nineteenth Centuries ◽  
Catalyzed Oxidation

The phenomenon of bioluminescence has fascinated layman and scientist alike for many centuries. During the eighteenth and nineteenth centuries a number of observations were reported on the physiology of bioluminescence in Renilla, the common sea pansy. More recently biochemists have directed their attention to the molecular basis of luminosity in this colonial form. These studies have centered primarily on defining the chemical basis for bioluminescence and its control. It is now established that bioluminescence in Renilla arises due to the luciferase-catalyzed oxidation of luciferin. This results in the creation of a product (oxyluciferin) in an electronic excited state. The transition of oxyluciferin from its excited state to the ground state leads to light emission.

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