Advances in the Enzymatic Reduction of Ketones

2007 ◽  
Vol 40 (12) ◽  
pp. 1412-1419 ◽  
Author(s):  
Jeffrey C. Moore ◽  
David J. Pollard ◽  
Birgit Kosjek ◽  
Paul N. Devine
2007 ◽  
Vol 9 (11) ◽  
pp. 2163-2166 ◽  
Author(s):  
Gonzalo de Gonzalo ◽  
Iván Lavandera ◽  
Kurt Faber ◽  
Wolfgang Kroutil

ChemInform ◽  
2008 ◽  
Vol 39 (17) ◽  
Author(s):  
Jeffrey C. Moore ◽  
David J. Pollard ◽  
Birgit Kosjek ◽  
Paul N. Devine

2017 ◽  
Vol 68 (9) ◽  
pp. 2196-2203 ◽  
Author(s):  
Mara Crisan ◽  
Gheorghe Maria

Novel coupled enzymatic systems reported important applications in the industrial bio-catalysis. Multi-enzymatic reactions can successfully replace complex chemical syntheses, using milder reaction conditions, and generating less waste. For such systems acting simultaneously, the model-based engineering calculations (design, reactor operation optimization) are difficult tasks, because they must account for interacting reactions, differences in enzymes optimal activity domains and deactivation kinetics. The determination of the optimal operating mode (enzyme ratios, enzyme feeding policy, temperature, pH) often turns into a difficult multi-objective optimization problem with multiple constraints to be solved for every particular system. The paper focuses on applying a modular screening procedure that can identify the optimal operating policy of an enzymatic reactor, which minimizes the enzyme consumption, given the process kinetic model, and an imposed production capacity. Following an optimization procedure, the process effectiveness is evaluated in a systematic approach, by including simple batch reactor (BR), batch with intermittent addition of the key-enzyme following certain optimal policies (BRP). Exemplification is made for the case of the enzymatic reduction of D-fructose to mannitol by using suspended MDH (mannitol dehydrogenase) and NADH (Nicotinamide adenine dinucleotide) cofactor, with the in-situ continuous regeneration of the cofactor by the expense of formate degradation in the presence of suspended FDH (Formate dehydrogenase).


2008 ◽  
Vol 5 (7) ◽  
pp. 591-593 ◽  
Author(s):  
Ling-Zhen Chen ◽  
Jia-Jian Peng ◽  
Jia-Yun Li ◽  
Ying Bai ◽  
Ying-Qian Hu ◽  
...  

Author(s):  
Rashmi Kumari ◽  
Vasumathy R ◽  
Dhanya Sunil ◽  
Raghumani Singh Ningthoujam ◽  
Badri Narain Pandey ◽  
...  

AbstractThe bioreductive enzymes typically upregulated in hypoxic tumor cells can be targeted for developing diagnostic and drug delivery applications. In this study, a new fluorescent probe 4−(6−nitro−1,3−dioxo−1H−benzo[de]isoquinolin−2(3H)−yl)benzaldehyde (NIB) based on a nitronaphthalimide skeleton that could respond to nitroreductase (NTR) overexpressed in hypoxic tumors is designed and its application in imaging tumor hypoxia is demonstrated. The docking studies revealed favourable interactions of NIB with the binding pocket of NTR-Escherichia coli. NIB, which is synthesized through a simple and single step imidation of 4−nitro−1,8−naphthalic anhydride displayed excellent reducible capacity under hypoxic conditions as evidenced from cyclic voltammetry investigations. The fluorescence measurements confirmed the formation of identical products (NIB-red) during chemical as well as NTR−aided enzymatic reduction in the presence of NADH. The potential fluorescence imaging of hypoxia based on NTR-mediated reduction of NIB is confirmed using in-vitro cell culture experiments using human breast cancer (MCF−7) cells, which displayed a significant change in the fluorescence colour and intensity at low NIB concentration within a short incubation period in hypoxic conditions. Graphical abstract


1940 ◽  
Vol 136 (3) ◽  
pp. 747-774 ◽  
Author(s):  
Erwin Haas ◽  
B.L. Horecker ◽  
T.R. Hogness

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