Hi Mohammed
I work for the last almost 25 years in the biocatalysis of a big chemical company...I would take the words of Obama " Yes, we can!" The exeptance is much better today, you have a lot of bioprocessing and a lot of bioconversions that work far better than traditional synthesis, solvent free, low temperature and low pressure settings that you can switch to almost any location worldwide. It is also not just a special favour that this big companies give to this technique; their likes base on hard economical facts, so you can be sure that if there is a preference for bioctalysis method, it needs to be better. New echnics like the construction of catalytical enzyme "antibodies" or the usage of new, non-natural amino acids to create new proteins offer you a far wider range in the future
I can give you an example from a field on which I worked for 10 years: the kinetic racemic separation of chiral molecules. There is no direct synthetic acess, because besides of a few very complex asymetric hydrogenisations, that have no practical value for comercial production, everything is done by cristallization. There are companies that offer the classical Pasteur's tartaric acid cristallisation in big industrial scale.
First, you need to do big material efforts to realize and recycle the chemicals. this can be ecomomically and logistically difficult... and second:
you are fixed on the cristall eutectic point of your mixture....this parameter fixes the lowest energy level to a specific concentration, what means that you cannot purify your product over this value, even if you cristallize until the end of days.
Mostly you try to use other cristallisation helpers with high chiral purity, but as your organic synthesis reaction always ends in racemic molecules, you need to get this from a "natural" ,means biochemical ,way
So you get in trouble if this value is f.E. ee=97,0% and your customer asks you for a high pure prodct, ee>99,5%. This is not obtainable with a "classic" method.
Nevertheless your kinetic racemic separation gives you the chance, even if the Quality of the reaction is not perfect, to purify up too the given purity.
In case of your desired enantiomer does not react with the enzyme, the wrong one diseapears in a higer number than 1:1 from the reaction you will always get almost 100% chiral purity. you can predict this, as soon as you see any kind of ciral activity between enzyme and substrate.
Other, fermenation based reactions can work with extremly cheap incredients or extremely high conversion rates
kind regars
I completely agree with you i asked this question because yesterday during giving a presentation a bout the biocatalysis as a new way to the future on of the audience (prof) told me that you can't compete with the chemical methods
Regards
I and my coworkers have been working in the field of enzymes as biocatalysts, and enzyme technology for more than 40 years. I, Klaus Buchholz and Uwe T. Bornscheuer last summarized its development until ≈2010 in Chapter I in our Book "Biocatalysts and Enzyme technology" in 2012. The best answer to your question is given in figure 1.5 (attached) in this chapter. Enzymes as catalysts now are about 30 % of the total catalyst market. The enzyme sales increased from 2 to 4 109 € from 2000 to 2010. The total market is larger, as many companies that use enymes as biocatalysts to produce desired products, produce them in their company. Both the enzyme sales and the employees in the companies that produce enzymes for sale still increases linearly. The numbers increase by a factor ≈ 2 in ten years. If you have no access to the book I can you Chapter I with more answers to your question per e-mail. Then I need your e-mail.
Thanks for the answer ,,, ı ve sent my E-mail address in a message to you
Regards
Several examples are given here: Bornscheuer, U.T. et al. (2012) Engineering the third wave in biocatalysis, Nature, 485, 185-194
See also the Sitagliptin case, where chemical and enzymatic method were compared: Desai AA (2011) Sitagliptin manufacture: a compelling tale of green chemistry, process intensification, and industrial asymmetric catalysis. Angew Chem Int Ed Engl 50:1974-1976
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