Industrial Bioprocessing provides you with the latest intelligence in the industrial bioprocessing field, including new processes to develop specialty chemicals, pharmaceuticals, alternative fuels, and chemical feedstocks. Each week, Industrial Bioprocessing presents you with the latest news on R&D, new business ventures, mergers and acquisitions, as well as marketing and sales initiatives. By subscribing you have an essential resource that allows you to gain and keep a competitive edge in this fast-paced field.
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* Company to Watch - highlights a biotech company on the brink of making a strong market impact.Patents - presents key patents to show the latest trends in intellectual property.
ENZYME IS ACTIVE AT SOLVENT/WATER INTERFACE
Along with the growing interest in enzymatic biosynthesis is the increased
popularity of two-phase liquid reaction systems. These systems make it possible
to optimize the culture of microorganisms in an aqueous environment while
carrying out the reaction efficiently in an organic solvent in which the
reactants and products are dissolved. While a great deal is known about enzyme
adsorption at air/liquid and solid/liquid interfaces, much less is known about
enzymatic behavior at the interfaces of two liquids. Harvey Blanch, C. J. Radke,
and Andrea Hickel of the University of California, Berkeley, have done something
to remedy this situation.
They investigated the activity of hydroxynitrile lyase at the interface
between diisopropyl ether (DIPE) and water ("Biotechnol Bioeng" 65:
425-436). The enzyme comes from the almond tree, Prunus amygdalus. Chemical
industry interest in hydroxynitrile lyase enzymes has increased recently because
of their ability to transform chiral cyanohydrins.
However, industrial-scale use of the enzyme faces several difficulties. When used in the aqueous phase the enantiomerical purity of the product drops, the enzyme is unstable at low pH, and it isn't available in large quantities. A two-phase liquid system could be the solution to these problems.
The researchers designed a cylindrical glass recycle reactor to follow the change of the enzyme's activity in cleaving mandelonitrile to form benzaldehyde. The exact area of the liquid/liquid interface is known. Activity can be measured by product formation. Substrate and product are dissolved in the top, DIPE liquid layer. The enzyme is in the aqueous buffer solution that forms the lower layer. The DIPE layer is recycled through an optical cell where product can be measured by UV spectroscopy.
They found that the enzyme adsorbs at the interface and is extremely stable.
It isn't denatured over a period of several hours, although the increase in
surface pressure shows that the enzyme is penetrating the interface.
Investigation shows that the enzymatic reaction takes place at the interface and not in the aqueous bulk phase. So the most obvious practical knowledge that comes out of this very basic research is that to design an efficient reactor the area of the interface must be large.
Sample Weekly Table of Contents
* ENZYME IS ACTIVE AT SOLVENT/WATER INTERFACE
* BIOSCIENCE GETS DAMAGED WASTEWATER PLANT BACK UP
* CHEAPER HYDROGEN WITH SYNTHETIC ENZYME
* AROMATIC POLYCARBONATES BY ENZYMATIC REACTION
* NATIONAL STARCH AND EXCELSIOR PART WAYS
* PROCESS CONVERTS WASTE INTO FEED MATERIAL
* CONTROLLED FED-BATCH PROCESS DEGRADES PHENOL
* SOME IMPORTANT PATENTS FOR YOU TO CHECK