Co-immobilized coupled enzyme systems in biotechnology
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چکیده
منابع مشابه
Co-immobilized coupled enzyme systems in biotechnology.
The development of coimmobilized multi-enzymatic systems is increasingly driven by economic and environmental constraints that provide an impetus to develop alternatives to conventional multistep synthetic methods. As in nature, enzyme-based systems work cooperatively to direct the formation of desired products within the defined compartmentalization of a cell. In an attempt to mimic biology, c...
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Aroma is a remarkable factor of quality and consumer preference in wine, representing a distinctive feature of the product. Most aromatic compounds in varietals are in the form of glycosidic precursors, which are constituted by a volatile aglycone moiety linked to a glucose residue by an O-glycosidic bond; glucose is often linked to another sugar (arabinose, rhamnose or apiose). The use of solu...
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The advantages of immobilized enzyme over its soluble counterpart arise from their improved stability andeasy separation from the reaction media, leading to decrease in production cost. Immobilization methodsrange from adsorption onto matrices, entrapment, cross-linking and covalent bonding to prefabricatedcarriers or activated supports. Changes in kinetic properties of immobi...
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Microreaction technology, which is an interdisciplinary science and engineering area, has been the focus of different fields of research in the past few years. Several microreactors have been developed. Enzymes are a type of catalyst, which are useful in the production of substance in an environmentally friendly way, and they also have high potential for analytical applications. However, not ma...
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A bacterial enzyme(s) capable of hydrolyzing nine organophosphate insecticides was covalently bound to glass. The efficiency of this binding reaction ranged from 4 to 17%. Under continuous column operation, the immobilized enzyme(s) had an extrapolated half-life of 280 days. The specific activity of this glass-covalently bound hydrolase activity for parathion varied from 0.035 to 0.15 mumol/min...
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ژورنال
عنوان ژورنال: Biotechnology and Genetic Engineering Reviews
سال: 2010
ISSN: 0264-8725,2046-5556
DOI: 10.1080/02648725.2010.10648146