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the largest uorescence intensity signals for the same bulk glucose concentration (a) Simultaneous coadsorption of both enzymes to underivatized polystyrene. (b) Nonpolymerizing covalent immobilization of glucose-6-phosphate dehydrogenase, followed by cross-linked immobilization of hexokinase. (c) Coimmobilization of the two enzymes through tyrosine residues to form a bienzyme monolayer on the polystyrene surface. 4. Why is the operational stability of an enzyme-based thermal sensor for oxalic acid expected to be poorer than an amperometric oxalate sensor prepared using the same enzyme, oxalate oxidase
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Directed Evolution for the Design of Macromolecular Bioassay Reagents
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8.1. INTRODUCTION Macromolecular reagents, mainly enzymes and antibodies, are widely used in bioanalytical chemistry. Proteins used as reagents are obtained mainly from natural microbial, plant, or animal sources, but in some cases an industrial strain of microorganism, able to produce large amounts of the desired protein, is selected. Sometimes the protein of interest is produced by a bacterial strain not suitable for industrial production. To overcome this problem, the gene coding for the protein may be cloned into an appropriate bacterial strain, and the resulting recombinant bacterium is used as the protein source. Both of these methods allow the production of proteins that are identical, at least in their primary structure, to the original natural protein. From the origin of life until the present time, enzymes and other biomolecules have been naturally selected for their abilities to perform relevant functions in a living cell. This slow biological evolution process is responsible for molecular design changes. Evolution and adaptation are necessary in order to cope with environmental and biological changes along the geological time span, improving the tness of the selected phenotypes. Natural biological evolution occurs as a result of naturally occurring mutations, fragmentation and loss of DNA, duplication, and other genetic processes. Furthermore, sexual recombination increases the possibility of successful genetic combinations. The selection of improved variants occurs as a result of environmental conditions or selection pressures. Natural proteins are adapted or optimized for function in speci c physicochemical conditions. For example, enzymes isolated from bacteria found in Antarctic seawater have high activity at low temperature, but they are denatured at relatively low temperature. Thermophilic bacteria adapted to survive on hotspring water or in volcanic lakes harbor thermostable enzymes possessing almost no activity at low
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Bianalytical Chemistry, by Susan R. Mikkelsen and Eduardo Corton ISBN 0-471-54447-7 Copyright # 2004 John Wiley & Sons, Inc.
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INTRODUCTION
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temperature. The combination of thermostability and low-temperature activity in the same enzyme is not found in nature, because naturally occurring biomolecules are not adapted to cope with such extreme temperature changes. However, enzymes possessing these two characteristics have been designed or evolved in the laboratory. Biological macromolecules have evolved their structures and functions for speci c intracellular conditions. Posttranslational modi cations occur to regulate structure and function in this environment. For example, the enzymatic turnover rate is one of the variables that can be controlled to regulate cellular metabolic pathways that are critical to ensure life. Biomolecules adapted to the complex intracellular environment generally do not possess ideal properties for analytical or industrial applications, where control of activity (through modi cation) and concentration (through biosynthesis and degradation rate) is irrelevant. The differences in the requirements for intracellular and analytical or industrial environments have created new research opportunities for the design of nonnatural biomolecules by genetic modi cation of their naturally occurring counterparts. Goals for enzymatic targets of directed protein evolution have been to increase stability to denaturing agents (temperature, pH, organic solvents), improve solubility in water organic solvent mixtures, and increase activity and/or af nity for substrate. More ambitious projects have also been undertaken to design enzymes with catalytic activity for new (but usually related) substrates. Goals for antibody targets are related to improvement of af nity, production of antibodies with new binding selectivities, and the design of catalytically active
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TABLE 8.1. Examples of Biomolecules Improved by Directed Evolutiona Biomolecule Subtilisin E (protease) Altered Function Increased activity (%170-fold) in organic solvents (60% dimethylformamide) Activity toward a new substrate (cefotaxime) Thermostability and activity increase (14  C) Gained activity toward substrates poorly degraded, improved activity 40-Fold brighter bacterial colonies Tolerates loss of structural disul de bridge Increased enantioselectivity in hydrolysis Approach Error-prone PCR
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b-Lactamase (degradation of antibiotics, i.e., penicillin) p-Nitrobenzyl esterase Biphenyl dioxygenases (degradation of polychlorinated biphenyls) Green orescent protein Immunoglobulin variable domain Lipase
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