Titlebook: Directed Enzyme Evolution: Advances and Applications; Miguel Alcalde Book 2017 Springer International Publishing AG 2017 biocatalysis.biom

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Konstruktionsvalidierung durch Simulation,ed by catalytic concentrations of H.O., which acts as both oxygen donor and as final electron acceptor, this stable, soluble, and extracellular enzyme is a potential biocatalyst for dozens of transformations that are of considerable interest in organic synthesis. In this chapter we describe the main

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https://doi.org/10.1007/978-3-658-03047-6gains, oilseeds, and legumes and is indigestible by monogastric animals such as poultry and swine. Supplementation of phytase in animal feed proved to improve animal nutrition and decrease phosphorous pollution. Several phytases were discovered in the last century, and today a highly competitive mar

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https://doi.org/10.1007/978-3-658-03047-6traits with hundreds of genetic determinants and for organisms with few genetic tools. Directed evolution mimics natural evolution in the laboratory via iterative cycles of diversity generation and functional selection or screening to isolate evolved mutants with desirable phenotypes. In this chapte

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https://doi.org/10.1007/978-3-658-03047-6satisfy a wide range of biotechnological applications, from synthetic biology through to industrial biocatalysis. Laboratory evolution is an iterative process, alternating between creating genetic diversity and selection/screening to identify improved variants. This book chapter focuses on genetic d

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https://doi.org/10.1007/978-3-531-94062-5es in protein scaffolds for laboratory-directed evolution and molecular design. Furthermore, the two features are not necessarily incompatible, and proteins may simultaneously be promiscuous/flexible and highly stable. In fact, it appears plausible that the combination of the two features was not un

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https://doi.org/10.1007/978-3-531-94062-5lysis. Although this technique does not require any structural/mechanistic knowledge of the system, the frequency of improved mutations is usually low. For this reason, computational tools are increasingly used to focus the search in sequence space, enhancing the efficiency of laboratory evolution.

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Directed Evolution of an Allosteric Tryptophan Synthase to Create a Platform for Synthesis of Noncao acids. We used directed evolution to enhance the activity of TrpB from . (.TrpB), so that it can act as a stand-alone biocatalyst. Remarkably, we found that mutational activation mimics the allosteric activation induced by binding of TrpA. Toward our goal of expanding the substrate scope of this r

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Engineering Therapeutic Enzymes,ng of therapeutic enzymes. More specifically, our review will focus on three categories of therapeutic enzymes: pharmaceutical enzymes where the protein itself constitutes the therapeutic agent, prodrug-activating enzymes where the protein indirectly triggers a clinical effect, and diagnostic enzyme

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Improving CO2 Fixation by Enhancing Rubisco Performance, focus on using .. The inherent sensitivity of . viability to the pentose sugar substrate of Rubisco, RuBP, is being exploited in an increasingly effective manner to select for Rubisco mutants with increased activity. Here we review the differing directed evolution technologies used to evolve Rubisc

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Recent Advances in Directed Phytase Evolution and Rational Phytase Engineering,ty, pH stability, pH optima, and protease resistance have been discussed with respect to structural perspective and potential molecular mechanism for improvement. Importance of cooperative substitutions and a way to identify these interactions are discussed. Recent development in screening technolog