By Sergio Riva, Wolf-Dieter Fessner
This prepared reference offers environmentally pleasant and stereoselective tools of contemporary biocatalysis. The skilled and well known crew of editors have amassed most sensible foreign authors for this ebook. They disguise such rising subject matters as chemoenzymatic tools and multistep enzymatic reactions, whereas displaying how those novel equipment and ideas can be utilized for useful purposes. Multidisciplinary subject matters, together with directed evolution, dynamic kinetic solution, and continuous-flow technique also are discussed.
From the contents:
* Directed Evolution of Ligninolytic Oxidoreductases: from practical Expression to Stabilization and Beyond
* New traits within the In Situ Enzymatic Recycling of NAD(P)(H) Cofactors
* Monooxygenase-Catalyzed Redox Cascade Biotransformations
* Biocatalytic Redox Cascades concerning w-Transaminases
* Multi-Enzyme platforms and Cascade Reactions concerning Cytochrome P450 Monooxygenases
* Chemo-Enzymatic Cascade Reactions for the Synthesis of Glycoconjugates
* Synergies of Chemistry and Biochemistry for the creation of Beta-Amino Acids
* Racemizable Acyl Donors for Enzymatic Dynamic Kinetic Resolution
* Stereoselective Hydrolase-Catalyzed procedures in Continuous-Flow Mode
* views on Multienzyme strategy Technology
* Nitrile changing Enzymes excited about average and artificial Cascade Reactions
* Mining Genomes for Nitrilases
* Key-Study at the Kinetic elements of the In-Situ NHase/AMase Cascade approach of M. imperiale Resting Cells for Nitrile Bioconversion
* Enzymatic Stereoselective Synthesis of Beta-Amino Acids
* New purposes of Transketolase: Cascade Reactions for Assay Development
* Aldolases as Catalyst for the Synthesis of Carbohydrates and Analogs
* Enzymatic iteration of Sialoconjugate Diversity
* Methyltransferases in Biocatalysis
* Chemoenzymatic Multistep One-Pot Processes
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Additional info for Cascade Biocatalysis Integrating Stereoselective and Environmentally Friendly Reactions
2009) Narrowing laccase substrate speciﬁcity using active site saturation mutagenesis. Comb. Chem. High Throughput Screening, 12, 269–274. B. (2009) Improving the functional expression of a Bacillus licheniformis laccase by random and sitedirected mutagenesis. , 9, 12. T. (2010) Laboratory evolution of laccase for substrate speciﬁcity. J. Mol. Catal. , 62, 230–234. Gupta, N. T. (2010) Directed evolution of CotA laccase for increased substrate speciﬁcity using Bacillus subtilis spores. Protein Eng.
Recently, the MtL-R2 mutant was converted into an alkalophilic fungal laccase . 0 was used as the main discriminatory factor. 0). 0. After 20 generations, the successful in vitro evolution of MtL can be attributed to the plasticity and robustness of this thermostable protein, highlighting that there may be an additional margin for further engineering. 3 Directed Evolution of Ligninolytic High-Redox Potential Laccases (HRPLs) Two HRPLs from the basidiomycete PM1 laccase (PM1L) and Pycnoporus cinnabarinus laccase (PcL) were subjected to parallel comprehensive directed evolution in order to achieve functional expression in S.
76, 99–107. C. H. (2012) Directed evolution of the peroxidase activity of a novo-designed protein. Protein Eng. Des. , 25 (9), 445–451. , and Takahashi, H. (2003) Improvement of H2 O2 stability of manganese peroxidase by combinatorial mutagenesis and high-throughput screening using in vitro expression with protein disulﬁde isomerase. , 16, 423–428. K. (2008) Functionality improvement of fungal lignin peroxidase by DNA shufﬂing for 2,4-dichlorophenol degradability and H2 O2 stability. J. , 133, 110–115.
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