By Prof. Dr. Uwe T. Bornscheuer, Prof. Dr. Romas J. Kazlauskas(auth.)
From studies to the 1st edtion:
"Bornscheuer and Kazlauskas have set out, and succeeded, in generating a definitive guide on hydrolytic enzymes (especially lipases, esterases, and proteases) for natural chemists. this can be without difficulty the easiest ebook of its sort and will be unreservedly steered to natural chemists who've an curiosity in utilizing hydrolytic enzymes in synthesis." (Nicholas J. Turner, college of Edinburgh)
"The booklet is an quintessential resource of data at the use of hydrolases in natural synthesis. the subject material is particularly good set out, and the chapters are sincerely written and awarded from a severe perspective. Bornscheuer and Kazlauskas have succeeded admirably in describing the functions and obstacles of using hydrolytic enzymes and in severely comparing them. No library will be with out the book." (Fritz Theil, WITEGA Angewandte Werkstoff-Forschung GmbH, Berlin)
the second one variation of this super profitable and well-proven booklet provides contemporary advancements within the use of hydrolases for natural synthesis, reflecting particularly the big growth made in enzyme discovery and optimization with a brand new bankruptcy on "Protein assets and Optimization of Biocatalyst Performance".
The popular authors survey the stereoselective reactions of hydrolases, in particular lipases, esterases and proteases, giving researchers an summary of what has labored some time past for you to pass judgement on tips to clear up their very own artificial difficulties. In overall, the booklet comprises over a thousand chemical constructions, rounded off by means of a few 1,800 precious references.
Content:
Chapter 1 creation (pages 1–3):
Chapter 2 Designing Enantioselective Reactions (pages 5–24):
Chapter three selecting response Media: Water and natural Solvents (pages 25–42):
Chapter four Protein assets and Optimization of Biocatalyst functionality (pages 43–59):
Chapter five Lipases and Esterases: Sections 5.1 ? 5.2 (pages 61–140):
Chapter five Lipases and Esterases: Sections 5.3 ? 5.4 (pages 141–183):
Chapter 6 Proteases and Amidases (pages 185–210):
Chapter 7 Phospholipases (pages 211–214):
Chapter eight Epoxide Hydrolases (pages 215–226):
Chapter nine Hydrolysis of Nitriles (pages 227–240):
Chapter 10 different Hydrolases (pages 241–248):
Read Online or Download Hydrolases in Organic Synthesis: Regio- and Stereoselective Biotransformations, Second Edition PDF
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Extra resources for Hydrolases in Organic Synthesis: Regio- and Stereoselective Biotransformations, Second Edition
Sample text
Selected examples of lipase-catalyzed asymmetric syntheses are shown in Fig. 23; more are included in the survey of enantioselectivity in Sect. , 1996). The lipase-catalyzed asymmetric syntheses include a wide range of primary and secondary alcohols, as well as carboxylic acids. , 1991), a mesosecondary alcohol. 2 Asymmetric Syntheses purity (95% ee). Many of the primary alcohol examples are 2-substituted 1,3-propanediols, which are versatile synthetic starting materials. The dihydropyridine example below is a chiral acid, but the acetyloxymethyl group places the stereocenter in the alcohol part of the ester; thus, this prochiral compound can be classified as a chiral alcohol.
1995; Halling, 1990; 1994; 1996). , 1992a). , 1994; 1995). Polar solvents require more added water than nonpolar solvents because polar solvents competed more effectively with the lipase for the available water. Bell et al. (1995) suggested that water activity is like temperature, while water content is like heat content. Two systems may have the same water activity or temperature, but at the same time differ in the water content or heat content. Of the available methods for controlling the thermodynamic water activity (Tab.
The most common method is the cross-linking of adsorbed biocatalysts with glutaraldehyde. Several enzymes from the Chirazyme series were immobilized by this method. , 1985). Covalent immobilization often increases the thermal or operational stability of the enzyme, but does not activate it. , 2001). The native enzyme and two carrier-linked lipase preparations show no or only modest changes in activity and enantioselectivity in the kinetic resolution of a racemic carboxylic acid ethylester. However, two immobilisates exhibited substantially altered properties (Tab.