Christian Wandrey

Bio: Christian Wandrey is an academic researcher from Bayer. The author has contributed to research in topics: Amino acid & Membrane reactor. The author has an hindex of 6, co-authored 16 publications receiving 399 citations. Previous affiliations of Christian Wandrey include Clausthal University of Technology.

Ultrafiltration for the Separation of Biocatalysts

Abstract: The application of ultrafiltration in biotechnology is reviewed emphasizing the separation of catalytically active species. Ultrafiltration as a separation process as well as its application to membrane reactors is analyzed. On the basis of an application-oriented theory of ultrafiltration, the essential aspects for process design are described. A survey of applications is given.

Process development and economic aspects in enzyme engineering. Acylase L-methionine system

Abstract: An integral study of chemical reaction engineering and process development including economic aspects was carried out using the optical resolution of aminoacids by means of native and carrier-fixed acylase as example. Continuous operation is not only possible with carrier-fixed enzymes but also with native enzymes using ultrafiltration devices for catalyst retention. It could experimentally be proved on a 1 kg L-methionine/d-scale that the use of soluble acylase in membrane-reactors is economically superior to the carrier-fixed type in the tube-reactors. In all cases where immobilization of enzymes cannot be achieved with high activity yield or remarkable increase in stability, the homogeneous catalysis with soluble enzymes in continuously operating membrane-reactors might be a very promising alternative. — These studies were performed at the “Institut fur Technische Che-mie der Technischen Universitat Hannover”, West-Germany.

Aldolases for Use in Carbohydrate Synthesis: Enzymatic Reaction Engineering as a Tool for Process Optimization

Abstract: In many cases Aldolases have been proved to be useful for the synthesis of carbohydrates [1]. Here we present the optimization of reaction conditions for the application of N-acetylneuraminic acid aldolase for the synthesis of N-acetylneuraminic acid (Neu5Ac) in a continuous process which is suitable for large-scale production.

Process for the stereoselective preparation of functionalized vicinal diols

Abstract: The present invention relates to a process for the kinetic resolution of racemic functionalized epoxides in the presence of microorganisms, crude or pure preparations thereof comprising a polypeptide having epoxide hydrolase activity. Preferred microorganisms are yeasts and bacteria which may also be recombinant.

Engineering the third wave of biocatalysis

Abstract: Over the past ten years, scientific and technological advances have established biocatalysis as a practical and environmentally friendly alternative to traditional metallo- and organocatalysis in chemical synthesis, both in the laboratory and on an industrial scale. Key advances in DNA sequencing and gene synthesis are at the base of tremendous progress in tailoring biocatalysts by protein engineering and design, and the ability to reorganize enzymes into new biosynthetic pathways. To highlight these achievements, here we discuss applications of protein-engineered biocatalysts ranging from commodity chemicals to advanced pharmaceutical intermediates that use enzyme catalysis as a key step.

Microbial enzymes: industrial progress in 21st century

Abstract: Biocatalytic potential of microorganisms have been employed for centuries to produce bread, wine, vinegar and other common products without understanding the biochemical basis of their ingredients. Microbial enzymes have gained interest for their widespread uses in industries and medicine owing to their stability, catalytic activity, and ease of production and optimization than plant and animal enzymes. The use of enzymes in various industries (e.g., food, agriculture, chemicals, and pharmaceuticals) is increasing rapidly due to reduced processing time, low energy input, cost effectiveness, nontoxic and eco-friendly characteristics. Microbial enzymes are capable of degrading toxic chemical compounds of industrial and domestic wastes (phenolic compounds, nitriles, amines etc.) either via degradation or conversion. Here in this review, we highlight and discuss current technical and scientific involvement of microorganisms in enzyme production and their present status in worldwide enzyme market.

Biocatalysis in Organic Chemistry and Biotechnology: Past, Present, and Future

Abstract: Enzymes as catalysts in synthetic organic chemistry gained importance in the latter half of the 20th century, but nevertheless suffered from two major limitations. First, many enzymes were not accessible in large enough quantities for practical applications. The advent of recombinant DNA technology changed this dramatically in the late 1970s. Second, many enzymes showed a narrow substrate scope, often poor stereo- and/or regioselectivity and/or insufficient stability under operating conditions. With the development of directed evolution beginning in the 1990s and continuing to the present day, all of these problems can be addressed and generally solved. The present Perspective focuses on these and other developments which have popularized enzymes as part of the toolkit of synthetic organic chemists and biotechnologists. Included is a discussion of the scope and limitation of cascade reactions using enzyme mixtures in vitro and of metabolic engineering of pathways in cells as factories for the production o...

Biocatalysis: Enzymatic Synthesis for Industrial Applications

Abstract: Biocatalysis has found numerous applications in various fields as an alternative to chemical catalysis. The use of enzymes in organic synthesis, especially to make chiral compounds for pharmaceuticals as well for the flavors and fragrance industry, are the most prominent examples. In addition, biocatalysts are used on a large scale to make specialty and even bulk chemicals. This review intends to give illustrative examples in this field with a special focus on scalable chemical production using enzymes. It also discusses the opportunities and limitations of enzymatic syntheses using distinct examples and provides an outlook on emerging enzyme classes.

Laboratory Evolution of Stereoselective Enzymes: A Prolific Source of Catalysts for Asymmetric Reactions

Abstract: Asymmetric catalysis plays a key role in modern synthetic organic chemistry, with synthetic catalysts and enzymes being the two available options. During the latter part of the last century the use of enzymes in organic chemistry and biotechnology experienced a period of rapid growth. However, these biocatalysts have traditionally suffered from several limitations, including in many cases limited substrate scope, poor enantioselectivity, insufficient stability, and sometimes product inhibition. During the last 15 years, the genetic technique of directed evolution has been developed to such an extent that all of these long-standing problems can be addressed and solved. It is based on repeated cycles of gene mutagenesis, expression, and screening (or selection). This Review focuses on the directed evolution of enantioselective enzymes, which constitutes a fundamentally new approach to asymmetric catalysis. Emphasis is placed on the development of methods to make laboratory evolution faster and more efficient, thus providing chemists and biotechnologists with a rich and non-ending source of robust and selective catalysts for a variety of useful applications.