Industrial biocatalysis

Some of the industrial biocatalysts are nitrile hydralase (Nitto Chemicals), which has a productivity of 50 g acrylamide per litre per hour penicillin G amidase (Smith Kline Beechem and others), which has a productivity of 1 - 2 tonnes 6-APA per kg of the immobilized enzyme glucose isomerase (Novo Nordisk, etc.), which has a productivity of 20 tonnes of high fmctose syrup per kg of immobilized enzyme (Cheetham, 1998). Wandrey et al. (2000) have given an account of industrial biocatalysis past, present, and future. It appears that more than 100 different biotransformations are carried out in industry. In the case of isolated enzymes the cost of enzyme is expected to drop due to an efficient production with genetically engineered microorganisms or higher cells. Rozzell (1999) has discussed myths and realities... 

Zhao, H.M., Chockalingam, K. and Chen, Z.L. (2002) Directed evolution of enzymes and pathways for industrial biocatalysis. Current Opinion in Biotechnology, 13, 104—110. 

The second general approach is to use whole cells that contain the enzyme or enzymes used in the biocatalytic process. The use of whole cells has the added advantage that coenzyme-dependent enzymes can be used because it is possible to regenerate the relevant coenzyme, through metabolism of the whole cells. This, of course, requires that the whole cells are not only physically intact but also meta-bolically active. Since coenzymes are often involved in building new molecules, industrial biocatalysis typically uses whole-cell systems. 

Panke, S., Held, M. and Wubbolts, M., Trends and innovations in industrial biocatalysis for the production of fine chemicals. Curr. Opin. Biotechnol., 2004,15, 272-279. 

Birkett, J.A. and Robinson C. (1990) Biotransformation of cephalosporins an adjunct to chemistiy. In Real products from Industrial Biocatalysis, Royal Society of Chemistry. 

Rasor, P. and Tischer, W. (1998) Process benefit of enzyme iimnobilisation. Paper presented at Advances in industrial biocatalysis , InBio Emope 98. Amsterdam Spring Innovations Ltd. 

Nagao, A. and Kite, M. (1990) Lipase-catalyzed synthesis of fatty acid esters useful in the food industry. Biocatalysis, 3, 295-305. 

Deimis, J.S. and Davidson, A.A. (1998) Cost modelling of esterification processes. In Advances in Industrial Biocatalysis, InBio Europe 98 symposium proceedings. Stockport, UK Spring Iimovations Ltd. 

A. Kiener, M. Wubbolts, and B. Without, Industrial biocatalysis today and tomorrow, Nature (London), 2001, 409, 258-268. 

A. Zaks, Industrial biocatalysis, Curr. Opin. Chem. Biol. 2001, 5, 130-136. 

Figure 5.2 Chemical structures of three common coenzymes NADH, ATP, and coenzyme A. Since coenzymes and cofactors are often complex and expensive molecules, their regeneration is crucial in industrial biocatalysis applications.

For most enzymes, the CLEC is much more robust than the simple isolated enzyme. CLECs can withstand higher temperatures, they denature more slowly in organic solvents, and they are less susceptible to proteolysis [71]. Moreover, since there is no external support involved, CLECs exhibit a high volumetric productivity. These advantages, together with the tunable particle size (typically 1-100 pm), make CLECs attractive for industrial biocatalysis applications. 

JJ Lalonde, C Govardhan, RA Persichetti, Y-F Wang, AL Margolin. Process-scale application of CLECs the processing and economic benefits of using cross-linked enzyme crystals as biocatalysts. Proc. Industrial Biocatalysis InBio 96, Manchester, UK, 1996. 

Schmid A, Dordick JS, Hauer B, Kiener A, Wubbolts M, Witholt B (2001) Industrial biocatalysis today and tomorrow. Nature 409 258-268... 

Shimada, Y., Watanabe, Y., and Nagao, T. 2005a. Application of lipases to industrial-scale purification of oil- and fat-related compounds. In C. T. Hou (Ed.), Handbook of Industrial Biocatalysis (Chap. 8). Boca Raton, FL CRC Press, Taylor Francis Group. 

Taniguchi, H. 2005. Carbohydrate active-enzymes for the production of oligosaccharides. In Hou, Ching T. (Ed.), Flandbook of Industrial Biocatalysis (ch 20). London Taylor Francis. 

The production of single enantiomers of drug intermediates is increasingly important in the pharmaceutical industry. Biocatalysis provides organic chemists an alternate opportunity to prepare pharmaceutically important chiral compounds. The advantages of biocatalysis over chemical catalysis are that enzyme-catalyzed reactions are stereoselective and regioselective, and can be carried out at ambient temperature and atmospheric pressure providing an environmentally friendly system. The selective examples presented in this... 

The use of industrial enzymes for the synthesis of bulk and fine chemicals represents a somewhat specialized application for biocatalysts relative to their broader uses, as outlined above. Industrial biocatalysis is, however, becoming increasingly relevant within the chemical industry for the production of a wide range of materials (see Table 31.3).1,2,4-8 Broadly defined, a biocatalytic process involves the acceleration of a chemical reaction by a biologically derived catalyst. In practice, the biocatalysts concerned are invariably enzymes and are used in a variety of forms. These include whole cell preparations, crude protein extracts, enzyme mixtures, and highly purified enzymes, both soluble and immobilized. 

Wandrey C, Liese A, Kihumbu D. Industrial biocatalysis past, present, and future. Org. Process Res. Dev. 2000 4 286-290. 

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