A Seminar On The Application Of Enzymes For Biocatalyst

A Seminar On The Application Of Enzymes For Biocatalyst

A Seminar On The Application Of Enzymes For Biocatalyst


Abstract Enzymes have potential to catalyst a wide variety of chemical reactions. They are increasing being sought as environmentally friendly and cost effective alternative to conventionally friendly catalyst used in industries ranging from bioremediation to application in medicine and pharmaceutics. Despite the benefit, they are not suitable for use outside of their native cellular environment however protein engineering can be used to generate enzymes tailored for specific industrial application. The aim is to provide an over view of current industrial applications of enzyme properties.


Enzymes are biological catalysts that facilitate the majority of reaction that occur in biological system. They are fundamental to sustaining life and without them these reactions would not occur on useful omescale, where as non biological catalyst and synthetic reagent often require extreme reaction and constituent and can generate undesired side product.

During the last few years, directed evolution has emerged as the method of choice for engineering functions and properties of enzymes. Before the emergence of this technique, rational engineering, which relied on the gathering of extensive structure-function relationships of enzymes, offered the only possibility for the creation of new enzyme

Activities and some notable successes have been reported. However, rational redesign is beset by problems, most notably the amount of data that has first to be accumulated on each individual enzyme under study, and because, even now, our understanding of the relationship between enzyme structure and function is limited .in addition, the prediction of the effect of mutations is complicated by the growing realization that enzyme molecules exist in solution as a mixture of structural conformers, and that dynamics play an important role in enzyme function. For example, nuclear magnetic resonance (NMR) spectroscopy has identified residues both proximal and distal to the active site of dihydrofolate reductase (DHFR) that are highly dynamic and that are conserved across 36 diverse species of DHFR.


I am here by to discuss the application of enzymes for biocatalyst example of the ways in which enzymes have been used in commercial and industrials processes. The different industrial application have different requirement of the enzyme, for example, the chemical, medicine and pharmaceutical industries generally take full advantage of the high substrate specifically typically to associated with enzymes catalysis to produce fine chemicals and pharmaceutical compounds of enantionmeric purity. However, for many application enzymes are required to have broad substrate specificities because they are require to act on a range of materials. E.g. various Sturm, crude oil etc.


It has already been established that a wide range of enzyme specificities and function can be modified by directed evolution, however, protein and biological engineer become more adventurous, completely new enzyme activities and binding properties will fall with their remit.

The success of such effort will be dependent on intelligent choice of starting scaffold and the development of novel screening strategies for new activities.


Dr. J.L Porter,R.A. Rush,Prof.D.Ollie's.

Clarke H.R, Atkinson T and Holbrook JJ (1989) from analysis to synthesis

Osborne, M. J., Schnell J., Benkovic S. J., Dyson H. J. and Wright P. E. (2001) Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism. Biochemistry 40: 98469859

Van den Heuvel R.H.H fraaije M.W,ferrer

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