International Conference on Novel Enzymes

Enzymes work in aqueous solutions, at ambient temperature and produce little toxic waste – hence their use is often referred to as green or environmentally friendly chemistry. They have advantages for the pharmaceutical industry since they carry out their reactions in a specific way to produce purer and safer drugs. They also have many more applications such as helping to reduce greenhouse gas emissions, biofuel production, soap powders and cosmetics and within the food industry. They are already used in many aspects of our daily life.

Delegates discussed the discovery of new novel enzymes from organisms able to grow at high temperatures in volcanic areas, in black smokers in the deep oceans, and deep in South African Gold mines, 5km below the earth’s surface. Novel enzymes are also being discovered in marine viruses and in newly discovered novel viruses found in organisms that grow at high temperatures. These are often very evolutionary distant from enzymes we are more familiar with and are difficult to identify from their DNA sequence. It is also possible to identify new novel enzymes by just isolating the DNA from different natural sources. This is called metagenomics which allows identification of enzymes from the many bacteria that cannot be cultivated. Modern molecular biology techniques allow these genes to be identified and amplified so that the enzymes can be made in an easily cultivated bacterium such as Escherichia coli. To identify the different activities of the newly discovered enzymes rapid screening techniques have been developed with both natural and un-natural substrates.

One problem with the use of enzymes industrially is their stability which can be enhanced by immobilising them onto a solid support or trapping them within gels. This also allows their recovery and subsequent reuse making for a cheaper and easier industrial process. An alternative approach is to use naturally thermostable enzymes which are often isolated from the evolutionary ancient branch of life called the Archaea. The enzymes from these organisms are often unique to this branch of life since they are found in novel metabolic pathways. Many other archaeal enzymes have features between those of the bacteria and higher eukaryotic cells.

Enzymes can be modified genetically to have improved properties for activity and stability. Computational approaches can be used to help fully exploit an enzyme’s catalytic potential or its substrate specificity. This can also be used for inhibition of an enzyme’s activity in relation to drug design. These computer based methods can be combined with an experimental approach. Many industrially used enzymes have been modified from natural enzymes so they are optimised for the industrial process. All of these aspects were included in the first two days of the meeting and the last day was devoted to industrial applications including the use of enzymes to make metabolites urgently needed for identification of compounds for the area of metabolomics.

The conference allowed participants from both academia and industry to exchange ideas within this multidisciplinary area of research. It attracted many people to the South West of UK and Exeter University for the first time. The invited speakers will contribute their papers to a special edition of the Journal of Biocatalysis and Biotransformations.

The conference was generously sponsored by a range of companies including Sprin Technologies, Rigaku, New England Biolabs, Iris, Sigma Aldrich, Merck, Laboratory Analysis Limited, Bioline and Qiagen. Several of these companies had industrial exhibits in the Peter Chalk Centre where there were also over 30 posters.