Exploitable results COLDZYME: Molecular characterization of cold-active enzymes from psychrophillic microorganisms as a basis for novel biotechnology The COLDZYME project brought together leading European laboratories working in the field of microbiology, biochemistry, molecular biology, protein crystallography and enzyme chemistry, in order to improve understanding of the cold-active enzymes from psychrophillic ("cold-loving") bacteria, in order to provide fundamental information needed for their exploitation in novel biotechnologies such as cold-water washing, production of biopharmaceuticals and environmental sensors. The enzymes which are used currently in industrial applications and domestic products, work preferentially at warm to hot temperatures because they are derived almost entirely from organisms which grow best at temperatures around 30-40 degrees C. However, many biotechnological applications require much lower temperatures, typically that of cold water. Psychrophilic bacteria provide the opportunity to obtain and exploit such enzymes, but before that can be achieved basic information is needed about their structure. The COLDZYME project has facilitated great strides to be made in the understanding of the way in which cold-active enzymes are folded so that they remain flexible and therefore active at low temperatures (in complete contrast to enzymes from organisms that live at higher temperatures). New bacteria isolated from the Alps and Antarctica have served as the source of enzymes such as alpha amylase (which digests starch) and dehydrogenases (which oxidize specific substrates). The general experimental approach has been to clone the relevant gene and then to use it to produce large amounts of the enzyme protein for crystallization and structural determinations. Knowledge of the gene sequence also used to engineer mutants that have improved properties relating to thermal stability and activity. The structure of alpha amylase has been determined in a complex with the inhibitor acarbose and the regulation of the enzyme as well as the basis of its cold activity determined. This information has medical relevance because compounds such as acarbose are useful in therapy of such diseases as diabetes. The structures of cold-active protein-degrading enzymes have also been elucidated and one has been engineered with better properties in relation to cold-water washing. Cold-active dehydrogenase enzymes that oxidize chemicals such as alcohol or lactic acid have been studied and a laboratory prototype of a cold-active sensor that could be developed for on-line environmental monitoring has been tested. These examples serve to illustrate how the advance in basic knowledge has provided the potential for biotechnological application. Importantly, the COLDZYME project has maintained Europe's pre-eminence in the field of cold-active enzymes and provided a platform for future work on both fundamental and applied aspects that are needed for developing the new technology. COLDZYME: enzymes for washing powders that are active at low temperatures Enzymes found in Antarctic bacteria can be used both in industrial applications and in domestic products such as washing powder as they active at low temperatures thus giving huge energy savings. Washing machines would no longer need heating elements, for example. Other applications for low-temperature enzymes include contact lens cleansing, biosensors for environmental monitoring and indeed environmental depollution. There are also a variety of potential uses for cold active enzymes in the pharmaceutical industries or in food processing, particularly in the dairy sector. Enzymes secreted by bacteria collected in the Alps and Antarctica are being. isolated and characterized. In order to carry out its catalytic function, a protein molecule must remain flexible. These enzymes are folded in such a way that they stay flexible at temperatures at which those produced by normal bacteria stop working, This characteristic can be used to engineer low-temperature activity into other enzymes. The psychrophilic bacteria themselves are also being studied with a view to using them as 'cell factories' to produce large quantities of genetically-engineered cold-active enzymes. Novel biotechnologies may also develop from certain enzymes that show new specificities when operated cold. For some compounds, specific isomers could be produced by running bio-transformations at lower temperatures, changing or improving the purity of the product. Crystallizing enzymes that degrade starch and protein has already been successfully completed and nuclear magnetic resonance facilities are being used to analyse protein flexibility with a view to producing cold-water washing powder. Searching for OpenAIRE data... There was an error trying to search data from OpenAIRE No results available
