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ZyGEM's cornerstones are the Genes, Enzymes and Microbes from our culture collection. These organisms were isolated from a wide range of extreme environments and so produce enzymes with extraordinary and unique properties.
Enzymes are proteins that catalyze chemical reactions in a highly specific way and so are often referred to as "Biocatalysts". Their specificity means that the unwanted by-products produced by standard chemical reactions can be avoided. For example, chemical processes fail to differentiate between stereo-isomers (mirror images of the same compound) and so often, chemically produced agents such as pharmaceuticals and agrochemicals can be mixtures of compounds all with the same chemical formula but with different three-dimensional shapes. Usually, only one of the variants is useful … and sometimes, the others are highly toxic!
When manufacturing complex molecules, enzymes are an obvious choice. However, the uptake of this technology has been slowed by the fact that enzymes, being biological compounds, need precise reaction conditions; otherwise they are inactive or are destroyed.
The breadth of ZyGEM's culture collection and knowledge-base means that we can tailor the enzyme of choice to fit current and new sample processes. The goal being to optimize the process without costly changes in the manufacturing plant or the workflow. With well-studied organisms growing across a 100°C range of temperatures, ZyGEM can accommodate most needs.
The first enzyme to be released from the ZyGEM product pipeline is neutral proteinase from Bacillus sp. EA1 and is the key component of the initial forensicGEM™ and prepGEM™ kits. This enzyme was discovered in the 1980's by Profs. Hugh Morgan and Roy Daniel. Neutral Proteinase are enzymes that act on proteins to break them down into small soluble peptides. This particular family of enzymes are sometimes known as microbial metalloprotenases [EC: 18.104.22.168] – enzymes that are stabilized by Calcium and enhanced by Magnesium.
EA1 proteinase is well characterized , having been studied for over twenty years. Nineteen publications describing it have been published in the scientific press and two patents granted. Having been originally isolated for its activity on cartilage, it was selected from a panel of over 80 proteinases chosen as potential candidates for DNA extraction because of its effectiveness in degrading animal tissue in buffer conditions compatible with the PCR. One of our first major applications for the enzyme is a one-step, closed tube DNA extraction system.