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Metagenomics: a proven shortcut to enzyme genes.

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Metagenomics may at first seem to be a long, involved route to finding genes essential for making an industrial enzyme. Actually, it is much faster than many other approaches.

Here is how it works: First, microorganisms are collected from the outdoors and brought into the laboratory. The microbes' genes and other deoxyribonucleic acid (DNA) are, for research purposes, transferred into other organisms--such as a harmless laboratory strain of Escherichia coli (E. coli.

Each E. coli organism can take up and activate only a few of the borrowed genes. That makes close-up scrutiny of those genes much easier. In Petri dish tests, scientists determine whether any of the borrowed genes endow any E. coli with the ability to produce an enzyme of interest. One that degrades xylan would be of interest because xylan forms the backbone of hemicellulose, a molecule that complicates production of cellulosic ethanol.

If any E. coli are now equipped with a xylan-degrading enzyme, or "xylanase," it takes only a few more steps to fmd which gene holds the blueprint for making that enzyme. Once the new xylanase gene is found and its structure is determined, the gene can be copied. After that, it can be shuttled into other microbes, such as yeasts. The yeasts follow the gene's instructions, churning out large quantities of the enzyme for further study.

If the enzyme proves to be worthwhile, it might be produced commercially.

(Source: Agricultural Research, October 2008.)

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Publication:Nutrition Health Review
Article Type:Brief article
Geographic Code:1USA
Date:Sep 22, 2010
Words:240
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