Scientists at the U.S. Division of Vitality’s Brookhaven National Laboratory have found a brand new function in a plant enzyme that would have implications for the design of new chemical catalysts. The enzyme catalyzes, or initiates, one of the cornerstone chemical reactions wanted to synthesize a wide range of natural molecules, along with those present in lubricants, cosmetics, and those used as raw materials for making plastics.
Shanklin and his group published a paper explaining the research in the journal Plant Physiology.
The group discovered in the middle of their ongoing analysis into enzymes that desaturate plant oils. These desaturase enzymes strip hydrogen atoms off specific adjoining carbon atoms in a hydrocarbon chain and put a double bond between those carbon atoms. Shanklin’s group had previously developed a triple mutant version of a desaturase enzyme with interesting properties, they usually have been studying the three mutations individually to see what each one concluded.
Two of the single mutant enzymes turned out to remove the double bond between adjacent carbon atoms and added an “OH” to every carbon to produce a fatty acid with two adjoining hydroxyl teams.
Fatty acids containing such adjacent OH teams, often known as diols, are essential chemical parts for making lubricants, like those that preserve hot engines working smoothly. They will also be transformed into building blocks for making plastics or different commodity products.
The most effective industrial catalysts for this response are costly, highly risky, and poisonous, he noted.
Another drawback is that there are distinct forms of diols, and it is onerous for chemists to make a single pure form.