9029-60-1

Microorganisms, fungi, plants, and their enzymes can be used to synthesize natural flavor compounds. Probably the most important example is the biotechnological production of the highly sought after vanillin. Recently, disrupted cells of the edible basidiomycete Pleurotus sapidus were deployed as a potent biocatalyst for the transformation of (+)-valencene to natural (+)-nootkatone.
The enzyme responsible for the biotransformation was biochemically characterized and purified, and the enzyme encoding cDNA was amplified from a cDNA library by polymerase chain reaction [112]. The catalytic reaction sequence of the enzyme was further investigated and a lipoxygenase-type oxidation of (+)-valencene via secondary and tertiary hydroperoxides was suggested. In ongoing research, the dioxygenase was heterologously expressed in the cytosol and periplasm of Escherichia coli. Only recently, the enzyme was identified as a potent 13S-lipoxygenase (LOXPsa1; linoleate:oxygen 13-oxidoreductase, EC 1.13.11.12), and the kinetic parameters of the recombinant enzyme were determined by using linoleic acid as the substrate.

Lipoxidases (LOXs) are nonheme iron proteins. It is widely present in plants, some microorganisms, and animals. They are categorized as LOX-1, LOX-2, and LOX-3 considering pH and optimum temperature, substrate specificity, and level of inhibition by different agents.

Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.