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.
Lipoxidase from
Glycine max (soybean) has been used:
- to study the effects of 2-(α-D-glucopyranosyl)methyl-2,5,7,8-tetramethylchroman-6-ol(TMG) on oxidation of lipoproteins
- as a representative enzyme for lipoxygenases in microplate assay platform to screen for enzymes degrading wood extractives
- as a positive control in lipoxygenase inhibitory activity assay
Lipoxidase from Glycine max (soybean) has been used for the modification of low density lipoprotein, isolated from human plasma.
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.
