Abstract
The use of monoamine oxidases (MAOs) in amine oxidation is a great example of how biocatalysis can be applied in the agricultural or pharmaceutical industry and manufacturing of fine chemicals to make a shift from traditional chemical synthesis towards more sustainable green chemistry. This article reports the screening of fourteen Antarctic fungi strains for MAO activity and the discovery of a novel psychrozyme MAOP3 isolated from the Pseudogymnoascus sp. P3. The activity of the native enzyme was 1350 ± 10.5 U/L towards a primary (n-butylamine) amine, and 1470 ± 10.6 U/L towards a secondary (6,6-dimethyl-3-azabicyclohexane) amine. MAO P3 has the potential for applications in biotransformations due to its wide substrate specificity (aliphatic and cyclic amines, pyrrolidine derivatives). The psychrozyme operates at an optimal temperature of 30 °C, retains 75% of activity at 20 °C, and is rather thermolabile, which is beneficial for a reduction in the overall costs of a bioprocess and offers a convenient way of heat inactivation. The reported biocatalyst is the first psychrophilic MAO; its unique biochemical properties, substrate specificity, and effectiveness predispose MAO P3 for use in environmentally friendly, low-emission biotransformations.
Highlights
In the second step—oxidative—hydrogen atoms from the reduced FADH2 are transferred by the enzyme to the oxygen molecule, which is reduced to hydrogen peroxide, and flavin adenine dinucleotide (FAD) returns to its oxidized form
The research presented in this work was aimed at identifying the first psychrophilic monoamine oxidases (MAOs)
Fourteen Antarctic fungi strains belonging to the collection of psychrophilic microorganisms at IMIB TUL were cultured for 14 days in an induction medium containing n-butylamine as the sole nitrogen source
Summary
Monoamine oxidases (MAOs) (E.C. 1.4.3.4) belong to the class of oxidoreductases and catalyze the oxidative deamination of biogenic and xenobiotic amines using flavin adenine dinucleotide (FAD) as a prosthetic group and oxygen as an ultimate acceptor of hydrogen atoms [1]. The reactions in which one of the products is released before the second substrate binds to the enzyme’s active site are known as Ping Pong reactions. This means that oxidative deamination is a two-step reaction. In the second step—oxidative—hydrogen atoms from the reduced FADH2 are transferred by the enzyme to the oxygen molecule, which is reduced to hydrogen peroxide, and FAD returns to its oxidized form. The imine intermediate, which leaves the enzyme’s active site before the binding of the oxygen molecule, is spontaneously hydrolyzed to an aldehyde or a ketone [4,5]
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