Bioconversion of Airborne Methylamine by Immobilized Recombinant Amine Oxidase from the Thermotolerant Yeast Hansenula polymorpha

Aliphatic amines, including methylamine, are air-pollutants, due to their intensive use in industry and the natural degradation of proteins, amino acids, and other nitrogen-containing compounds in biological samples. It is necessary to develop systems for removal of methylamine from the air, since a...

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Main Authors: Sasi Sigawi, Marina Nisnevitch, Oksana Zakalska, Andriy Zakalskiy, Yeshayahu Nitzan, Mykhailo Gonchar
Format: Article
Language:English
Published: Wiley 2014-01-01
Series:The Scientific World Journal
Online Access:http://dx.doi.org/10.1155/2014/898323
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author Sasi Sigawi
Marina Nisnevitch
Oksana Zakalska
Andriy Zakalskiy
Yeshayahu Nitzan
Mykhailo Gonchar
author_facet Sasi Sigawi
Marina Nisnevitch
Oksana Zakalska
Andriy Zakalskiy
Yeshayahu Nitzan
Mykhailo Gonchar
author_sort Sasi Sigawi
collection DOAJ
description Aliphatic amines, including methylamine, are air-pollutants, due to their intensive use in industry and the natural degradation of proteins, amino acids, and other nitrogen-containing compounds in biological samples. It is necessary to develop systems for removal of methylamine from the air, since airborne methylamine has a negative effect on human health. The primary amine oxidase (primary amine : oxygen oxidoreductase (deaminating) or amine oxidase, AMO; EC 1.4.3.21), a copper-containing enzyme from the thermotolerant yeast Hansenula polymorpha which was overexpressed in baker’s yeast Saccharomyces cerevisiae, was tested for its ability to oxidize airborne methylamine. A continuous fluidized bed bioreactor (CFBR) was designed to enable bioconversion of airborne methylamine by AMO immobilized in calcium alginate (CA) beads. The results demonstrated that the bioreactor with immobilized AMO eliminates nearly 97% of the airborne methylamine. However, the enzymatic activity of AMO causes formation of formaldehyde. A two-step bioconversion process was therefore proposed. In the first step, airborne methylamine was fed into a CFBR which contained immobilized AMO. In the second step, the gas flow was passed through another CFBR, with alcohol oxidase from the yeast H. polymorpha immobilized in CA, in order to decompose the formaldehyde formed in the first step. The proposed system provided almost total elimination of the airborne methylamine and the formaldehyde.
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issn 2356-6140
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spelling doaj-art-37a452903a8643689866337745fbc7c22025-02-03T00:59:58ZengWileyThe Scientific World Journal2356-61401537-744X2014-01-01201410.1155/2014/898323898323Bioconversion of Airborne Methylamine by Immobilized Recombinant Amine Oxidase from the Thermotolerant Yeast Hansenula polymorphaSasi Sigawi0Marina Nisnevitch1Oksana Zakalska2Andriy Zakalskiy3Yeshayahu Nitzan4Mykhailo Gonchar5Department of Chemical Engineering and Biotechnology, Ariel University, 40700 Ariel, IsraelDepartment of Chemical Engineering and Biotechnology, Ariel University, 40700 Ariel, IsraelDepartment of Analytical Biotechnology, Institute of Cell Biology, National Academy of Science of Ukraine, Drahomanov Street 14/16, Lviv 79005, UkraineDepartment of Analytical Biotechnology, Institute of Cell Biology, National Academy of Science of Ukraine, Drahomanov Street 14/16, Lviv 79005, UkraineThe Mina and Everard Goodman Faculty of Life Sciences, Bar-Ilan University, 52900 Ramat Gan, IsraelDepartment of Analytical Biotechnology, Institute of Cell Biology, National Academy of Science of Ukraine, Drahomanov Street 14/16, Lviv 79005, UkraineAliphatic amines, including methylamine, are air-pollutants, due to their intensive use in industry and the natural degradation of proteins, amino acids, and other nitrogen-containing compounds in biological samples. It is necessary to develop systems for removal of methylamine from the air, since airborne methylamine has a negative effect on human health. The primary amine oxidase (primary amine : oxygen oxidoreductase (deaminating) or amine oxidase, AMO; EC 1.4.3.21), a copper-containing enzyme from the thermotolerant yeast Hansenula polymorpha which was overexpressed in baker’s yeast Saccharomyces cerevisiae, was tested for its ability to oxidize airborne methylamine. A continuous fluidized bed bioreactor (CFBR) was designed to enable bioconversion of airborne methylamine by AMO immobilized in calcium alginate (CA) beads. The results demonstrated that the bioreactor with immobilized AMO eliminates nearly 97% of the airborne methylamine. However, the enzymatic activity of AMO causes formation of formaldehyde. A two-step bioconversion process was therefore proposed. In the first step, airborne methylamine was fed into a CFBR which contained immobilized AMO. In the second step, the gas flow was passed through another CFBR, with alcohol oxidase from the yeast H. polymorpha immobilized in CA, in order to decompose the formaldehyde formed in the first step. The proposed system provided almost total elimination of the airborne methylamine and the formaldehyde.http://dx.doi.org/10.1155/2014/898323
spellingShingle Sasi Sigawi
Marina Nisnevitch
Oksana Zakalska
Andriy Zakalskiy
Yeshayahu Nitzan
Mykhailo Gonchar
Bioconversion of Airborne Methylamine by Immobilized Recombinant Amine Oxidase from the Thermotolerant Yeast Hansenula polymorpha
The Scientific World Journal
title Bioconversion of Airborne Methylamine by Immobilized Recombinant Amine Oxidase from the Thermotolerant Yeast Hansenula polymorpha
title_full Bioconversion of Airborne Methylamine by Immobilized Recombinant Amine Oxidase from the Thermotolerant Yeast Hansenula polymorpha
title_fullStr Bioconversion of Airborne Methylamine by Immobilized Recombinant Amine Oxidase from the Thermotolerant Yeast Hansenula polymorpha
title_full_unstemmed Bioconversion of Airborne Methylamine by Immobilized Recombinant Amine Oxidase from the Thermotolerant Yeast Hansenula polymorpha
title_short Bioconversion of Airborne Methylamine by Immobilized Recombinant Amine Oxidase from the Thermotolerant Yeast Hansenula polymorpha
title_sort bioconversion of airborne methylamine by immobilized recombinant amine oxidase from the thermotolerant yeast hansenula polymorpha
url http://dx.doi.org/10.1155/2014/898323
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