Bioconversion of airborne methylamine by immobilized recombinant amine oxidase from the thermotolerant yeast Hansenula polymorpha. 2014

Sasi Sigawi, and Marina Nisnevitch, and Oksana Zakalska, and Andriy Zakalskiy, and Yeshayahu Nitzan, and Mykhailo Gonchar
Department of Chemical Engineering and Biotechnology, Ariel University, 40700 Ariel, Israel ; The Mina and Everard Goodman Faculty of Life Sciences, Bar-Ilan University, 52900 Ramat Gan, Israel.

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.

UI MeSH Term Description Entries
D008744 Methylamines Derivatives of methylamine (the structural formula CH3NH2).
D010843 Pichia Yeast-like ascomycetous fungi of the family Saccharomycetaceae, order SACCHAROMYCETALES isolated from exuded tree sap. Hansenula,Hansenulas,Pichias
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D004800 Enzymes, Immobilized Enzymes which are immobilized on or in a variety of water-soluble or water-insoluble matrices with little or no loss of their catalytic activity. Since they can be reused continuously, immobilized enzymes have found wide application in the industrial, medical and research fields. Immobilized Enzymes,Enzyme, Immobilized,Immobilized Enzyme
D005822 Genetic Vectors DNA molecules capable of autonomous replication within a host cell and into which other DNA sequences can be inserted and thus amplified. Many are derived from PLASMIDS; BACTERIOPHAGES; or VIRUSES. They are used for transporting foreign genes into recipient cells. Genetic vectors possess a functional replicator site and contain GENETIC MARKERS to facilitate their selective recognition. Cloning Vectors,Shuttle Vectors,Vectors, Genetic,Cloning Vector,Genetic Vector,Shuttle Vector,Vector, Cloning,Vector, Genetic,Vector, Shuttle,Vectors, Cloning,Vectors, Shuttle
D006631 Amine Oxidase (Copper-Containing) A group of enzymes including those oxidizing primary monoamines, diamines, and histamine. They are copper proteins, and, as their action depends on a carbonyl group, they are sensitive to inhibition by semicarbazide. Diamine Oxidase,Histaminase,Amine Oxidase, Copper-Containing,Copper Amine Oxidase,Diaminobenzidine Oxidase,Semicarbazide-Sensitive Amine Oxidase,Xylylene Diamine Oxidase,Amine Oxidase, Copper,Amine Oxidase, Copper Containing,Amine Oxidase, Semicarbazide-Sensitive,Copper-Containing Amine Oxidase,Diamine Oxidase, Xylylene,Oxidase, Copper Amine,Oxidase, Copper-Containing Amine,Oxidase, Diamine,Oxidase, Diaminobenzidine,Oxidase, Semicarbazide-Sensitive Amine,Oxidase, Xylylene Diamine,Semicarbazide Sensitive Amine Oxidase
D000393 Air Pollutants Any substance in the air which could, if present in high enough concentration, harm humans, animals, vegetation or materials. Substances include GASES; PARTICULATE MATTER; and volatile ORGANIC CHEMICALS. Air Pollutant,Air Pollutants, Environmental,Environmental Air Pollutants,Environmental Pollutants, Air,Air Environmental Pollutants,Pollutant, Air,Pollutants, Air,Pollutants, Air Environmental,Pollutants, Environmental Air
D001673 Biodegradation, Environmental Elimination of ENVIRONMENTAL POLLUTANTS; PESTICIDES and other waste using living organisms, usually involving intervention of environmental or sanitation engineers. Bioremediation,Phytoremediation,Natural Attenuation, Pollution,Environmental Biodegradation,Pollution Natural Attenuation
D012441 Saccharomyces cerevisiae A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement. Baker's Yeast,Brewer's Yeast,Candida robusta,S. cerevisiae,Saccharomyces capensis,Saccharomyces italicus,Saccharomyces oviformis,Saccharomyces uvarum var. melibiosus,Yeast, Baker's,Yeast, Brewer's,Baker Yeast,S cerevisiae,Baker's Yeasts,Yeast, Baker

Related Publications

Sasi Sigawi, and Marina Nisnevitch, and Oksana Zakalska, and Andriy Zakalskiy, and Yeshayahu Nitzan, and Mykhailo Gonchar
January 1990, Journal of chemical technology and biotechnology (Oxford, Oxfordshire : 1986),
Sasi Sigawi, and Marina Nisnevitch, and Oksana Zakalska, and Andriy Zakalskiy, and Yeshayahu Nitzan, and Mykhailo Gonchar
January 2006, Preparative biochemistry & biotechnology,
Sasi Sigawi, and Marina Nisnevitch, and Oksana Zakalska, and Andriy Zakalskiy, and Yeshayahu Nitzan, and Mykhailo Gonchar
January 2014, BioMed research international,
Sasi Sigawi, and Marina Nisnevitch, and Oksana Zakalska, and Andriy Zakalskiy, and Yeshayahu Nitzan, and Mykhailo Gonchar
April 1992, Yeast (Chichester, England),
Sasi Sigawi, and Marina Nisnevitch, and Oksana Zakalska, and Andriy Zakalskiy, and Yeshayahu Nitzan, and Mykhailo Gonchar
January 2005, Artificial cells, blood substitutes, and immobilization biotechnology,
Sasi Sigawi, and Marina Nisnevitch, and Oksana Zakalska, and Andriy Zakalskiy, and Yeshayahu Nitzan, and Mykhailo Gonchar
November 2003, FEMS yeast research,
Sasi Sigawi, and Marina Nisnevitch, and Oksana Zakalska, and Andriy Zakalskiy, and Yeshayahu Nitzan, and Mykhailo Gonchar
July 1989, Biochimica et biophysica acta,
Sasi Sigawi, and Marina Nisnevitch, and Oksana Zakalska, and Andriy Zakalskiy, and Yeshayahu Nitzan, and Mykhailo Gonchar
April 1993, FEBS letters,
Sasi Sigawi, and Marina Nisnevitch, and Oksana Zakalska, and Andriy Zakalskiy, and Yeshayahu Nitzan, and Mykhailo Gonchar
September 2010, Applied microbiology and biotechnology,
Sasi Sigawi, and Marina Nisnevitch, and Oksana Zakalska, and Andriy Zakalskiy, and Yeshayahu Nitzan, and Mykhailo Gonchar
November 2012, Applied microbiology and biotechnology,
Copied contents to your clipboard!