Scholarship 17/00159-0 - Química verde - BV FAPESP
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Green chemistry: monoamine oxidases (MAO) and imine reductases expression for piperidine synthesis

Grant number: 17/00159-0
Support Opportunities:Scholarships in Brazil - Post-Doctoral
Start date: May 01, 2017
End date: April 30, 2019
Field of knowledge:Physical Sciences and Mathematics - Chemistry - Organic Chemistry
Agreement: GlaxoSmithKline
Principal Investigator:Anita Jocelyne Marsaioli
Grantee:José Matheus Camargo Bonatto
Host Institution: Instituto de Química (IQ). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
Associated research grant:14/50249-8 - Green chemistry: sustainable synthetic methods employing benign solvents, safer reagents, and bio-renewable feedstock, AP.PCPE

Abstract

The concepts of "green chemistry" emerged in the 1990s and include, among others, selective catalysis, degradable chemicals, low toxicity and low risk products. The chemical reactions catalyzed by Enzymes generate regioselective, biodegradable products and act under mild conditions, thus being an extremely interesting and attractive alternative to traditional organic synthesis. Also, biocatalysis has been especially used in industry, being of great importance in research and development. Many enzymes are able to turn substrates into products that are hardly obtainable on chemical routes. Therefore in this context, there is a great demand and importance for the search of new enzymes or improvements in existing enzymes.Brazilian biodiversity presents a huge potential for discovery of new targets of interest in "green chemistry", and knowledge of the genomic sequence of many microorganisms can provide us with knowledge for frontier research in the characterization of enzymes and protein expression of interest and application In the chemical, pharmaceutical and bio-product industries, for example.Previous work by our group carried out the implementation of the high performance screening technique for the detection of enzymatic activity of monoamine oxidase (MAO) in a library of fungi isolated from human skin. Fungus of the genus Marasmius sp. They had a high enzymatic conversion to MAO. We used the LaCTAD facility to sequence the genome from fungus, and found a primary sequence with high homology to the MAO of Aspergillus niger already deposited in databases.In the present project, we intend to use tools of Molecular Biology and Biochemistry to perform the heterologous expression of this enzyme MAO, Iminoredutases, and other enzymes of interest during the project, for the enantioselective dimerization of small molecules and especially in heterocyclic systems. Therefore, we aimed at the cloning, expression, purification and characterization of the MAO and Iminorubutase enzymes of Marasmius sp., Through the heterologous expression in E. coli, and to enable our laboratory to express several enzymes of interest and application in "green chemistry". (AU)

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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
DIAS, FABIO L.; ASSUMPCAO, MARCELO; PEIXOTO, PEDRO S.; BIANCHI, MARCELO B.; COLLACO, BRUNO; CALHAU, JACKSON. Using Seismic Noise Levels to Monitor Social Isolation: An Example From Rio de Janeiro, Brazil. Geophysical Research Letters, v. 47, n. 16, . (16/18445-7, 17/00159-0)
ASSUMPCAO, MARCELO; CARVALHO, JURACI M.; DIAS, FABIO L.; DROUET, STEPHANE; BARBOSA, JOSE ROBERTO; DE BIANCHI, MARCELO BELENTANI; COLLACO, BRUNO. Magnitude relations between the teleseismic mb, the regional mR and Mw for intraplate earthquakes in Brazil. Journal of South American Earth Sciences, v. 120, p. 5-pg., . (13/24215-6, 17/00159-0)