Search of enzymes for use in chemical transformation of the lignin model compounds

• Grant number: 13/13501-8
• Support Opportunities: Scholarships in Brazil - Doctorate
• Start date: September 01, 2013
• End date: October 31, 2015
• Field of knowledge: Physical Sciences and Mathematics - Chemistry - Organic Chemistry
• Principal Investigator: Leandro Helgueira de Andrade
• Grantee: Wagner Cezar Cavalcanti dos Santos
• Host Institution: Instituto de Química (IQ). Universidade de São Paulo (USP). São Paulo , SP, Brazil

Abstract

Lignin, a very abundant natural polymer, is a byproduct in the manufacturing process of pulp. Due to the added value that cellulose has, lignin is not so valued. However, its application as a sustainable source has potential to produce fuel as well as phenols and carboxylic acids.Its structure, which has phenolic units, several studies involving lignin model compounds are conducted in order to obtain a method of producing phenols by a sustainable source. Thus, studies related to the fragmentation of lignin appear promising as a way to increase its commercial value. The application of routes with enzyme as catalysts can be a viable alternative, since such catalysts are biodegradable, and promote selective reactions in mild conditions.There are several papers in the literature regarding reactions with model compounds mediated by chemical catalysts, however, there are very few reports about enzyme-mediated reactions.This work is dedicated to investigate the best reaction conditions for obtaining carboxylic acids and phenols from lignin model compounds, which will be used enzymes such as alcohol dehydrogenase, Baeyer-Villiger mono-oxygenases and lipases. Subsequently, it is intended to induce the growth of micro-organisms and isolate them in order to apply in reactions with lignin model compounds. Thus the evaluation of their performance in the reactions is proposed. This can lead us to a detection of the enzymes responsible for each chemical transformation (alcohol dehydrogenases, mono-oxygenases and hydrolases).