From Structure to Catalysis: Recent Developments in the Biotechnological Applications of Lipases
Author(s) -
Cristiane Dinis Anobom,
Anderson S. Pinheiro,
Galdino Andrade,
Érika C.G. Aguieiras,
Guilherme C. de Andrade,
Marcelo V. Moura,
Rodrigo Volcan Almeida,
Denise Maria Guimarães Freire
Publication year - 2014
Publication title -
biomed research international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 126
eISSN - 2314-6141
pISSN - 2314-6133
DOI - 10.1155/2014/684506
Subject(s) - biochemical engineering , bioprocess , rational design , biocatalysis , protein engineering , computer science , microbiology and biotechnology , chemistry , enzyme , organic chemistry , biology , nanotechnology , catalysis , materials science , engineering , paleontology , ionic liquid
Microbial lipases are highly appreciated as biocatalysts due to their peculiar characteristics such as the ability to utilize a wide range of substrates, high activity and stability in organic solvents, and regio- and/or enantioselectivity. These enzymes are currently being applied in a variety of biotechnological processes, including detergent preparation, cosmetics and paper production, food processing, biodiesel and biopolymer synthesis, and the biocatalytic resolution of pharmaceutical derivatives, esters, and amino acids. However, in certain segments of industry, the use of lipases is still limited by their high cost. Thus, there is a great interest in obtaining low-cost, highly active, and stable lipases that can be applied in several different industrial branches. Currently, the design of specific enzymes for each type of process has been used as an important tool to address the limitations of natural enzymes. Nowadays, it is possible to “order” a “customized” enzyme that has ideal properties for the development of the desired bioprocess. This review aims to compile recent advances in the biotechnological application of lipases focusing on various methods of enzyme improvement, such as protein engineering (directed evolution and rational design), as well as the use of structural data for rational modification of lipases in order to create higher active and selective biocatalysts.
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