From structure to catalysis: recent developments in the biotechnological applications of lipases.

Cristiane D Anobom,Anderson S Pinheiro,Denise M Freire,Guilherme C Andrade,Rodrigo V Almeida,Erika C G Aguieiras,Rafael A De-Andrade,Marcelo V Moura

doi:10.1155/2014/684506

Cristiane D Anobom, Anderson S Pinheiro + Show 6 more

Open Access

https://doi.org/10.1155/2014/684506

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Abstract

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.

Highlights

Lipases are enzymes that catalyze the hydrolysis of fats and oils with release of free fatty acids, diglycerides, monoglycerides, and glycerol
Lipases may act under mild conditions, are highly stable in organic solvents, show broad substrate specificity, and usually show high regioand/or stereoselectivity in catalysis
Since the BRIDGE-T lipase project (1990–1994) until today, numerous three-dimensional structures of lipases from several different organisms have been reported, shedding light onto the mechanism used by these enzymes during catalysis

Summary

Introduction

Lipases (triacylglycerol acyl hydrolases, E.C. 3.1.1.3) are enzymes that catalyze the hydrolysis of fats and oils with release of free fatty acids, diglycerides, monoglycerides, and glycerol. Lipases may act under mild conditions, are highly stable in organic solvents, show broad substrate specificity, and usually show high regioand/or stereoselectivity in catalysis. This versatility makes lipases one of the most widely used group of biocatalysts for biotechnological processes [3,4,5]. Lipases find applications in food modification, detergent formulation, cosmetic, pharmaceutical, leather, textile, and paper industries, biodiesel and biopolymer production, or pretreatment of lipid-rich wastewaters [1, 6]. These enzymes are found in many species of animals, plants, bacteria, and fungi. Microbial lipases are the most appealing ones mainly because of their applied properties, such as versatility and ease of mass production [5, 6]

Hydrolysis of Oils and Fats

Structural Features of Lipases

Findings

Tailor-Made Lipases