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Int. J. Mol. Sci. 2015, 16(9), 20774-20840; doi:10.3390/ijms160920774

Recombinant Lipases and Phospholipases and Their Use as Biocatalysts for Industrial Applications

Consiglio per la Ricerca in Agricoltura e l'Analisi dell'Economia Agraria, Centro di Ricerca per la Cerealicoltura, S.S. 673 Km 25, 200-71122 Foggia, Italy
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Academic Editor: Vladimír Křen
Received: 22 May 2015 / Revised: 17 July 2015 / Accepted: 11 August 2015 / Published: 1 September 2015
(This article belongs to the Special Issue Molecular Biocatalysis)
View Full-Text   |   Download PDF [2389 KB, uploaded 1 September 2015]   |  

Abstract

Lipases and phospholipases are interfacial enzymes that hydrolyze hydrophobic ester linkages of triacylglycerols and phospholipids, respectively. In addition to their role as esterases, these enzymes catalyze a plethora of other reactions; indeed, lipases also catalyze esterification, transesterification and interesterification reactions, and phospholipases also show acyltransferase, transacylase and transphosphatidylation activities. Thus, lipases and phospholipases represent versatile biocatalysts that are widely used in various industrial applications, such as for biodiesels, food, nutraceuticals, oil degumming and detergents; minor applications also include bioremediation, agriculture, cosmetics, leather and paper industries. These enzymes are ubiquitous in most living organisms, across animals, plants, yeasts, fungi and bacteria. For their greater availability and their ease of production, microbial lipases and phospholipases are preferred to those derived from animals and plants. Nevertheless, traditional purification strategies from microbe cultures have a number of disadvantages, which include non-reproducibility and low yields. Moreover, native microbial enzymes are not always suitable for biocatalytic processes. The development of molecular techniques for the production of recombinant heterologous proteins in a host system has overcome these constraints, as this allows high-level protein expression and production of new redesigned enzymes with improved catalytic properties. These can meet the requirements of specific industrial process better than the native enzymes. The purpose of this review is to give an overview of the structural and functional features of lipases and phospholipases, to describe the recent advances in optimization of the production of recombinant lipases and phospholipases, and to summarize the information available relating to their major applications in industrial processes. View Full-Text
Keywords: : lipases; phospholipases; biocatalysis; heterologous expression; protein engineering; industrial applications : lipases; phospholipases; biocatalysis; heterologous expression; protein engineering; industrial applications
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MDPI and ACS Style

Borrelli, G.M.; Trono, D. Recombinant Lipases and Phospholipases and Their Use as Biocatalysts for Industrial Applications. Int. J. Mol. Sci. 2015, 16, 20774-20840.

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