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

Borrelli GM, Trono D - Int J Mol Sci (2015)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: 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. graziamaria.borrelli@entecra.it.

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.

No MeSH data available.


Related in: MedlinePlus

Reactions catalyzed by lipases. Lipases catalyze the cleavage of carboxyl ester bonds. This reaction occurs in the presence of water as substrate or product in hydrolysis and esterification, respectively, of an alcohol in alcoholysis, of an organic acid in acidolysis, of ammonia in aminolysis, and between two different esters in interesterification.
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ijms-16-20774-f001: Reactions catalyzed by lipases. Lipases catalyze the cleavage of carboxyl ester bonds. This reaction occurs in the presence of water as substrate or product in hydrolysis and esterification, respectively, of an alcohol in alcoholysis, of an organic acid in acidolysis, of ammonia in aminolysis, and between two different esters in interesterification.

Mentions: Under natural conditions, such as in the presence of excess water, lipases act at the organic–aqueous interface to catalyze the hydrolysis of carboxylate ester bonds and the release free fatty acids (FFAs) and organic alcohols (Figure 1). As the equilibrium between the forward and reverse reactions is controlled by the water activity (aw) of the reaction mixture, under limiting water conditions the reverse reaction, the esterification, can occur (Figure 1). Under low aw, different transesterification reactions can also be achieved. The term transesterification refers to the exchange of groups between an ester and an alcohol (alcoholysis), between an ester and an acid (acidolysis), between an ester and an amine (aminolysis), or between two esters (interesterification) [14] (Figure 1).


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

Borrelli GM, Trono D - Int J Mol Sci (2015)

Reactions catalyzed by lipases. Lipases catalyze the cleavage of carboxyl ester bonds. This reaction occurs in the presence of water as substrate or product in hydrolysis and esterification, respectively, of an alcohol in alcoholysis, of an organic acid in acidolysis, of ammonia in aminolysis, and between two different esters in interesterification.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4613230&req=5

ijms-16-20774-f001: Reactions catalyzed by lipases. Lipases catalyze the cleavage of carboxyl ester bonds. This reaction occurs in the presence of water as substrate or product in hydrolysis and esterification, respectively, of an alcohol in alcoholysis, of an organic acid in acidolysis, of ammonia in aminolysis, and between two different esters in interesterification.
Mentions: Under natural conditions, such as in the presence of excess water, lipases act at the organic–aqueous interface to catalyze the hydrolysis of carboxylate ester bonds and the release free fatty acids (FFAs) and organic alcohols (Figure 1). As the equilibrium between the forward and reverse reactions is controlled by the water activity (aw) of the reaction mixture, under limiting water conditions the reverse reaction, the esterification, can occur (Figure 1). Under low aw, different transesterification reactions can also be achieved. The term transesterification refers to the exchange of groups between an ester and an alcohol (alcoholysis), between an ester and an acid (acidolysis), between an ester and an amine (aminolysis), or between two esters (interesterification) [14] (Figure 1).

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: 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. graziamaria.borrelli@entecra.it.

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.

No MeSH data available.


Related in: MedlinePlus