Alteration of lipase properties by protein engineering methods

Bornscheuer, Uwe T.

doi:10.1051/ocl.2008.0192

Cited by 20 publications

(14 citation statements)

References 40 publications

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“…Genetic engineering nowadays represents the most efficient approach to generate a “tailor-made” enzyme for a given application. Two main strategies have been developed to design proteins that work better or under unusual conditions: rational design and directed evolution [ 12 , 158 ].…”

Section: Heterologous Expressionmentioning

confidence: 99%

“…For instance, heterologous expression systems are increasingly being used to overproduce recombinant lipases and phospholipases, thus overcoming the constraints related to the production of native enzymes [ 10 ]. Moreover, the application of protein engineering has enabled scientists to rapidly tailor the properties of biocatalysts, thus generating new lipase and phospholipase variants that have catalytic and stability properties that better fit the needs of industrial processes [ 11 , 12 , 13 ].…”

Section: Introductionmentioning

confidence: 99%

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

Borrelli

Trono

2015

IJMS

278

182

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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.

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Section: Heterologous Expressionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Borrelli

Trono

2015

IJMS

278

182

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“…There is also the option to utilize solid residues, from rapeseed after biodiesel production to obtain second generation biofuels to establish integrated process conditions [139]. The application of biotechnology in the synthesis of biodiesel should cover the improvement of microdiesel synthesis and medium engineering as well as the application of protein engineering, directed evolution, and metagenome resources for further improvement of process efficiency [99,105]. Further progress and standardization of methods of biodiesel analysis is also expected [140][141][142][143].…”

Section: Discussionmentioning

confidence: 99%

“…There are traditional, conventional methods for improving lipase stability by immobilization including using nanoparticles (Table 5) and the application of reaction medium engineering methods [97,98], but current molecular biology methods represent the most important methodology available to obtain tailor-made enzymes [99,100]. Two approaches are possible for obtaining better biocatalysts: rational protein design and directed evolution methods [101][102][103].…”

Section: A) Conversionmentioning

confidence: 99%

The application of biotechnological methods for the synthesis of biodiesel

Adamczak

Bornscheuer

Bednarski

2009

Euro J Lipid Sci & Tech

Self Cite

113

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Synthesis of biodiesel is performed mainly by chemical catalysis, but can also be performed by enzymatic or microbial methods, and these might play an important role in future substitution of petroleum-based diesel. To discover sustainable, economically attractive biotechnological processes for biodiesel synthesis, close cooperation between different disciplines is needed. Currently, lipases are the enzymes of choice for the synthesis of fatty acid esters (FAE) from fats and oils, yielding biodiesel with the methyl esters (FAME) as the most important product. More recently, the direct production of FAE using engineered whole cell microorganism has also been described (MicroDiesel). Current enzymatic processes are still hampered by the high costs of the biocatalyst, but significant progress has recently been made leading to the first industrial enzymatic biodiesel production. Enzymatic biodiesel production is mostly attractive because of the starting materials (waste frying oils, oils with high water content, etc.), for which conventional chemical interesterification can hardly be applied.

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“…metagenome screening approaches for the identification of new catalysts or genetic engineering for alteration or optimisation of the catalyst properties [14][15][16][17]. An overview of successful examples of lipase optimisation has recently been compiled [18]. The stability and substrate specificity have been optimised using different protein engineering methods.…”

Section: Biocatalysts For Lipid Transformationsmentioning

confidence: 99%

Lipid biotechnology: Industrially relevant production processes

Schörken¹,

Kempers²

2009

Euro J Lipid Sci & Tech

152

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The biotechnological transformation of vegetable oils and animal fats has been successfully developed up to an industrial scale in recent years. However, biotechnology is still a niche technology in the oleochemical industry, which classically relies on chemical transformation processes. Nevertheless, the impact of biotechnology is rising, with an increasing number of biotech-based products, especially in the area of lipidderived specialties, entering the market. In this review we give a summary of the industrially relevant processes in the field of lipid biotechnology.

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Alteration of lipase properties by protein engineering methods

Cited by 20 publications

References 40 publications

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

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

The application of biotechnological methods for the synthesis of biodiesel

Lipid biotechnology: Industrially relevant production processes

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