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Specific Strategies for One-Step and Simultaneous Immobilization-Purification of Lipases

TLDR
The use of the techniques that permit to join immobilization and purification of lipases in a single step are discussed, including control of the immobilization conditions by interfacial activation on hydrophobic supports, the development of specific supports with affinity for lipases, and the use of bio-affinity supports including immuno- and lectin affinity.
Abstract
Lipases are the biocatalysts with outstanding prospects in industry and medicine They have proven to be useful in various hydrolytic and synthetic reactions However, there are some limitations for impure lipases that may restrict their widely uses in industrial applications Purification is sometimes vital for the characterization of the function, structure, and interactions of lipases The lipase immobilization is also an efficient strategy for increasing the enzyme activity and stability, and getting a simpler recovery Lipases are naturally produced together with many other proteins that they may occupy some surface of immobilization solid support and decrease the final activity The coupling of immobilization and purification of lipase will overcome the mentioned problems and obtain the maximum purification yields The present mini-review will discuss the use of the techniques that permit to join immobilization and purification of lipases in a single step, including control of the immobilization conditions by interfacial activation on hydrophobic supports, the development of specific supports with affinity for lipases, and the use of bio-affinity supports including immuno- and lectin affinity HIGHLIGHTS •Lipases are the biocatalysts with outstanding prospects in industry and medicine •Simultaneous immobilization-purification may enhance lipase activity and stability •Lipases have a mechanism of interfacial activation in the presence of hydrophobic interfaces •The lipase immobilization on hydrophobic supports is a much-utilized strategy •Bio-affinity is a promising approach to increase lipase final yield and activity

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Advances in enzyme immobilization using magnetic polymer microspheres

TL;DR: The magnetic polymer microspheres are novel functional polymers with wide applications in biochemical industry, cytology, and biomedical engineering in the past decades as mentioned in this paper, and they have been applied in many applications.
References
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Journal ArticleDOI

Industrial applications of microbial lipases

TL;DR: Various industrial applications of microbial lipases in the detergent, food, flavour industry, biocatalytic resolution of pharmaceuticals, esters and amino acid derivatives, making of fine chemicals, agrochemicals, use as biosensor, bioremediation and cosmetics and perfumery are described.
Journal ArticleDOI

Potential of Different Enzyme Immobilization Strategies to Improve Enzyme Performance

TL;DR: The advantages and disadvantages of the different existing immobilization strategies to solve the different aforementioned enzyme limitations are given and some advice to select the optimal strategy for each particular enzyme and process is given.
Journal ArticleDOI

‘Interfacial activation’ of lipases: facts and artifacts

TL;DR: Lipases can be pragmatically redefined as carboxyl-esterases acting on long-chain acylglycerols: they are simply fat-splitting ‘ferments'.
Journal ArticleDOI

Strategies for the one-step immobilization–purification of enzymes as industrial biocatalysts

TL;DR: The development of tailor-made heterofunctional supports as a tool to immobilize-stabilize-purify some proteins will be discussed in deep, using low concentration of adsorbent groups and a dense layer of groups able to give an intense multipoint covalent attachment.
Journal ArticleDOI

Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase.

TL;DR: The crystal structure of an extracellular triglyceride lipase inhibited irreversibly by diethyl p-nitrophenyl phosphate (E600) was solved by X-ray crystallographic methods and refined to a resolution of 2.65 A.
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