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Open AccessJournal ArticleDOI

Heterofunctional supports in enzyme immobilization: from traditional immobilization protocols to opportunities in tuning enzyme properties.

TLDR
This Review will discuss the suitable properties of the groups able to give the covalent attachment, and the groups unable to produce the first enzyme adsorption on the support, as well as the likely pathways for the evolution.
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This article is published in Biomacromolecules.The article was published on 2013-07-16 and is currently open access. It has received 418 citations till now.

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Glutaraldehyde in bio-catalysts design: a useful crosslinker and a versatile tool in enzyme immobilization

TL;DR: Glutaraldehyde, an apparently old fashioned reactive, remains the most widely used and with broadest application possibilities among the compounds used for the design of biocatalyst.
Journal ArticleDOI

Enzyme immobilization by adsorption: a review

TL;DR: In this paper, a comparative analysis of the literature reports on the recent trends in the enzyme immobilization by adsorption is presented, where both carriers, carrier modifiers and procedures developed for effective adaption of the enzymes are discussed.
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

Importance of the Support Properties for Immobilization or Purification of Enzymes

TL;DR: This review will focus its attention on the requirements of a support surface to produce the desired objectives, the ideal physical properties of the matrix, the properties ofThe introduced reactive groups, the best surface activation degree to reach the desired objective, and the Properties of the reactive groups will be discussed.
Journal ArticleDOI

Immobilization of lipases on hydrophobic supports involves the open form of the enzyme

TL;DR: The results confirm that the lipases immobilized on octyl agarose presented their open form stabilized while the covalent preparation maintains a closing/opening equilibrium that may be modulated by altering the medium.
References
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Journal ArticleDOI

Improvement of enzyme activity, stability and selectivity via immobilization techniques

TL;DR: In all cases, enzyme engineering via immobilization techniques is perfectly compatible with other chemical or biological approaches to improve enzyme functions and the final success depend on the availability of a wide battery of immobilization protocols.
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Industrial biocatalysis today and tomorrow

TL;DR: Biocatalytic processes can now be carried out in organic solvents as well as aqueous environments, so that apolar organic compounds aswell as water-soluble compounds can be modified selectively and efficiently with enzymes and bioc atalytically active cells.
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Metal chelate affinity chromatography, a new approach to protein fractionation

TL;DR: A highly flexible method based on affinities which can be used in a more selective fashion by modern chromatographic techniques is described here.
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Enzyme immobilization: The quest for optimum performance

TL;DR: Different methods for the immobilization of enzymes are critically reviewed, with emphasis on relatively recent developments, such as the use of novel supports, e.g., mesoporous silicas, hydrogels, and smart polymers, novel entrapment methods and cross-linked enzyme aggregates (CLEAs).
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Cyanohydridoborate anion as a selective reducing agent

TL;DR: The use of modified boron hydrides as selective reducing agents for organic functional g roups has been studied extensively as discussed by the authors, with a focus on reducing a wide variety of organic functional groups with remarkable selectivity.
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