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Co-aggregation of penicillin g acylase and polyionic polymers: an easy methodology to prepare enzyme biocatalysts stable in organic media.

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TLDR
The development and optimization of a protocol to produce a novel type of biocatalyst that combines the good properties of cross-linked enzyme aggregates (CLEAs) and hydrophilic microenvironments using penicillin acylase as a model shows that CLEA-GDPs have a highly increased stability in organic media.
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This article is published in Biomacromolecules.The article was published on 2004-03-18. It has received 119 citations till now. The article focuses on the topics: Penicillin amidase & Immobilized enzyme.

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Citations
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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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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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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.
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Immobilised enzymes: science or art?

TL;DR: Combinatorial approaches are increasingly applied in the design of robust immobilised enzymes by rational combination of fundamental immobilisation techniques or with other relevant technologies to solve specific problems that cannot be solved by one of these basic immobilised techniques.
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Stabilization of multimeric enzymes: Strategies to prevent subunit dissociation

TL;DR: In this review, different strategies to stabilize multimeric enzymes at different levels are revised and special emphasis is put on the new immobilization strategies specifically designed to involve the maximum amount of enzyme subunits in the immobilization (and thus, in the further multipoint covalent attachment).
References
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Journal ArticleDOI

Why are enzymes less active in organic solvents than in water

TL;DR: In order to exploit fully the biotechnological opportunities afforded by nonaqueous enzymology, the issue of often drastically diminished enzymatic activity in organic solvents compared with that in water must be addressed and resolved as mentioned in this paper.
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Aldehyde-agarose gels as activated supports for immobilization-stabilization of enzymes

TL;DR: Aldehyde groups, moderately separated from support surfaces, are proposed as suitable active groups for developing strategies to insolubilize-stabilize enzymes by multipoint covalent attachment to activated preexistent supports.
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Penicillin Acylase in the Industrial Production of β-Lactam Antibiotics

TL;DR: Immobilized penicillin acylase is a biocatalyst suitable for the kinetically controlled industrial synthesis of semi-synthetic antibiotics in aqueous environments.
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Cross-linked enzyme aggregates with enhanced activity: application to lipases

TL;DR: Preparations with up to ten times enhanced activity in organic medium were prepared and precipitation of the lipases from Thermomyces lanuginosus and Rhizomucor miehei afforded CLEAs with three and two times, respectively, the hydrolytic activity of the native enzymes.
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Enzymatic protecting group techniques.

TL;DR: In this article, the introduction and removal of protecting groups is one of the most important and widely carried out synthetic transformations in preparative organic chemistry, in particular in the highly selective construction of complex, polyfunctional molecules, e.g., oligonucleotides, oligosaccharides, peptides, and conjugates thereof.
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