Journal ArticleDOI
Strategies for enzyme stabilization by intramolecular crosslinking with bifunctional reagents
Reads0
Chats0
TLDR
In this article, a strategy to obtain intramolecular crosslinking is discussed, which consisted of three consecutive steps to direct the reaction to the formation of intramolescular crosslinks: (a) enzyme are partially modified with the bifunctional reagent in a very controlled fashion; (b) the excess of reagent is removed; and (c) the modified enzyme is incubated long-term to allow a crosslink reaction without the competition of additional single point modifications.About:
This article is published in Enzyme and Microbial Technology.The article was published on 1995-06-01. It has received 147 citations till now. The article focuses on the topics: Reagent & Immobilized enzyme.read more
Citations
More filters
Journal ArticleDOI
Enzyme stability and stabilization—Aqueous and non-aqueous environment
TL;DR: An overview of the denaturation mechanisms in aqueous and non-aqueous environment is given in this article, and various methods of enzyme stabilization with respect to their use in the aqueously and nonaqueous environments have been given.
Journal ArticleDOI
Glutaraldehyde in bio-catalysts design: a useful crosslinker and a versatile tool in enzyme immobilization
Oveimar Barbosa,Claudia Ortiz,Ángel Berenguer-Murcia,Rodrigo Torres,Rafael C. Rodrigues,Roberto Fernandez-Lafuente +5 more
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
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.
Journal ArticleDOI
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).
Journal ArticleDOI
A single step purification, immobilization, and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports
Agatha Bastida,Pilar Sabuquillo,Pilar Armisén,Roberto Fernandez-Lafuente,Joan Huguet,Jose M. Guisan +5 more
TL;DR: These results suggest that lipases recognize these "well-defined" hydrophobic supports as solid interfaces and they become adsorbed through the external areas of the largeHydrophobic active centers of their "open and hyperactivated structure", which becomes a very promising immobilization method with general application for most lipases.
References
More filters
Journal ArticleDOI
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.
Book ChapterDOI
Stabilization of enzymes against thermal inactivation.
TL;DR: Developments in protein chemistry and the understanding of thermophily, along with sensible analyses of enzyme thermoinactivation and use of common sense will undoubtedly lead to many new approaches to stabilization of enzymes at high temperatures.
Book ChapterDOI
[56] Carbodiimide modification of proteins.
K.L. Carraway,D.E. Koshland +1 more
TL;DR: A carbodiimide-nucleophile procedure for modifying carboxyl groups in proteins can be utilized under mild conditions for the quantitative determination of all carboxy groups or for the modification of selected residues in activity studies.
Book
Protein function : a practical approach
TL;DR: Minizing protein in activation ligand-protein binding affinities ligand blotting affinity labelling cross-linking of protein subunits and ligands by the introduction of disulphide bonds determining the roles of subunits in protein function analysis of sequence-specific DNA-binding proteins identification and purification.
Journal ArticleDOI
The principles of enzyme stabilization I. Increase in thermostability of enzymes covalently bound to a complementary surface of a polymer support in a multipoint fashion
TL;DR: This technique allows preparation of both highly stable water-insoluble enzymes (on formation of gel cross-linked with N,N′-methylene bisacrylamide) and soluble stabilized enzymes (if polymerization is performed without other than the enzyme cross-linking agents).