Enzyme stabilization by glutaraldehyde crosslinking of adsorbed proteins on aminated supports

López‐Gallego, Fernando; Betancor, Lorena; Mateo, César; Hidalgo, Aurélio; Alonso-Morales, Noelia; Dellamora-Ortiz, Gisela Maria; Guisán, José M.; Fernández‐Lafuente, Roberto

doi:10.1016/j.jbiotec.2005.05.021

Cited by 275 publications

(162 citation statements)

References 22 publications

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“…Following immobilization of RgDAAO using glutaraldehyde vapors, a stable enzyme−PPD matrix is formed. 38,39 The immobilized enzyme was yellow in color, meaning it was in its holoenzyme form. The full biosensor assembly is shown in Figure 2E.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Disk-Shaped Amperometric Enzymatic Biosensor for in Vivo Detection of d-serine

et al. 2014

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At the synapse, D-serine is an endogenous coagonist for the N-methyl-D-aspartate receptor (NMDAR). It plays an important role in synaptic transmission and plasticity and has also been linked to several pathological diseases such as schizophrenia and Huntington's. The quantification of local changes in D-serine concentration is essential to further understanding these processes. We report herein the development of a disk-shaped amperometric enzymatic biosensor for detection of D-serine based on a 25 μm diameter platinum disk microelectrode with an electrodeposited poly-m-phenylenediamine (PPD) layer and an R. gracilis D-amino acid oxidase (RgDAAO) layer. The disk-shaped D-serine biosensor is 1−5 orders of magnitude smaller than previously reported probes and exhibits a sensitivity of 276 μA cm −2 mM −1 with an in vitro detection limit of 0.6 μM. We demonstrate its usefulness for in vivo applications by measuring the release of endogenous D-serine in the brain of Xenopus laevis tadpoles.

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Section: ■ Results and Discussionmentioning

confidence: 99%

Disk-Shaped Amperometric Enzymatic Biosensor for in Vivo Detection of d-serine

et al. 2014

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“…In fact, some studies suggest that GAX impairs proper enzyme conformation by cross-linking vital surface residues, resulting in decreased enzymatic activity and limited functionality. 24 The following subsection details how GAX alters GOx structure in the absence and presence of H 2 O 2 and LMWM.…”

Section: Previous Internal Strategy: Glutaraldehyde Cross-linking Of mentioning

confidence: 99%

“…42,43 With nonactivated supports, primary amino groups as well as other amino groups on the enzyme's surface react with the support layer, leading to greater conformational changes and lower stability. 24 The deleterious effects of GAX on GOx also derive from side reactions of H 2 O 2 with glutaraldehyde to produce epoxides. Peracchia 44 demonstrated the production of epoxides from H 2 O 2 and glutaraldehyde using nuclear magnetic resonance spectroscopy.…”

Section: Degradation Of Glutaraldehyde Cross-linked Glucose Oxidasementioning

confidence: 99%

Common Causes of Glucose Oxidase Instability in In Vivo Biosensing: A Brief Review

Harris

Reyes

López

2013

J Diabetes Sci Technol

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Abbreviations: (CBD) chitin-binding domain, (ELP) elastin-like polypeptide, (GAX) glutaraldehyde cross-linking, (GOx) AbstractClinical management of diabetes must overcome the challenge of in vivo glucose sensors exhibiting lifetimes of only a few days. Limited sensor life originates from compromised enzyme stability of the sensing enzyme. Sensing enzymes degrade in the presence of low molecular weight materials (LMWM) and hydrogen peroxide in vivo. Sensing enzymes could be made to withstand these degradative effects by (1) stabilizing the microenvironment surrounding the sensing enzyme or (2) improving the structural stability of the sensing enzyme genetically. We review the degradative effect of LMWM and hydrogen peroxide on the sensing enzyme glucose oxidase (GOx). In addition, we examine advances in stabilizing GOx against degradation using hybrid silica gels and genetic engineering of GOx. We conclude molecularly engineered GOx combined with silica-based encapsulation provides an avenue for designing long-term in vivo sensor systems.

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“…Glutaraldehyde activation significantly reduced the ability of these enzymes to desorb from the supports due to their high ionic strengths, thereby suggesting that glutaraldehyde promoted strong support-protein reaction. This approach provided a simple strategy for obtaining excellent enzyme immobilization rate and desired stability for various biotechnological applications 7,8 . Moreover, glutaraldehyde was also exploited for preparing crosslinked enzyme aggregates (CLEAs) mainly in case of enzymes that have low density of surface reactive groups and therefore may pose problem to obtain a final solid catalyst 9,10 .…”

Section: Fig 1: Chemical Properties Of Glutaraldehydementioning

confidence: 99%

Role of Glutaraldehyde in Imparting Stability to Immobilized β-Galactosidase Systems

Satar

Jafri

Rasool

et al. 2018

Braz. arch. biol. technol.

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This review article highlights the role of glutaraldehyde as a matrix activator/stabilizer in imparting higher operational and thermal stability to β-galactosidase (βG) for biotechnological applications. Glutaraldehyde has been used extensively as a crosslinking agent as well as for functionalization of matrices to immobilize β-galactosidase. Immobilized β-galactosidase systems (IβGS) obtained as a result of glutaraldehyde treatment has been employed to hydrolyze whey and milk lactose in batch reactors, continuous packed-bed and fluidized bed reactors under various operational conditions. Moreover, these IβGS have also been utilized for the production of galactooligosaccharides in food, dairy and fermentation industries. It was observed that glutaraldehyde provided

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Enzyme stabilization by glutaraldehyde crosslinking of adsorbed proteins on aminated supports

Cited by 275 publications

References 22 publications

Disk-Shaped Amperometric Enzymatic Biosensor for in Vivo Detection of d-serine

Disk-Shaped Amperometric Enzymatic Biosensor for in Vivo Detection of d-serine

Common Causes of Glucose Oxidase Instability in In Vivo Biosensing: A Brief Review

Role of Glutaraldehyde in Imparting Stability to Immobilized β-Galactosidase Systems

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