Inactivation of Enzymes by Inert Gas Bubbling: <i>A Kinetic Study</i>

Caussette, Mylène; Gaunand, Alain; Planche, Henri; Monsan, Pierre; Lindet, Brigitte

doi:10.1111/j.1749-6632.1998.tb10311.x

Cited by 7 publications

(13 citation statements)

References 5 publications

(4 reference statements)

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“…Deactivation of FDH at Gas-Liquid Interfaces. The linear dependence on interfacial area of the FDH inactivation found in this work in a bubble column has also been observed with lysozyme at nitrogen-buffer (15)(16)(17), air-liquid, and hydrophobic (PTFE) solidliquid interfaces (18), as well as for lipase but not for pectin methylesterase (15). Likewise, correlations between deactivation rate or rate constant and interfacial area have also been observed for various enzymes (R-and δ-chymotrypsin, papain, trypsin, urease and RNase) at aqueous-organic interfaces (13,14).…”

Section: Ion Hydration Vs Dipole Cavity Model: Deactivation Of Fdh Assupporting

confidence: 78%

“…Relative Importance of Mechanical Stress and Salt Environment for Deactivation of FDH. FDH is deactivated according to first-order kinetics with respect to time in quiescent aqueous salt solution, log([E] t /[E] 0 ) ) -k d ‚t, and with respect to total pumped volume in a gear pump, log([E] t /[E] 0 ) ) -k‚N v (16). With k d ) 0.165/ day in a 1.0 M ammonium formate solution ( Figure 2) and k ) 3.2 × 10 -3 L -1 (see above), we can assess the relative importance of each deactivating effect.…”

Section: Ion Hydration Vs Dipole Cavity Model: Deactivation Of Fdh Asmentioning

confidence: 99%

“…Biocatalytic processes can achieve space‐time yields in excess of 1 kg/(L·d) (3, 5). One essential drawback of biocatalysts, however, is their often insufficient stability even in aqueous medium as they deactivate at extremes of temperature ( T < 10 °C or T > 50−70 °C) (6, 7) or pH value (pH < 4−5 or pH > 10−11) (8, 9), under shear (10–12), or in the presence of organic solvents (13, 14) and gas or solid interfaces such as gas bubbles (15–18). At extreme conditions of temperature or pH value or in the presence of organic solvents, proteins become thermodynamically unstable and thus unfold and concomitantly lose activity.…”

Section: Introductionmentioning

confidence: 99%

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Deactivation of Formate Dehydrogenase (FDH) in Solution and at Gas‐Liquid Interfaces

Bommarius

Karau

2005

Biotechnology Progress

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Enzymes, increasingly important in the synthesis of fine chemicals and pharmaceutical intermediates, are often insufficiently stable under reacting conditions. We have investigated the stability, in homogeneous aqueous solution and at gas-liquid interfaces, of formate dehydrogenase (FDH), important for cofactor regeneration, from Candida boidinii and overexpressed in E. coli. When exposed to mechanical stress, residual activity, [E](t)/[E](0), and residual protein were found to scale proportionally with gas-liquid surface area in the bubble column, verifying a surface-driven process, and with time and total throughput in a gear pump, but did not seem to be influenced much by shear in a Couette viscometer. All FDH variants are deactivated by chaotropes but not kosmotropes: the first-order deactivation constant k(d) correlates well with the Jones-Dole coefficient B but not well with the surface tension increment deltasigma of various concentrated ammonium salt solutions. This finding might provide guidance for focusing the search for quantitative theories of Hofmeister effects.

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Section: Ion Hydration Vs Dipole Cavity Model: Deactivation Of Fdh Assupporting

confidence: 78%

Section: Ion Hydration Vs Dipole Cavity Model: Deactivation Of Fdh Asmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Deactivation of Formate Dehydrogenase (FDH) in Solution and at Gas‐Liquid Interfaces

Bommarius

Karau

2005

Biotechnology Progress

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“…Mesoporous materials have attracted much attention due to their porous structure, which may permit full dispersal of enzyme molecules without the possibility of interacting with any external interface. Moreover, the immobilized enzyme molecules will not be in contact with any external hydrophobic interface [218,219] and cannot inactivate the enzymes immobilized on a porous solid [188]. In the presence of an organic solvent, the immobilized enzymes may be in contact with molecules that are soluble in the aqueous phase, but not with the molecules in the organic phase.…”

Section: Immobilization To Upgrade Industrial Enzymesmentioning

confidence: 99%

From Protein Engineering to Immobilization: Promising Strategies for the Upgrade of Industrial Enzymes

Singh

Tiwari

Singh

et al. 2013

IJMS

388

195

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Enzymes found in nature have been exploited in industry due to their inherent catalytic properties in complex chemical processes under mild experimental and environmental conditions. The desired industrial goal is often difficult to achieve using the native form of the enzyme. Recent developments in protein engineering have revolutionized the development of commercially available enzymes into better industrial catalysts. Protein engineering aims at modifying the sequence of a protein, and hence its structure, to create enzymes with improved functional properties such as stability, specific activity, inhibition by reaction products, and selectivity towards non-natural substrates. Soluble enzymes are often immobilized onto solid insoluble supports to be reused in continuous processes and to facilitate the economical recovery of the enzyme after the reaction without any significant loss to its biochemical properties. Immobilization confers considerable stability towards temperature variations and organic solvents. Multipoint and multisubunit covalent attachments of enzymes on appropriately functionalized supports via linkers provide rigidity to the immobilized enzyme structure, ultimately resulting in improved enzyme stability. Protein engineering and immobilization techniques are sequential and compatible approaches for the improvement of enzyme properties. The present review highlights and summarizes various studies that have aimed to improve the biochemical properties of industrially significant enzymes.

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“…Four studies have concerned lysozyme. In the first two (Caussette et al 1998(Caussette et al , 1999, bubbling N 2 through a lysozyme solution strongly enhanced inactivation that otherwise depended on pH and temperature. Inactivation in a stirred reactor was a first order process that depended on the agitator power and the area of the various interfaces, including the gas-liquid interface (Colombie et al 2001).…”

Section: Gas-liquid Interfacesmentioning

confidence: 99%

Effects of shear on proteins in solution

2010

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The effects of "shear" on proteins in solution are described and discussed. Research on this topic covers many decades, beginning with investigations of possible denaturation of enzymes during processing, whilst more recent concerns are how the quality of therapeutic proteins might be affected by shear or shear related effects.The paradigm that emerges from most studies is that shear in the fluid mechanical sense is unlikely by itself to damage most proteins and that interfacial phenomena are critically important. In particular, moving gas-liquid interfaces can be very deleterious. Aggregation of therapeutic proteins on nanoparticles shed from solid surfaces is a recent concern because of potential consequences on patient safety. It is clear that labeling such damage as "shear" is a mistake as this inhibits clear investigations of, and thinking about, the true causes of damage to proteins in solution during processing.

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Inactivation of Enzymes by Inert Gas Bubbling: A Kinetic Study

Cited by 7 publications

References 5 publications

Deactivation of Formate Dehydrogenase (FDH) in Solution and at Gas‐Liquid Interfaces

Deactivation of Formate Dehydrogenase (FDH) in Solution and at Gas‐Liquid Interfaces

From Protein Engineering to Immobilization: Promising Strategies for the Upgrade of Industrial Enzymes

Effects of shear on proteins in solution

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