Enzymatically active membranes: Some properties of cellophane membranes supporting cross-linked enzymes

Broun, G.; Sélégny, Éric; Avraméas, Stratis; Thomas, Daniel

doi:10.1016/0005-2744(69)90305-2

Cited by 65 publications

(5 citation statements)

References 8 publications

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“…Stabilities (thermal, chemical, and mechanical) of water-insoluble enzyme derivatives have also been described (46,76). Most notably, thermal stability of immobilized enzymes has been shown to vary from greater down to a lesser extent relative to the native enzyme.…”

Section: Application To Substances Of Biological Interestmentioning

confidence: 99%

Glutaraldehyde: Behavior in Aqueous Solution, Reaction with Proteins, and Application to Enzyme Crosslinking

et al. 2004

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Glutaraldehyde possesses unique characteristics that render it one of the most effective protein crosslinking reagents. It can be present in at least 13 different forms depending on solution conditions such as pH, concentration, temperature, etc. Substantial literature is found concerning the use of glutaraldehyde for protein immobilization, yet there is no agreement about the main reactive species that participates in the crosslinking process because monomeric and polymeric forms are in equilibrium. Glutaraldehyde may react with proteins by several means such as aldol condensation or Michael-type addition, and we show here 8 different reactions for various aqueous forms of this reagent. As a result of these discrepancies and the unique characteristics of each enzyme, crosslinking procedures using glutaraldehyde are largely developed through empirical observation. The choice of the enzyme-glutaraldehyde ratio, as well as their final concentration, is critical because insolubilization of the enzyme must result in minimal distortion of its structure in order to retain catalytic activity. The purpose of this paper is to give an overview of glutaraldehyde as a crosslinking reagent by describing its structure and chemical properties in aqueous solution in an attempt to explain its high reactivity toward proteins, particularly as applied to the production of insoluble enzymes.

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Section: Application To Substances Of Biological Interestmentioning

confidence: 99%

Glutaraldehyde: Behavior in Aqueous Solution, Reaction with Proteins, and Application to Enzyme Crosslinking

et al. 2004

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“…For a Michaelis-Menten enzyme such as glucose oxidase (33)(34)(35), the enzyme-catalyzed reaction rate can be expressed as a function of the substrate concentration, i.e., D-(1)-glucose concentration, as (36) vðtÞ ¼ v m ½Glu out ðtÞ K m 1 ½Glu out ðtÞ :…”

Section: Enzymatic Reaction Ratementioning

confidence: 99%

Modeling Leakage Kinetics from Multilamellar Vesicles for Membrane Permeability Determination: Application to Glucose

Faure

Nallet

Roux

et al. 2006

Biophysical Journal

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The glucose permeability of bilayers formed from phosphatidylcholine, Brij30, and sodium octadecyl sulfate has been determined via an enzymatic reaction. Glucose is encapsulated in either uni- or multilamellar vesicles (MLV) and its concentration in the dispersion medium is monitored by spectrophotometry analysis through the rate of glucose oxidase-catalyzed reaction of glucose oxidation. A kinetic model of leakage, taking explicitly into account one, two, or n(w)-walls (n(w) >> 1) for the vesicles and assuming an enzymatic Michaelis-Menten behavior, is proposed and used to fit the experimental data. The two-wall model was chosen to fit experimental data obtained on MLV since an average value of 1.7 bilayers was estimated for MLV by cryo-TEM imaging. A permeability value of 5.8 +/- 4.4 10(-9) cm/s was found. The proposed model is validated by the measurement of the bilayer permeability deduced from the modeling of glucose leakage from unilamellar vesicles with the same composition. In this latter case, a value of 8.3 +/- 0.7 10(-9) cm/s is found for the permeability, which is within the error bar of the value found with MLV.

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“…(1 97 1 ) concluded that thermal stability is lowered by adsorption or covalent binding of enzymes. However, improved thermal stabilities have been reported for CM-cellulose-ficin (Hornby et al, 1966;, glucose oxidase immobilized o n cellophane sheets (Broun et al, 1969), acetylcholinesterase entrapped in silastic (Pennington et al, 1968), papain coupled t o glass (Weetal, 1969), and b-galactosidase covalently linked t o a polyisocyanate polymer (Hustad et al, 1973a). Enzymes that exhibited lower heat stabilities after immobilization include invertase bound to porous glass (Weetal, 1973a) and papain bound t o neutral carriers such as leucinep-aminophenylalanine , S-MDA resins (Goldstein, 1970;Goldstein et al, 1970), p-aminobenzyl cellulose (Goldstein, 1970;Goldstein et al, 1970) and collodion (Goldman et al, 1965(Goldman et al, , 1968.…”

Section: Stabilitymentioning

confidence: 99%

SYMPOSIUM: Immobilized Enzymes in Food Systems

Olson¹,

Richardson²

1974

Journal of Food Science

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S Economics of immobilization and characteristics of immobilized enzymes and substrates which are important in treatment of foods are discussed. Methods of immobilizing enzymes and activity and stability of enzymes which may be used in food processing and analyses are controlled and limited by the properties of foods. Specific immobilized enzymes which have been used or show promise for use in food processing and analysis are described.

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Enzymatically active membranes: Some properties of cellophane membranes supporting cross-linked enzymes

Cited by 65 publications

References 8 publications

Glutaraldehyde: Behavior in Aqueous Solution, Reaction with Proteins, and Application to Enzyme Crosslinking

Glutaraldehyde: Behavior in Aqueous Solution, Reaction with Proteins, and Application to Enzyme Crosslinking

Modeling Leakage Kinetics from Multilamellar Vesicles for Membrane Permeability Determination: Application to Glucose

SYMPOSIUM: Immobilized Enzymes in Food Systems

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