Cross-linking of α-chymotrypsin and other proteins by reaction with glutaraldehyde

Jansen, Eugene F.; Tomimatsu, Yoshio; Olson, Alfred C.

doi:10.1016/0003-9861(71)90492-9

Cited by 54 publications

(18 citation statements)

References 19 publications

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“…Jansen et al [36] showed that the optimum pH for GA insolubilization varies from proteins to proteins. Specially, the pH for the most rapid insolubilization of BSA was found to be nearly the same as its isoelectricpoint (pI; pH 4.7).…”

Section: Resultsmentioning

confidence: 99%

pH-responsive protein microcapsules fabricated via glutaraldehyde mediated covalent layer-by-layer assembly

2008

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Bovine serum albumin (BSA) hollow microcapsules were fabricated through glutaraldehyde (GA) mediated covalent layer-by-layer assembly. The GA crosslinking of the adsorbed BSA on the colloidal particles enabled their surfaces to be covered by reactive aldehyde groups, which reacted with BSA molecules to result in another covalently linked layer. Repeating of this cycle could then yield particles coated with BSA multilayers. Hollow microcapsules well dispersed in water were obtained after core removal. The good integrity and morphology of the BSA capsules were confirmed and characterized by confocal laser scanning microscopy, scanning electron microscopy and scanning force microscopy. The obtained BSA microcapsules possess reversible pH response, i.e., the capsules are permeable to macromolecules below pH 4 or above pH 10, while impermeable in between. The mechanisms of permeability transition were discussed. Using this property, dextran, with a molecular weight of~155 kDa, was successfully loaded.

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Section: Resultsmentioning

confidence: 99%

pH-responsive protein microcapsules fabricated via glutaraldehyde mediated covalent layer-by-layer assembly

2008

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“…43 The acid azide reaction involves the epsilon-amino groups of lysine to form an amide. 84 Glutaraldehyde was used to insolubilize enzymes and proteins without supporting materials by Avrameas, 85 Jansen and Olson, 86 Avrameas and Guibert, 87 and Jansen et al 88 Since the reaction is simple, gentle, and inexpensive, many reports for immobilization with glutaraldehyde have been published.•"• 43 -8 '" An additional advantage of using the glutaraldehyde method is that there are no toxic substances produced. Glutaraldehyde cross-linked collagen used in the manufacture of sausage casing has been applied for GRAS (generally recognized as safe) status as direct human food ingredient."…”

Section: A Immobilized Enzymesmentioning

confidence: 99%

“…Amino groups of enzymes and the inside surface of a nylon tube were cross-linked with glutaraldehyde. 88 -' 08 " 110 Goldstein et al" 1 immobilized trypsin on polyisonitrile nylon through either its amino or carboxyl groups depending on buffers. Alpha-galactosidase immobilized on nylon micro fibrils was utilized to hydrolyze the oligosaccharides.…”

Section: A Immobilized Enzymesmentioning

confidence: 99%

Modification of plant proteins by immobilized proteases

Lee

Lopez

1984

C R C Critical Reviews in Food Science and Nutrition

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A potential application of plant proteins could be a replacement of animal proteins now in use in the food industry on the basis of certain specific functional properties plant proteins have. Modification of the chemical structure of selected plant proteins is needed to replace more expensive animal proteins as food ingredients that have specific functional characteristics. Structure modification may be achieved by physical, chemical, or microbiological methods, or by a combination of these. Immobilized enzyme techniques offer significant advantages for protein modification. Knowledge of the molecular properties of plant proteins is essential to understand the basis of protein functionality, to modify proteins so that they acquire desirable functional properties, and to predict potential applications of modified plant proteins. This paper reviews all the above mentioned aspects of plant protein chemistry and potential utilization.

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“…The hemagglutinating activity was assayed with 2% saline suspension of 3 times washed erythrocytes, using the doubling dilution procedure with a lectin solution. The protein concentration was found by measuring the A2so or by the method in [ 10]. The hemagglutination titer was interpreted visually after 1 h and expressed as the higher dilution showing detectable agglutination.…”

Section: Stroma Preparationmentioning

confidence: 99%

“…After freezedrying, the stroma was polymerized with glutaraldehyde in order to preserve the integrity of its protein composition. This was done following the technique in [9,10] ; 52 mg freeze-dried stroma in 23 ml PBS were mixed with 2.5 ml 25% glutaraldehyde solution adjusting to pH 7.2 with 2 M KOH solution. After 16 h incubation at 20°C, the polymerized material was extensively washed with PBS and incubated overnight with 25 ml 1 M glycine in PBS in order to neutralize the free-reactive glutaraldehyde groups on the stroma.…”

Section: Stroma Preparationmentioning

confidence: 99%