Covalent immobilisation of invertase onto a reactive film composed of 2-hydroxyethyl methacrylate and glycidyl methacrylate: properties and application in a continuous flow system

Bayramoğlu, Gülay; Akgöl, Sinan; Bulut, Adnan; Deni̇zli̇, Adil; Arıca, M. Yakup

doi:10.1016/s1369-703x(02)00170-5

Cited by 111 publications

(50 citation statements)

References 36 publications

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“…The free trypsin had an optimal temperature of 45 ºC, whereas the optimal temperature of the immobilized trypsin shifted to 55 ºC (which is also less favourable for biomedical applications). Upon immobilization, the covalent coupling of the protein molecule to the support significantly reduced its freedom to undergo the conformational changes that lead to denaturation (Arica et al, 1995;Bayramoglu et al, 2003). Similar results have been observed for trypsin and other proteases covalently immobilized to other supports like soap-free P(MMA-EA-AA) latex particles (Kang et al, 2005), a chitosan membrane (Krajewska et al, 1990) and a modified polysulphone membrane (Pozniak et al, 1995).…”

Section: Effect Of Ph On Activitysupporting

confidence: 58%

Cotton gauze bandage: a support for protease immobilization for use in biomedical applications

Seabra¹,

Gil²

2007

Rev. Bras. Cienc. Farm.

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Section: Effect Of Ph On Activitysupporting

confidence: 58%

Cotton gauze bandage: a support for protease immobilization for use in biomedical applications

Seabra¹,

Gil²

2007

Rev. Bras. Cienc. Farm.

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“…A large number of enzymes were successfully immobilized with very high activity yields on appropriate supports. These immobilized products were intended for use in the construction of artificial organs, biosensors, or bioreactors (Bayramoglu et al, 2003). The selection of support materials and the method of immobilization are very important for carrying out the desired enzymatic reactions.…”

Section: Resultsmentioning

confidence: 99%

Biochemical studies on immobilized fungal β-glucosidase

Ahmed

El-Shayeb

Hashem

et al. 2013

Braz. J. Chem. Eng.

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-β-Glucosidase from Aspergillus niger was immobilized on sponge by covalent binding through a spacer group (glutaraldehyde). Sponge-immobilized enzyme had the highest immobilization yield (95.67%) and retained 63.66% of the original activity exhibited by the free enzyme. The optimum pH of the immobilized enzyme remains almost the same as for the free enzyme (pH 4.0). The optimum temperature for β-glucosidase activity was increased by 10 ºC after immobilization. The activation energy (E a ) of the immobilized β-glucosidase was lower than the free enzyme (3.34 and 4.55 kcal/mol), respectively. Immobilized β-glucosidase exhibited great thermal stability and retained all the initial activity after incubation at 55 ºC for 2 h; however, the free enzyme retained 89.25% under the same condition. The calculated half-life (t ½ ) value of heat inactivation of immobilized enzyme at 60, 65 and 70 ºC was 213.62, 72.95 and 56.80 min, respectively, whereas at these temperatures the free enzyme was less stable (half-life of 200.0, 55.31 and 49.5 min, respectively). The deactivation rate constant at 65 ºC for the immobilized β-glucosidase is 9.5x10 -3 / min, which was lower than that of the free form (12.53x10 -3 / min). The immobilization process improved the pH stability of the enzyme (immobilized and free enzyme retained 69.35 and 39.86%, respectively, of their initial activity after 45 min at pH 7.5). The effect of some chemical substances on the activity of the immobilized and free β-glucosidase has been investigated. In the presence of sodium dodecyl sulfate (SDS) and p-chloromercuri benzoate (p-CMB) the immobilized enzyme retained 36.13 and 45.34%, respectively, of the initial activity, which is higher than that of free enzyme (13.71 and 1.61%, respectively). The Michaelis constant (K m ) value of the free enzyme was 40.0 mM, while the apparent K m value for the immobilized enzyme was 46.51 mM. The maximum reaction rate (v max ) of immobilized β-glucosidase was smaller than that of the free enzyme by 7.69%. Sponge-immobilized β-glucosidase was repeatedly used to hydrolyze cellobiose (5 and 8 cycles with retained activity of 67.32 and 51.04%, respectively).

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“…Soluble invertase is used in the sweet industry in the production of artificial honey. Enzyme-catalyzed hydrolysis has the advantage of colourless products compared to the coloured version obtained through acid hydrolysis (Arica, Senel, Alaeddinoglu, Patir, & Denizli, 2000;Bayramoglu, Akgol, Bulut, Denizli, & Arica, 2003). Invertase has been immobilized on a variety of support materials.…”

Section: Introductionmentioning

confidence: 99%

Enhanced pH and thermal stabilities of invertase immobilized on montmorillonite K-10

Gopinath

Sugunan

2006

Food Chemistry

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Invertase was adsorbed onto micro-porous acid-activated montmorillonite clay (K-10) by two procedures, namely adsorption and covalent binding. The immobilized enzymes were characterized by XRD, surface area measurements and 27 Al NMR. XRD measurements revealed an expansion of clay layers due to immobilization which suggests that intercalation had taken place. Surface area measurements also support this observation. 27 Al NMR showed that interaction of enzyme with tetrahedral and octahedral Al changes with the immobilization procedure. Sucrose hydrolysis was performed in a batch reactor. The immobilized enzymes showed enhanced pH and thermal stabilities. Optimum pH and temperature were found to increase upon immobilization. The effectiveness factor (g) and Michaelis constant (K m ) suggest that diffusional resistances play a major role in the reaction. The immobilized invertase could be stored in buffer of pH 5 and 6 at 5°C without any significant loss in activity for 20 days.

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Covalent immobilisation of invertase onto a reactive film composed of 2-hydroxyethyl methacrylate and glycidyl methacrylate: properties and application in a continuous flow system

Cited by 111 publications

References 36 publications

Cotton gauze bandage: a support for protease immobilization for use in biomedical applications

Cotton gauze bandage: a support for protease immobilization for use in biomedical applications

Biochemical studies on immobilized fungal β-glucosidase

Enhanced pH and thermal stabilities of invertase immobilized on montmorillonite K-10

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