Inherent non-linearities in immobilized enzyme assays and possibilities for selectivity in enzyme immobilization

Çörüşlü, Engin; Pekin, B.

doi:10.1007/bf01141128

Biotechnol Lett

1983

DOI: 10.1007/bf01141128

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Inherent non-linearities in immobilized enzyme assays and possibilities for selectivity in enzyme immobilization

Engin Çörüşlü

B. Pekin

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1984

1991

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Cited by 4 publications

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Silica carriers for immobilization of thermostable α‐amylase

Добрева

Иванова

1991

Acta Biotechnologica

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The possibilities for immobilization of thermostable a-amylase from Baci2lus lichenijormis 44MBS2 on silica carriers activated b y different methods have been studied. Immobilization on Ti(1V)-activated GPG, Chromosorb P, quartz powder and pumice stone was sufficiently effective.The preparation immobilized on CPG showed a shift in p H end temperature-profiles of enzyme action. They were found to be changed from p H 6,O-6,5 to p H 8,5 end from 90°C to SOOC, respectively, when compared to these parameters of the soluble enzyme. Immobilization leads t o enhancement of thermostability. Possibilities for batchwise use of the immobilized preparation were established.

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Silica carriers for immobilization of thermostable α‐amylase

Добрева

Иванова

1991

Acta Biotechnologica

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Immobilization of enzymes in porous supports: Effects of support–enzyme solution contacting

Dennis

Clark

Bailey

et al. 1984

Biotech & Bioengineering

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Proteins have been immobilized in porous support particles held in a fixed-bed reactor through which protein solution is continuously circulated. Changing the recirculation flow rate alters the observed immobilization kinetics and the maximum enzyme loading which can be achieved for glucose oxidase and glucoamylase on carbodiimide-treated activated carbon and for glucoamylase immobilized on CNBr-Sepharose 4B. Direct microscopic examination of FITC-labelled protein in sectioned Sepharose particles and indirect activity-loading studies with activated carbon-enzyme conjugates all indicate that immobilized enzyme is increasingly localized near the outer surface of the support particles at larger recirculation flow rates. Restricted diffusion of enzymes may be implicated in this phenomenon. These contacting effects may be significant considerations in the scaleup of processes for protein impregnation in porous supports, since apparent activity and stability of the final preparation depend on internal protein distribution.

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Influence of the Reactant Concentrations on the Binding Mode of α‐Amylase

Çörüşlü

Pekin

1984

Starch Stärke

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Carboxymethylcellulose activated to varying extents by cyanogen bromide was used in insolubilizing Bacillus subtilis α‐amylase. The retention of native activities in the resulting derivatives toward soluble starch and the amounts of bound enzyme were determined. The effect of enzyme concentration in the coupling medium on the retention of activity was also investigated. The results are shown to accord with the hypothesis that the enzyme molecules tend to concentrate more on the surface of the carrier than inside the pores as the reactivities of the components in the coupling reaction are increased.

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Inherent non-linearities in immobilized enzyme assays and possibilities for selectivity in enzyme immobilization

Cited by 4 publications

References 8 publications

Silica carriers for immobilization of thermostable α‐amylase

Silica carriers for immobilization of thermostable α‐amylase

Immobilization of enzymes in porous supports: Effects of support–enzyme solution contacting

Influence of the Reactant Concentrations on the Binding Mode of α‐Amylase

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