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Journal ArticleDOI

Effect of enzyme ratio on the properties of glucose oxidase and catalase immobilized on modified perlite

Leman Tarhan, +1 more
- 01 Jan 1992 - 
- Vol. 27, Iss: 1, pp 11-15
TLDR
In this article, perlite modified by silanization and treatment with glutaraldehyde was used as a support for the co-immobilization of glucose oxidase and catalase.
About
This article is published in Process Biochemistry.The article was published on 1992-01-01. It has received 12 citations till now. The article focuses on the topics: Immobilized enzyme & Glucose oxidase.

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Citations
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Journal ArticleDOI

Glucose oxidase--an overview.

TL;DR: Various purification techniques for higher recovery of glucose oxidase are described here, and issues of enzyme kinetics, stability studies and characterization are addressed.
Journal ArticleDOI

Understanding the structure and function of catalases: clues from molecular evolution and in vitro mutagenesis.

TL;DR: This review gives an overview about the structural organisation of different evolutionary lines of all enzymes capable of efficient dismutation of hydrogen peroxide, as well as major potential applications in biotechnology and clinical medicine justify further investigations.
Journal ArticleDOI

Bentonite and sepiolite as supporting media: Immobilization of catalase

TL;DR: In this article, a function of pH, temperature and ionic strength for free and immobilized enzyme activities on bentonite and sepiolite was studied, and the results showed that the storage stabilities of immobilized catalases were higher than free catalase.
Journal ArticleDOI

Simultaneous co-immobilization of glucose oxidase and catalase in their substrates

TL;DR: Co-immobilization of GOD and CAT in the presence of their substrates highly improved the activity and reusability of both enzymes.
References
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Journal ArticleDOI

A New and Rapid Method for the Determination of Glucose by Measurement of Rate of Oxygen Consumption

TL;DR: In this article, a new glucose oxidase method employing a polarographic oxygen sensor with a circuit modified to record the rate of oxygen consumption is presented, which provides a direct measure of the glucose level in the sample; results are obtainable within 20 sec. after sample (100 µl.) addition and within 3 min after a blood sample is withdrawn from a patient.
Book ChapterDOI

[9] The kinetics of immobilized enzyme systems

TL;DR: The kinetic behavior observed when an enzyme is included within a solid matrix that is in contact with a solution, containing the substrate and, also, with the situation, in which the enzyme is attached to the interior surface of a tube, through which substrate solution is flowing.
Journal ArticleDOI

Deactivation of immobilized beef liver catalase by hydrogen peroxide.

TL;DR: A model has been developed which predicts the rate of decomposition of peroxide and inactivation of catalase in a flow reactor and first order dependence on peroxide concentration is assumed.
Journal ArticleDOI

An enzyme coimmobilized with a microorganism: The conversion of cellobiose to ethanol using β‐glucosidase and Saccharomyces cerevisiae in calcium alginate gels

TL;DR: The coimmobilized preparation was superior to a combination of separately immobilized biocatalysts, however, in this preparation, one‐half the enzyme activity was lost within a week when incubated at the operational temperature in the absence of substrate.
Journal ArticleDOI

High‐yield method for immobilization of enzymes

TL;DR: Two types of polyethylenimine‐coated glass microbeads were synthesized and used for the immobilization of glucose oxidase from Aspergillus niger and catalase and found to be superior to the immobilized activities attainable on aminopropyl‐activated glass microBeads.
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