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GLUCOSE-OXIDASE - AN IDEAL ENZYME
CRANFIELD INST TECHNOL,CTR BIOTECHNOL,CRANFIELD MK43 0AL,BEDS,ENGLAND; QUEEN ELIZABETH MED CTR,WOLFSON RES LABS,BIRMINGHAM B15 2TH,W MIDLANDS,ENGLAND; .
Cranfield University, UK.ORCID iD: 0000-0002-1815-9699
1992 (English)In: Biosensors & bioelectronics, ISSN 0956-5663, E-ISSN 1873-4235, Vol. 7, no 3, 165-185 p.Article, review/survey (Refereed) Published
Abstract [en]

The properties of glucose oxidase (GOD) are described in relation to the widespread use of this enzyme in biosensors, The shortcomings of other enzymes that oxidize glucose are indicated. Isolation of and early work on the enzyme are briefly reviewed. The sources and the physical characteristics of the enzyme are listed. The structure of GOD and how it relates to the immobilization and stability of the enzyme is described along with other factors that influence stability. The role of flavin adenine dinucleotide and attempts to use it in immobilization of the enzyme are described. Inhibitors of the enzyme are listed, and substrates of the enzyme and the reaction mechanism are considered in detail. The role of electron acceptors in amperometric biosensors is described, and alternatives to their use are highlighted. Other uses of the enzyme are described and the properties of the enzyme are summarized with reference to a commercially successful biosensor.

Place, publisher, year, edition, pages
Elsevier Science B.V., Amsterdam. , 1992. Vol. 7, no 3, 165-185 p.
Keyword [en]
GLUCOSE OXIDASE; DISCOVERY; SOURCES; PHYSICAL PROPERTIES; STRUCTURE; STABILITY; INHIBITORS; FAD; SUBSTRATES; REACTION MECHANISM; BIOSENSOR; ENZYME ELECTRODE; GLUCOSE SENSOR; ELECTROCHEMICAL MEDIATORS
National Category
Engineering and Technology
Identifiers
URN: urn:nbn:se:liu:diva-65301ISI: A1992HL77100003OAI: oai:DiVA.org:liu-65301DiVA: diva2:394932
Available from: 2011-02-04 Created: 2011-02-04 Last updated: 2017-12-11

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TURNER, APF

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