Investigation into immobilisation of lactate oxidase to improve stability

Citation
B. Lillis et al., Investigation into immobilisation of lactate oxidase to improve stability, SENS ACTU-B, 68(1-3), 2000, pp. 109-114
Citations number
15
Categorie Soggetti
Spectroscopy /Instrumentation/Analytical Sciences","Instrumentation & Measurement
Journal title
SENSORS AND ACTUATORS B-CHEMICAL
ISSN journal
09254005 → ACNP
Volume
68
Issue
1-3
Year of publication
2000
Pages
109 - 114
Database
ISI
SICI code
0925-4005(20000825)68:1-3<109:IIIOLO>2.0.ZU;2-2
Abstract
Lactate oxidase (LOx) is an unstable enzyme. In this work, a variety of imm obilisation techniques are investigated in an effort to improve the long-te rm stability of the enzyme. These include covalent linkage to two membrane types, encapsulation in a BSA gel and four different sol-gel matrices. The enzyme glucose oxidase (GOx) was also immobilised in the same sol-gel matri ces. The methods were assessed for both activity and stability of the enzym e and the mechanical rigidity of the matrix. The BSA and sol-gels both form ed physically robust enzyme layers. The enzyme retained its activity in the BSA gel for 20 days. Activity of the enzyme was much higher in the sol-gel matrices and remained stable fur at least 55 days. Sol-gel processing cond itions were also investigated. (C) 2000 Elsevier Science S.A. All lights re served.