journal article·2009-01

Tuning Surface Morphology of Inorganic Supports for Adsorptive Immobilization of Enzymatic Active Substances

G. A. Kovalenko, L. V. Perminova, T. V. Chuenko, N. A. Rudina

Composite Interfaces· Volume 16· Issue 4-6
Publisher page

Abstract

A comprehensive study of composite carbon–mineral supports was performed to determine specific features of the adsorptive immobilization for such enzymes as glucoamylase and invertase. The catalytic properties (activity and stability) of immobilized enzymes were found to depend significantly on the morphology of the carbon layer synthesized on the support surface. After tuning the surface morphology towards immobilizing enzymes, a layer of catalytic filamentous carbon (CFC) was found to ensure the highest stability and activity of the prepared biocatalysts due to its mesoporous structure and optimal hydrophilic–hydrophobic balance. The supports used for immobilization of enzymes can be arranged in the following order of observed enzymatic activity and stability: supports coated by graphite-like carbon layer ≈ non-carbonized supports << CFC-coated supports.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Enzyme Catalysis and Immobilization · Electrochemical sensors and biosensors · Enzyme function and inhibition

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

a Institute of Catalysis, 630090 Novosibirsk, Russia, Novosibirsk State University, 630090 Novosibirsk, Russia;, Email: galina@catalysis.ru

b Institute of Catalysis, 630090 Novosibirsk, Russia

c Institute of Catalysis, 630090 Novosibirsk, Russia

d Institute of Catalysis, 630090 Novosibirsk, Russia

References (15)

Show source-provided references
1. 10.1002/bit.26021041310.1002/bit.260210413 ↗
2. 10.1002/(SICI)1097-4628(19990404)72:1<69::AID-APP7>3.0.CO;2-L10.1002/(SICI)1097-4628(19990404)72:1<69::AID-APP7>3.0.CO;2-L ↗
3. 10.1016/S0141-0229(98)00048-910.1016/S0141-0229(98)00048-9 ↗
4. 10.1016/S0141-0229(99)00129-510.1016/S0141-0229(99)00129-5 ↗
5. Reily P. J. · Appl. Biochem. Bioengng · 1979 · 2 · 185
6. 10.1007/BF0292214710.1007/BF02922147 ↗
7. 10.1016/0141-0229(93)90142-O10.1016/0141-0229(93)90142-O ↗
8. 10.1016/S0032-9592(00)00269-710.1016/S0032-9592(00)00269-7 ↗
9. 10.1023/A:100887712666410.1023/A:1008877126664 ↗
10. 10.1016/S1381-5148(00)00036-510.1016/S1381-5148(00)00036-5 ↗
11. 10.1016/j.ces.2004.07.04710.1016/j.ces.2004.07.047 ↗
12. 10.1016/j.cattod.2005.06.05610.1016/j.cattod.2005.06.056 ↗
13. 10.1016/S1381-1169(01)00479-410.1016/S1381-1169(01)00479-4 ↗
14. 10.1134/S002315840706007910.1134/S0023158407060079 ↗
15. 10.1134/S002315840705021710.1134/S0023158407050217 ↗