Enzymatic activity of immobilized yeast phosphoglycerate kinase
This work reports the first evidence that recombinant yeast phosphoglycerate kinase (PGK) is still significantly active when immobilized on glass and muscovite mica. Using previous work to improve the sensitivity of the existing setup, Tapping Mode atomic force microscopy (AFM) was used in a liquid...
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| Veröffentlicht in: | Biosensors & bioelectronics 2007-05, Vol.22 (11), p.2449-2455 |
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| container_title | Biosensors & bioelectronics |
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| creator | Hurth, Cedric Tassius, Chantal Talbot, Jean-Claude Maali, Abdelhamid Moskalenko, Cendrine Minard, Philippe Aimé, Jean-Pierre Argoul, Françoise |
| description | This work reports the first evidence that recombinant yeast phosphoglycerate kinase (PGK) is still significantly active when immobilized on glass and muscovite mica. Using previous work to improve the sensitivity of the existing setup, Tapping Mode atomic force microscopy (AFM) was used in a liquid environment to determine the surface enzyme coverage of derivatized mica and glass slides. When associated to spectrophotometric measurements, the AFM data allows assessing the catalytic constant of surface enzymes and comparing it to bulk values. The validity of the Michaelis–Menten model for surface reactions is discussed, supported by spectroscopic measurements of the surface consumption of 1,3-bis-phosphoglycerate (1,3-BPG). Only a few percent of the enzyme material maintains its initial bulk activity. This value could constitute a guideline for biosensors made with the method used here whenever a rapid assessment of the remaining surface activity is needed. |
| doi_str_mv | 10.1016/j.bios.2006.09.007 |
| format | Article |
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Using previous work to improve the sensitivity of the existing setup, Tapping Mode atomic force microscopy (AFM) was used in a liquid environment to determine the surface enzyme coverage of derivatized mica and glass slides. When associated to spectrophotometric measurements, the AFM data allows assessing the catalytic constant of surface enzymes and comparing it to bulk values. The validity of the Michaelis–Menten model for surface reactions is discussed, supported by spectroscopic measurements of the surface consumption of 1,3-bis-phosphoglycerate (1,3-BPG). Only a few percent of the enzyme material maintains its initial bulk activity. 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This value could constitute a guideline for biosensors made with the method used here whenever a rapid assessment of the remaining surface activity is needed.</description><subject>Aluminum Silicates - chemistry</subject><subject>Atomic force microscopy (AFM)</subject><subject>Biocompatible Materials - chemistry</subject><subject>Biological and medical sciences</subject><subject>Biosensing Techniques - methods</subject><subject>Biotechnology</subject><subject>Enzymatic activity</subject><subject>Enzyme Activation</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Fundamental and applied biological sciences. 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| subjects | Aluminum Silicates - chemistry Atomic force microscopy (AFM) Biocompatible Materials - chemistry Biological and medical sciences Biosensing Techniques - methods Biotechnology Enzymatic activity Enzyme Activation Enzymes, Immobilized - chemistry Fundamental and applied biological sciences. Psychology Glass - chemistry Phosphoglycerate kinase Phosphoglycerate Kinase - chemistry Phosphoglycerate Kinase - ultrastructure Surface Properties Yeasts - enzymology |
| title | Enzymatic activity of immobilized yeast phosphoglycerate kinase |
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