A novel biosensor based on glucose oxidase for activity determination of α-amylase

Artificial Cells, Blood Substitutes, and Biotechnology

Volumn 39, Issue 5, 2011, Pages 298-303

  Altug, Cagri ^a   Mengulluoglu, Umut ^a   Kurt, Elif ^a   Kaya, Secil ^a   Dinckaya, Erhan ^a  

^a EGE UNIVERSITY   (Turkey)

Author keywords

amylase activity; biosensor; Clark electrode; glucose oxidase biosensor

Indexed keywords

AMYLASE ACTIVITY; BAKER'S YEAST; BIO-SENSOR SYSTEMS; BUFFER SYSTEM; CLARK ELECTRODES; DISSOLVED OXYGEN CONCENTRATIONS; GLUTARALDEHYDES; LINEAR RELATION; OPTIMIZATION PARAMETER; SAMPLE ANALYSIS; STARCH CONCENTRATION;

ALDEHYDES; AMYLASES; DISSOLVED OXYGEN; GLUCOSE; GLUCOSE SENSORS; PH EFFECTS; STARCH;

GLUCOSE OXIDASE;

AMYLASE; BUFFER; GELATIN; GLUCOSE OXIDASE; GLUTARALDEHYDE; STARCH;

ARTICLE; ENZYME ACTIVITY; ENZYMIC BIOSENSOR; HYDROLYSIS; NONHUMAN; OXYGEN CONCENTRATION; OXYGEN CONSUMPTION; PH; PROCESS OPTIMIZATION; PROTEIN CROSS LINKING; SACCHAROMYCES CEREVISIAE; TEMPERATURE;

ALPHA-AMYLASES; BIOSENSING TECHNIQUES; CHEMISTRY TECHNIQUES, ANALYTICAL; CROSS-LINKING REAGENTS; ELECTROCHEMISTRY; ELECTRODES; ENZYMES, IMMOBILIZED; GELATIN; GLUCOSE; GLUCOSE OXIDASE; GLUTARAL; HYDROGEN-ION CONCENTRATION; OXYGEN; REPRODUCIBILITY OF RESULTS; SENSITIVITY AND SPECIFICITY; STARCH; TEMPERATURE; YEASTS;

EID: 80052770770     PISSN: 10731199     EISSN: 15324184     Source Type: Journal    
DOI: 10.3109/10731199.2011.574635     Document Type: Article

References (20)

1. Gupta, R., Gigras, P., Mohapatra, H., Goswami, V., K., Chauhan, B. (2003). Microbial α -amylases: A biotechnological perspective. Process Biochemistry , 38: 1599-1616.
2. Payan, F. (2004). Structural basis for the inhibition of mammalian and insect α -amylases by plant protein inhibitors. Biochimica et Biophysica Acta , 1696: 171-180. (Pubitemid 38199847)
3. Strobl, S., Maskos, K., Wiegand, G., Huber, R., Gomis-Rüth, F., X., and Glockshuber, R. (1998). A novel strategy for inhibition of α-amylases: Yellow meal worm α -amylase in complex with the Ragi bifunctional inhibitor at 2.5 Å resolution. Structure , 6: 911-921. (Pubitemid 28348653)
4. Tripathi, P., Leggio, L., L., Mansfeld, J., Ulbrich-Hofmann, R., Kayastha, A. M. (2007). α -amylase from mung beans ( Vigna radiata ) - Correlation of biochemical properties and tertiary structure by homology modeling. Phytochemistry , 68: 1623-1631. (Pubitemid 46879808)
5. Kumar, R. S. S., Singh, S. A., Rao, A. G. A. (2009). Conformational stability of α -amylase from malted sorghum ( Sorghum bicolor ): Reversible unfolding by denaturants. Biochimie , 91: 548-557.
6. Mielenz, J. R. (1983). Bacillus stearothermophilus contains a plasmid-borne gene for α -amylase. Proc. Natl. Acad. Sci. USA , 80: 5975-5979. (Pubitemid 14227595)
7. Nielsen, J. E., Borchert, T. V. (2000). Protein engineering of bacterial α -amylases. Biochimica et Biophysica Acta , 1543: 253-274.
8. Kumari, A., Rosenkranz, T., Kayastha, A. M., Fitter, J. (2010). The effect of calcium binding on the unfolding barrier: A kinetic study on homologous α -amylases. Biophysical Chemistry , 151: 54-60.
9. Francis, F., Sabu, A., Nampoothiri, K. M., Ramachandran, S., Ghosh, S., Szakacs, G., Pandey, A. (2003). Use of response surface methodology for optimizing process parameters for the production of α -amylase by Aspergillus oryzae . Biochemical Engineering Journal , 15: 107-115. (Pubitemid 36734018)
10. Goesaert, H., Slade, L., Levine, H., Delcour, J. A. (2009). Amylases and bread fi rming - an integrated view. Journal of Cereal Science , 50: 345-352.
11. Yamaguchi, M., Wakasugi, J., Sakakima, J. (2008). Competitive and product inhibition-based α -amylase activity analysis method. Clinical Biochemistry , 41: 325-330.
12. Priya, S., Kaur, N., Gupta, A. K. (2010). Puri fi cation, characterization and inhibition studies of α -amylase of Rhyzopertha dominica . Pesticide Biochemistry and Physiology , 98: 231-237.
13. Baks, T., Janssen, A. E. M., Boom, R. M. (2006). The effect of carbohydrates on α -amylase activity measurements. Enzyme and Microbial Technology , 39: 114-119.
14. Saxena, R. K., Dutt, K., Agarwal, L., Nayyar, P. (2007). A highly thermostable and alkaline amylase from a Bacillus sp. PN5. Bioresource Technology , 98: 260-265. (Pubitemid 44354867)
15. El-Naggar, M. M. A., Farag, M. G. (2010). Physical and biological treatments of polyethylene - rice starch plastic fi lms. Journal of Hazardous Materials , 176: 878-883.
16. Miller, G. L. (1959). Use of dinitrosalicylic acid reagent for determination of reducing sugar. Analytical Chemistry , 31: 426-428.
17. Farias, D. F., Carvalho, A. F. U., Oliveira, C. C., Sousa, N. M., Rocha-Bezerrra, L. C. B., Ferreira, P. M. P., Lima, G. P. G. and Hissa, D. C. (2010). Alternative method for quantifi cation of alfα-amylase activity. Braz. J. Biol. 70: 405-407.
18. Wong, D. W. S., Batt, S. B. and Robertson, G. H. (2000). Microassay for rapid screening of α -amylase activity. J. Agric. Food Chem. , 48: 4540-4543.
19. Sheehan, H., and McCleary, B. V. (1988). A new procedure for the measurement of fungal and bacterial α -amylase. Biotechnology Techniques , 2: 289-292.
20. Perten, H. (1984). A modifi ed falling-number method suitable for measuring both cereal and fungal alphα-amylase activity. Cereal Chem. , 61: 108-111.