A Novel Biosensor Based on Glucose Oxidase for Activity Determination of α – Amylase

REFERENCES

• Gupta, R., Gigras, P., Mohapatra, H., Goswami, V. K., Chauhan, B. (2003). Microbial α-amylases: A biotechnological perspective. Process Biochemistry, 38: 1599–1616.
   Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Strobl, S., Maskos, K., Wiegand, G., Huber, R., Gomis-Rüth, F. X., 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• Mielenz, J. R. (1983). Bacillus stearothermophilus contains a plasmid-borne gene for α-amylase. Proc. Natl. Acad. Sci. USA, 80: 5975–5979.
   PubMed Web of Science ®Google Scholar
• Nielsen, J. E., Borchert, T. V. (2000). Protein engineering of bacterial α-amylases. Biochimica et Biophysica Acta, 1543: 253–274.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   Web of Science ®Google Scholar
• Goesaert, H., Slade, L., Levine, H., Delcour, J. A. (2009). Amylases and bread firming – an integrated view. Journal of Cereal Science, 50: 345–352.
   Web of Science ®Google Scholar
• Yamaguchi, M., Wakasugi, J., Sakakima, J. (2008). Competitive and product inhibition-based α-amylase activity analysis method. Clinical Biochemistry, 41: 325–330.
   PubMed Web of Science ®Google Scholar
• Priya, S., Kaur, N., Gupta, A. K. (2010). Purification, characterization and inhibition studies of α-amylase of Rhyzopertha dominica. Pesticide Biochemistry and Physiology, 98: 231–237.
   Web of Science ®Google Scholar
• 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.
   Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• El-Naggar, M. M. A., Farag, M. G. (2010). Physical and biological treatments of polyethylene–rice starch plastic films. Journal of Hazardous Materials, 176: 878–883.
   PubMedGoogle Scholar
• Miller, G. L. (1959). Use of dinitrosalicylic acid reagent for determination of reducing sugar. Analytical Chemistry, 31: 426–428.
   Web of Science ®Google Scholar
• 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., Hissa, D. C. (2010). Alternative method for quantification of alfa-amylase activity. Braz. J. Biol. 70: 405–407.
   PubMed Web of Science ®Google Scholar
• Wong, D. W. S., Batt, S. B., Robertson, G. H. (2000). Microassay for rapid screening of α-amylase activity. J. Agric. Food Chem., 48: 4540–4543.
   PubMedGoogle Scholar
• Sheehan, H., McCleary, B. V. (1988). A new procedure for the measurement of fungal and bacterial α-amylase. Biotechnology Techniques, 2: 289–292.
   Google Scholar
• Perten, H. (1984). A modified falling-number method suitable for measuring both cereal and fungal alpha-amylase activity. Cereal Chem., 61: 108–111.
   Google Scholar