Inactivation of α-Amylase by Caffeine: Reducing the Break-down of Starch into Sugars
American Journal of Bioscience and Bioengineering
Volume 6, Issue 1, February 2018, Pages: 1-4
Received: Dec. 23, 2017;
Accepted: Dec. 28, 2017;
Published: Jan. 11, 2018
Views 2701 Downloads 264
Neel Rajan, Department of Chemistry, Pennsylvania State University, Du Bois, PA 15801, USA
Stephen James Koellner, Department of Chemistry, Pennsylvania State University, Du Bois, PA 15801, USA
Vincent Todd Calabrese, Department of Chemistry, Pennsylvania State University, Du Bois, PA 15801, USA
Arshad Khan, Department of Chemistry, Pennsylvania State University, Du Bois, PA 15801, USA
Follow on us
α-Amylase, an enzyme present in our saliva and pancreatic secretion, is responsible for the break-down of starch into glucose molecules. Glucose enters into our blood steam and provides energy for various activities. In this study we have noticed that in the presence of caffeine, the enzyme activity is decreased with a decrease in the amount of glucose liberated from the starch hydrolysis. This finding suggests a positive role played by caffeine in the controlling of blood sugar. A possible explanation of enzyme inactivation by caffeine has been discussed in terms of a two-step model that we proposed earlier.
Caffeine-Amylase Interaction, Inactivation of α-Amylase by Caffeine, Reducing the Starch Hydrolysis by Caffeine
To cite this article
Stephen James Koellner,
Vincent Todd Calabrese,
Inactivation of α-Amylase by Caffeine: Reducing the Break-down of Starch into Sugars, American Journal of Bioscience and Bioengineering.
Vol. 6, No. 1,
2018, pp. 1-4.
Copyright © 2018 Authors retain the copyright of this article.
This article is an open access article distributed under the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/
) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
D. J. Manners “Enzymic synthesis and degradation of starch and glycogen” Adv. Carbohydr. Chem. Volume 17, pp 371-430, 1962.
K. Kakiuchi, S. Kato, A. Imanishi, and T. Isemura “Association and Dissociation of Bacillus subtilis α-Amylase Molecule” J. Biochem, Volume 55, No. 2, pp 102-109, 1964.
J. A. Thoma, J. E. Spradlin, and S. Dygert “6 Plant and Animal Amylases” The Enzymes P. D. Boyer Edition, Volume 5, pp 115-189, 1971.
T. Takagi, H. Toda and T. Isemura “Bacterial and mold amylases” The Enzymes P. D. Boyer Edition, Volume 5, pp 235-271, 1971.
J. R. Whitaker “Principles of Enzymology for the Food Sciences” pp 433-467, 1972.
E. Boel, L. Brady, A. M. Brzozowski, Z. Derewenda, G. G. Dodson, V. J. Jensen, S. B. Petersen, H. Swift, L. Thim, and H. F. Woldike “Calcium binding in alpha-amylases: an x-ray diffraction study at 2.1-. ANG. resolution of two enzymes from Aspergillus” Biochemistry, Volume 29, pp 6244-6249, 1990.
A. K. Chandel, R. Rudravaram, L. V. Rao, R. Pogaku, and M. L. Narasu “Industrial enzymes in bioindustrial sector development: An Indian perspective, J. Comm. Biotechnol. Volume 13, No. 4, pp 283-291, 2007.
D. N. Lecker, and A. Khan “Theoretical and experimental studies of the effects of heat, EDTA, and enzyme concentration on the inactivation rate of α-amylase from Bacillus sp.” Biotechnol. Prog. Volume 12, pp 713-717, 1996.
D. N. Lecker and A. Khan, “Model for inactivation of α-amylase in the presence of salts: theoretical and experimental studies” Biotechnol. Prog. Volume 14, pp 621-625, 1998.
O. Fagain, “Understanding and increasing protein stability”. Biochem Biophys Acta. 1252, pp 1–14, 1995.
V. T. Calabrese, J. W. Minns, and A. Khan, “Suppression of α-amylase inactivation in the presence of ethanol: Application of a two-step model”, Biotechnol. Prog., 32, pp 1271- 1275 (2016).