Recent status on carbohydrate metabolizing enzyme inhibitors in regulation of diabetes: a mechanism based review
Keywords:α- Glucosidase, α-amylase, Sucrase, Maltase, Diabetes
The important therapeutic approach for treating type 2 diabetes mellitus is to decrease the post-prandial glucose levels which could be done by decreasing the absorption of glucose through the inhibition of the carbohydrates-hydrolyzing enzymes such as α-amylase and α-glucosidase present in the small intestinal brush border that are responsible for the breakdown of oligosaccharides and disaccharides into monosaccharide’s and suitable for absorption. Inhibition of α-amylase generally considered as strategy for the treatment of disorders in carbohydrate uptake, such as diabetes and obesity. Among the marketed allopathic preparations carbohydrates-hydrolyzing enzymes Inhibitors like acarbose, voglibose etc delay carbohydrate digestion and prolong overall carbohydrate digestion time, causing a reduction in the rate of glucose absorption and consequently blunting the postprandial plasma glucose rise. Some of the plants are also considered as an important source of chemical constituent with potential for inhibition of α-amylase and can be used as therapeutic purposes. In this review our efforts have been devoted to explore the mechanism based carbohydrates-hydrolyzing enzymes Inhibitors for the regulation of diabetes.
Murthy K.T.P., Sundarram A., α-Amylase Production and Applications: A Review, Journal of Applied & Environmental Microbiology, 2014, Vol. 2, No. 4, 166-175.
Prasad N.K., “Enzyme Technology: Pacemaker of Biotechnology”, PHI Learning Pvt. Ltd., 2011.
Gupta R., Gigras P., Mohapatra H., Goswami V.K. & Chauhan B. “Microbial α-amylases: a biotechnological perspective”, Process Biochemistry, 2003, 38 (11), 1599-1616.
Drauz K., Gröger H., & May O. (Eds.) Enzyme catalysis in organic synthesis: a comprehensive Handbook, John Wiley & Sons, (2012), Souza, P. M. D., “Application of microbial α-amylase in industry-A review”, Brazilian journal of microbiology, May (2010) 41 (4), 850-861.
Leonard R.J., Gastrointestinal Physiology, 7th edition, New delhi, India. Mosby An Imprint of Elsevier, 2007.
Kahn S.E., Porte D. Jr. Beta cell dysfunction in type 2 diabetes. In: Scriver C.R., Beauted A.L., Sly W.S., Valle D., eds. The metabolic and molecular bases of inherited disease, 8th edition New York: McGrow-Hill, 2001: 1407-1431.
Hanhineva K., Torronen R., Bondia-Pons I., Pekkinen J., Kolehmainen M., Mykkanen H. and Poutanen K., Impact of Dietary Polyphenols on Carbohydrate Metabolism, International Journal of Molecular Sciences ISSN 1422-0067, Int. J. Mol. Sci. 2010, 11, 1365-1402; doi:10.3390/ijms11041365.
Quezada-Calvillo R., Robayo-Torres, C.C., Ao Z., Hamaker, B.R., Quaroni, A., Brayer G.D., Sterchi E.E., Baker S.S., Nichols B.L. Luminal substrate "brake" on mucosal maltaseglucoamylase activity regulates total rate of starch digestion to glucose. J. Pediatr. Gastroenterol. Nutr. 2007, 45, 32–43.
Quezada-Calvillo R., Robayo-Torres C.C., Opekun A.R., Sen P., Ao Z., Hamaker B.R., Quaroni A., Brayer G.D., Wattler S., Nehls M.C., Sterchi E.E., Nichols B.L. Contribution of mucosal maltase-glucoamylase activities to mouse small intestinal starch alpha-glucogenesis. J. Nutr. 2007, 137, 1725–1733.
Quezada-Calvillo R., Sim L., Ao Z., Hamaker B.R., Quaroni A., Brayer G.D., Sterchi E.E., Robayo-Torres C.C., Rose D.R., Nichols B.L. Luminal starch substrate "brake" on maltaseglucoamylase activity is located within the glucoamylase subunit. J. Nutr. 2008, 138, 685–692.
Solomon A., Ahuja L., Mekonnen A., Tsehayneh K., Henok T., Belayhun K., Solomon G., Medical Biochemistry, Ethiopia Public Health Training Initiative, 2004.
Robert K., Murray R. K., Granner D. K., Mayes P. A., Rodwell, V. W. 1993. Harpers Biochemistry. 23rd ed. Prentice-Hall International Inc.
Apps D. K., Cohn B. B. and Steel C. M. 1992. Biochemistry. A concise text for medical students. 5th ed. ELBS with Baillie’re Tindall.
Guyton and Hall, Textbook of Medical Physiology, ninth edition: 1996.
Saltiel A.R., Pessin J.E., Insulin signaling pathways in time and space. Trends cell Biol. 2002; 12:65-71.
Paloma M.D.S., Paula M.D.S., Luiz A.S., Pérola D.O.M., Dâmaris S., α-Amylase Inhibitors: A Review of Raw Material and Isolated Compounds from Plant Source, J Pharm Pharmaceut Sci 15(1) 141 - 183, 2012.
Laar F.A., Lucassen P.L.B.J., Akkermans R.P., Lisdonk E.H., Rutten G.E.H.M., Weel C. Alpha-glucosidase inhibitors for type 2 diabetes mellitus (Cochrane Review). The Cochrane Library, 2008.
Yanovski S.Z., Yanovski J.A., Drug Therapy: Obesity. N. Engl. J. Med., 2002; 346: 5991-602.
Touger D.R., Loveren C.V., Sugars and dental caries. Am. J. Clin. Nutr., 2003; 78: 88S–92S.
Cheng A.Y.Y., Fantus I.G., Oral antihyperglycemic therapy for type 2 diabetes Mellitus. Can. Med. Assoc. J., 2005; 172: 213-226.
Aguiar L.G.K., Villela N.R., Bouskela E.A., Microcirculação no Diabetes: Implicações nas Complicações Crônicas e Tratamento da Doença. Arq Bras Endocrinol Metab 2007; 51: 204-211.
Funke I., Melzing M.F., Traditionally used plants in diabetes therapy - phytotherapeutics as inhibitors of a-amylase activity. Rev Bras Farmacogn, 2006; 16: 1-5.
Inzucchi S.E., Oral antihyperglycemic therapy for type 2 diabetes. JAMA, 2002; 287: 360-372.
Chakrabarti R., Rajagopalan R., Diabetes and insulin resistance associated disorders: Disease and the therapy. Current Sci, 2002; 83: 1533-1538.
Goke B., Herrmann R.C., The evolving role of alpha-glucosidase inhibitors. Diabetes/Metab Res, 1998; 14: S31-S38.
Lebowitz H.E., alpha-glucosidase inhibitors as agents in the treatment of diabetes Diabetes Rev, 1998; 6: 132-145.
Nair S.S., Kavrekar V., Mishra A., In-vitro studies on alpha amylase and alpha glucosidase inhibitory activities of selected plant extracts, European Journal of Experimental Biology, 2013, 3(1):128-132.
Olaokun O.O., McGraw J.L., Endy E.N.J., Naidoo V., Evaluation of the inhibition of carbohydrate hydrolyzing enzymes, antioxidant activity and polyphenolic content of extract of ten African Ficus spacies (Moraceae) used traditionally to treat diabetes, BMC Complementary and Alternative Medicine 2013, 13:94.
Jung M., Park M., Chul H.L., Kang Y., SEok-Keng E., Ki-Kim S., Curr. Med. Chem, 2006, 13, 1.
Kneen E., Sandstedt R.M., Hollenbeck C.M., Cereal Chem, 1943, 20:399.
Ganeshpurkar Aditya, Diwedi Varsha, Bhardwaj Yash, In-vitro alpha amylase and alpha glucosidase inhibitory potential of Trigonella foemum-graecum leaves extract, Pharmacological Study, page no. 109-112, volume-34, issue-1, year-2013, www.ayujournal.org/article.
Satish R., Madhavan R., Vasanthi R. Hannah, Amuthan Arul, In-vitro alpha glucosidase inhibitory activity of abraga chendhooram, a Siddha drug, International journal of pharmacology and clinical sciences, September 2012, Vol. 1, Issue 3, page no. 79-81.
Dsouza D., Lakshmidevi N., Models to study In-vitro antidiabetic activity of plants: A review, International Journal of Pharma and Bio Sciences, 2015, July,; 6(3): (B) 732-741.
Thorat K., Patil L., Limaye D., Kadam V., In-vitro Models for antidiabetic activity assessment, International journal of Research in Pharmaceutical and Biomedical sciences, Vol. 3 (2), Apr.-Jun 2012. Page no. 730-733.
Somani G., Chaudhari R., Sancheti J., Sathaye S., Inhibition of carbohydrate hydrolysing enzymes by methanolic extract of Couroupita Guianesis leaves, International Journal of Pharma and Bio Sciences, 2012, Oct.; 3(4): (P) 511-520.
Honda M., Hara Y., Inhibition of rat small intestinal Socrase and alpha-glucosidase activities by tea polyphenols. Bioscience, Biotechnology and Biochemistry, 57: 123-4, (1993).
Chaudhury A., Maeda K., Murayama R., et al., gastroenterology, 1996, 111:1313-20.
How to Cite
Copyright (c) 2020 Durgeshnandani Sinha, Trilochan Satapathy, Mehendra Kumar Dewangan, Arvind Kumar, Amit Roy
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.
In submitting an article to Journal of Applied Pharmaceutical Research (JOAPR) I certify that:
- I am authorized by my co-authors to enter into these arrangements.
- I warrant, on behalf of myself and my co-authors, that:
- the article is original, has not been formally published in any other peer-reviewed journal, is not under consideration by any other journal and does not infringe any existing copyright or any other third party rights;
- I am/we are the sole author(s) of the article and have full authority to enter into this agreement and in granting rights to JOAPR are not in breach of any other obligation;
- the article contains nothing that is unlawful, libellous, or which would, if published, constitute a breach of contract or of confidence or of commitment given to secrecy;
- I/we have taken due care to ensure the integrity of the article. To my/our - and currently accepted scientific - knowledge all statements contained in it purporting to be facts are true and any formula or instruction contained in the article will not, if followed accurately, cause any injury, illness or damage to the user.
- I, and all co-authors, agree that the article, if editorially accepted for publication, shall be licensed under the Creative Commons Attribution-NonCommercial 4.0 International License
- I, and all co-authors, agree that, if the article is editorially accepted for publication in Journal of Applied Pharmaceutical Research (JOAPR) data included in the article shall be made available under the Creative Commons 1.0 Public Domain Dedication waiver, unless otherwise stated. For the avoidance of doubt it is stated that sections 1, 2, and 3 of this license agreement shall apply and prevail.