Inhibition of baker’s yeast alpha glucosidase by extract and fractions of stem bark of Terminalia catappa Linn. (Combretaceae) Terminalia catappa Linn. (Combretaceae) stem bark fractions inhibited baker’s yeast alpha glucosidase

Main Article Content

Olusegun Ajala
Adeola Makinde
Comfort Ogah

Abstract

Background: Paucity of clinically applicable inhibitors has limited alpha glucosidase inhibition therapeutic strategy of type 2 diabetes management. The current investigation was aimed at evaluating the anti-diabetic alpha glucosidase inhibitory potentials of Terminalia catappa stem bark extract and its fractions, modeling the implicated intestinal brush border membrane alpha glucosidases with the baker’s yeast alpha glucosidase maltase.


Methods: A crude stem bark extract of Terminalia catappa and its n-hexane-, dichloromethane- and methanol-soluble fractions were incubated with the baker’s yeast alpha glucosidase at various final assay mixture concentrations, carrying along acarbose as reference standard.  IC50 values were calculated from % inhibition vs concentration plots and analyzed using one-way ANOVA with Tukey’s post hoc comparison.


Results: The methanol, n-hexane and dichloromethane fractions inhibited alpha glucosidase with IC50 values  173.85 ± 6.90 ?g/ml, 258.56 ± 12.90 ?g/ml and 329.90 ± 10.67 ?g/ml respectively which are in the same order as that of acarbose  (123.26 ± 15.56 ?g/ml) and significantly smaller (p < 0.0001) than that of the crude extract (527.67 ± 16.32 ?g/ml).


Conclusion:  The three fractions potently inhibited baker’s yeast alpha glucosidase, indicating presence of alpha glucosidase inhibitory molecules of diverse polarity and, hence, structures in the T. catappa stem bark extract. This investigation has suggested alpha glucosidase inhibition as a possible action mechanism of the anti-diabetic use of T. catappa, unmasking its stem bark extract as a repertoire for the discovery of compounds of diverse molecular structures with possible anti-diabetic alpha glucosidase inhibitory activities.

Downloads

Download data is not yet available.

Article Details

How to Cite
Ajala, O., Makinde, A., & Ogah, C. (2023). Inhibition of baker’s yeast alpha glucosidase by extract and fractions of stem bark of Terminalia catappa Linn. (Combretaceae): Terminalia catappa Linn. (Combretaceae) stem bark fractions inhibited baker’s yeast alpha glucosidase. Nigerian Journal of Pharmaceutical and Applied Science Research, 11(4), 1–7. Retrieved from http://mail.nijophasr.net/index.php/nijophasr/article/view/496
Section
Articles

References

Kuzuya T, Matsuda A. Classification of diabetes on the basis of etiologies versus degree of insulin deficiency. Diabetes Care. 1997;20(2):219.

Mayfield JA. Diagnosis and classification of diabetes mellitus: new criteria. American Family Physician. 1998;58(6):1355.

DeFronzo RA, Ferrannini E, Groop L, Henry RR, Herman WH, Holst JJ, Hu FB, Kahn CR, Raz I, Shulman GI, Simonson DC. Type 2 diabetes mellitus. Nature Reviews Disease Primers. 2015;1(1):1-22.

Forbes JM, Cooper ME. Mechanisms of diabetic complications. Physiological Reviews. 2013;93(1):137-88.

Westermark P, Johnson KH. The pathogenesis of maturity?onset diabetes mellitus: Is there a link to islet amyloid polypeptide?. Bioessays. 1988;9(1):30-3.

Galloway JA. Treatment of NIDDM with insulin agonists or substitutes. Diabetes Care. 1990;13(12):1209-39.

Nathan DM, Buse JB, Davidson MB, Ferrannini E, Holman RR, Sherwin R, Zinman B. Medical management of hyperglycemia in type 2 diabetes: a consensus algorithm for the initiation and adjustment of therapy: a consensus statement of the American Diabetes Association and the European Association for the Study of Diabetes. Diabetes Care. 2009;32(1):193-203.

Granner DK, O'Brien RM. Molecular physiology and genetics of NIDDM: importance of metabolic staging. Diabetes Care. 1992;15(3):369-95

McCarty MF. Exploiting complementary therapeutic strategies for the treatment of type II diabetes and prevention of its complications. Medical Hypotheses. 1997;49(2):143-52.

Jain S, Saraf S. Type 2 diabetes mellitus—Its global prevalence and therapeutic strategies. Diabetes & Metabolic Syndrome: Clinical Research & Reviews. 2010;4(1):48-56.

Krasikov VV, Karelov DV, Firsov LM. ?-Glucosidases. Biochemistry (Moscow). 2001;66(3):267-81.

Yamamoto, I., Muto, N., Nagata, E., Nakamura, T. and Suzuki, Y. Formation of a stable L-ascorbic acid ?-glucoside by mammalian ?-glucosidase-catalyzed transglucosylation. Biochimica et Biophysica Acta (BBA)-General Subjects. ., 1990;1035(1):44-50.

Herscovics A. Importance of glycosidases in mammalian glycoprotein biosynthesis. Biochimica et Biophysica Acta (BBA)-General Subjects. 1999;1473(1):96-107.

Caputo, A.T., Alonzi, D.S., Marti, L., Reca, I.B., Kiappes, J.L., Struwe, W.B., Cross, A., Basu, S., Lowe, E.D., Darlot, B. and Santino, A. Structures of mammalian ER ?-glucosidase II capture the binding modes of broad-spectrum iminosugar antivirals. Proceedings of the National Academy of Sciences. 2016;113(32):E4630-E4638.

Jockovic? N, Fischer W, Brandsch M, Brandt W, Dra?ger B. Inhibition of human intestinal ?-glucosidases by calystegines. Journal of Agricultural and Food Chemistry. 2013;61(23):5550-5557.

Lee, B.H., Rose, D.R., Lin, A.H.M., Quezada-Calvillo, R., Nichols, B.L. and Hamaker, B.R. Contribution of the individual small intestinal ?-glucosidases to digestion of unusual ?-linked glycemic disaccharides. Journal of Agricultural and Food Chemistry. 2016;64(33):6487-6494.

Lin AH, Lee BH, Chang WJ. Small intestine mucosal ?-glucosidase: A missing feature of in vitro starch digestibility. Food Hydrocolloids. 2016;53:163-71.

Tundis R, Loizzo MR, Menichini F. Natural products as ?-amylase and ?-glucosidase inhibitors and their hypoglycaemic potential in the treatment of diabetes: an update. Mini reviews in medicinal chemistry. 2010;10(4):315-31.

Butler PC, Rizza RA. Contribution to postprandial hyperglycemia and effect on initial splanchnic glucose clearance of hepatic glucose cycling in glucose-intolerant or NIDDM patients. Diabetes. 1991;40(1):73-81.

Mitrakou A, Kelley D, Veneman T, Jenssen T, Pangburn T, Reilly J, Gerich J. Contribution of abnormal muscle and liver glucose metabolism to postprandial hyperglycemia in NIDDM. Diabetes. 1990;39(11):1381-90.

Dirir AM, Daou M, Yousef AF, Yousef LF. A review of alpha-glucosidase inhibitors from plants as potential candidates for the treatment of type-2 diabetes. Phytochemistry Reviews. 2022;21(4):1049-79.

Reuser AJ, Wisselaar HA. An evaluation of the potential side?effects of ??glucosidase inhibitors used for the management of diabetes mellitus. European Journal of Clinical Investigation. 1994;24(S3):19-24.

Shai LJ, Magano SR, Lebelo SL, Mogale AM. Inhibitory effects of five medicinal plants on rat alpha-glucosidase: Comparison with their effects on yeast alpha-glucosidase. Journal of Medicinal Plants Research. 2011;5(13):2863-7.

Lachance H, Wetzel S, Kumar K, Waldmann H. Charting, navigating, and populating natural product chemical space for drug discovery. Journal of Medicinal Chemistry. 2012;55(13):5989-6001.

Tamilselvan N, Thirumalai T, Shyamala P, David E. A review on some poisonous plants and their medicinal values. Journal of Acute Disease. 2014 Jan 1;3(2):85-9.26. Divya N, Rengarajan RL, Radhakrishnan R, Abd_Allah EF, Alqarawi AA, Hashem A, Manikandan R, Anand AV. Phytotherapeutic efficacy of the medicinal plant Terminalia catappa L. Saudi Journal of Biological Sciences. 2019;26(5):985-988.

Mallik J, Al FA, Kumar BR. A Comprehensive review on pharmacological activity of Terminalia Catappa (combretaceae)-An update. Asian Journal of Pharmaceutical Research and Development. 2013;1(2):65-70.

Marjenah M, PUTRI NP. Morphological characteristic and physical environment of Terminalia catappa in East Kalimantan, Indonesia. Asian Journal of Forestry. 2017;1(1):33-9.

Kumar VD, Kokila GS, Sarvatha AD, Pradeepa D. Phytochemical Profiles, In Vitro Antioxidant, Anti Inflammatory and Antibacterial Activities of Aqueous Extract of Terminalia catappa L. leaves. Journal of Pharmaceutical Sciences and Research. 2021;13(6):340-6.

Olukotun AB, Bello IA, Oyewale OA. Phytochemical and anthelmintic activity of Terminalia catappa (Linn) leaves. Journal of Applied Sciences and Environmental Management. 2018;22(8):1343-1347.

Bankar SB, Bule MV, Singhal RS, Ananthanarayan L. Glucose oxidase—an overview. Biotechnology Advances. 2009;27(4):489-501.

https://www.biolabo.fr/pdfs/noticesE/biochimieE/AT-87409.pdf

Daum G. The yeast Saccharomyces cerevisiae, a eukaryotic model for cell biology. Microscopy Research and Technique. 2000;51(6):493-495.

Khatami SH, Vakili O, Ahmadi N, Soltani Fard E, Mousavi P, Khalvati B, Maleksabet A, Savardashtaki A, Taheri?Anganeh M, Movahedpour A. Glucose oxidase: Applications, sources, and recombinant production. Biotechnology and Applied Biochemistry. 2022;69(3):939-950.

Kornecki JF, Carballares D, Tardioli PW, Rodrigues RC, Berenguer-Murcia Á, Alcántara AR, Fernandez-Lafuente R. Enzyme production of D-gluconic acid and glucose oxidase: successful tales of cascade reactions. Catalysis Science & Technology. 2020;10(17):5740-5771.

Hillert M. Le Chatelier’s principle—restated and illustrated with phase diagrams. Journal of Phase Equilibria. 1995;16(5):403-410.

Horn JR, Shoichet BK. Allosteric inhibition through core disruption. Journal of Molecular Biology. 2004;336(5):1283-1291.