In the present work, we have studied the inhibitory effects of aqueous and alcoholic extracts of six Algerian medicinal plants known by their therapeutic virtues against diabetes. The total phenolic compounds content, assayed using Folin-Ciocalteu’s reagent, of the samples ranged from 0.183？mg/g to 43.088？mg/g and from 1.197？mg/g to 7.445？mg/g, expressed as gallic acid equivalent (GAE), for the, respectively, whereas the total flavonoids concentrations, detected using 2% of the aluminium chloride, ranged from 0.41？mg/g to 11.613？mg/g and from 0.0097？mg/g to 1.591？mg/g, expressed as rutin equivalents (RE), for the aqueous and methanolic extracts, respectively. The major plants were found to inhibit enzymatic activities of Aspergillus oryzae-amylase in a concentration dependent manner. The values of the inhibition constants ( ) have been determined according to the Dixon and Lineweaver-Burk methods. The results showed that the values were less than 55？ppm for the all extracts. A strong inhibition was found in the phenolic extract of Salvia officinalis with a of 8？ppm. 1. Introduction Diabetes mellitus (DM) is a chronic metabolic disorder caused by an absolute or relative lack of resistance to insulin. It is characterized by hyperglycemia and accompanied by various chronic vascular complications [1–3]. About 171 million people worldwide have diabetes, which is likely to be more than double by 2030 and around 3.2 million deaths every year are attributable to complication of diabetes, six deaths every minute [4, 5]. One therapeutic approach to decrease the hyperglycemia is to retard and reduce the digestion and absorption of ingested carbohydrate hydrolyzing enzymes (such as α-amylase and/or α-glucosidase) in the digestive organs [6–10]. The inhibition of enzymes involved in the digestion of carbohydrates can significantly decrease the postprandial increase of blood glucose after a mixed carbohydrate diet by delaying the process of carbohydrate hydrolysis and absorption [6, 11–13]. Therefore, safer natural amylase and glucosidase inhibitors have been reported from plant sources [14–16]. Arising from their biodiversity and their wealth of active ingredients, plants have been used from antiquity as sources of medicament against various diseases. These properties are usually attributed to secondary metabolites that are the subject of a lot of research in this field. This is particularly the case of polyphenol plants that are widely renowned in therapeutics as anti-inflammatories, enzyme inhibitors, and antioxidants, particularly flavonoids [6, 17–19]. Plant
References
[1]
J. Feng, X. W. Yang, and T. H. Liu, “Bio-assay guided isolation and identification of -glucosidase inhibitors from the leaves of Aquilaria sinensis,” Phytochemistry, vol. 72, no. 2-3, pp. 242–247, 2011.
[2]
A. Gholamhoseinian, H. Fallah, F. Sharifi-Far, and M. Mirtajaddini, “The inhibitory effect of some Iranian plants extracts on the alpha glucosidase,” Iranian Journal of Basic Medical Sciences, vol. 11, pp. 1–9, 2008.
[3]
B. Nickavar and G. Mosazadeh, “Influence of three morus species extracts on α-amylase activity,” Iranian Journal of Pharmaceutical Research, vol. 8, no. 2, pp. 115–119, 2009.
[4]
S. Sancheti and S. Seo, “Chaenomeles sinensis: a potent α-and β-glucosidase inhibitor,” The American Journal of Pharmacology and Toxicology, vol. 4, no. 1, pp. 8–11, 2009.
[5]
M. S. Deutschl？nder, M. van de Venter, S. Roux, J. Louw, and N. Lall, “Hypoglycaemic activity of four plant extracts traditionally used in South Africa for diabetes,” Journal of Ethnopharmacology, vol. 124, no. 3, pp. 619–624, 2009.
[6]
B. Nickavar, A. Alinaghi, and M. Kamalinejad, “Evaluation of the antioxidant properties of five Mentha species,” Iranian Journal of Pharmaceutical Research, vol. 7, no. 3, pp. 203–209, 2008.
[7]
M. R. Bhandari, N. Jong-Anurakkun, G. Hong, and J. Kawabata, “α-Glucosidase and α-amylase inhibitory activities of Nepalese medicinal herb Pakhanbhed (Bergenia ciliata, Haw.),” Journal of Food Chemistry, vol. 106, no. 1, pp. 247–252, 2008.
[8]
S. Shobana, Y. N. Sreerama, and N. G. Malleshi, “Composition and enzyme inhibitory properties of finger millet (Eleusine coracana L.) seed coat phenolics: mode of inhibition of α-glucosidase and pancreatic amylase,” Food Chemistry, vol. 115, no. 4, pp. 1268–1273, 2009.
[9]
B. Nickavar and G. Mosazadeh, “Influence of three morus species extracts on -amylase activity,” Iranian Journal of Pharmaceutical Research, vol. 8, no. 2, pp. 115–119, 2009.
[10]
S. Heo, J. Hwang, J. Choi, J. Han, H. Kim, and Y. Jeon, “Diphlorethohydroxycarmalol isolated from Ishige okamurae, a brown algae, a potent α-glucosidase and α-amylase inhibitor, alleviates postprandial hyperglycemia in diabetic mice,” European Journal of Pharmacology, vol. 615, no. 1-3, pp. 252–256, 2009.
[11]
H. Ali, P. J. Houghton, and A. Soumyanath, “α-Amylase inhibitory activity of some Malaysian plants used to treat diabetes; with particular reference to Phyllanthus amarus,” Journal of Ethnopharmacology, vol. 107, no. 3, pp. 449–455, 2006.
[12]
A. Fred-Jaiyesimi, A. Kio, and W. Richard, “α-Amylase inhibitory effect of 3β-olean-12-en-3-yl (9Z)-hexadec-9-enoate isolated from Spondias mombin leaf,” Food Chemistry, vol. 116, no. 1, pp. 285–288, 2009.
[13]
H. Gao, Y.-N. Huang, B. Gao, P. Li, C. Inagaki, and J. Kawabata, “Inhibitory effect on α-glucosidase by Adhatoda vasica Nees,” Journal of Food Chemistry, vol. 108, no. 3, pp. 965–972, 2008.
[14]
V. Le Berre-Anton, C. Bompard-Gilles, F. Payan, and P. Rougé, “Characterization and functional properties of the α-amylase inhibitor (α-AI) from kidney bean (Phaseolus vulgaris) seeds,” Biochimica et Biophysica Acta, vol. 1343, no. 1, pp. 31–40, 1997.
[15]
R. H. Nagaraj and T. N. Pattabiraman, “Purification and properties of an α-amylase inhibitor specific for human pancreatic amylase from proso (Panicium miliaceum) seeds,” Journal of Biosciences, vol. 7, no. 3-4, pp. 257–268, 1985.
[16]
M. Santimone, R. Koukiekolo, Y. Moreau et al., “Porcine pancreatic α-amylase inhibition by the kidney bean (Phaseolus vulgaris) inhibitor (α-AI1) and structural changes in the α-amylase inhibitor complex,” Biochimica et Biophysica Acta, vol. 1696, no. 2, pp. 181–190, 2004.
[17]
S. Chethan, Y. N. Sreerama, and N. G. Malleshi, “Mode of inhibition of finger millet malt amylases by the millet phenolics,” Food Chemistry, vol. 111, no. 1, pp. 187–191, 2008.
[18]
C. M. Ma, N. Sato, X. Y. Li, N. Nakamura, and M. Hattori, “Flavan-3-ol contents, anti-oxidative and α-glucosidase inhibitory activities of Cynomorium songaricum,” Food Chemistry, vol. 118, no. 1, pp. 116–119, 2010.
[19]
J. Médart, Manuel pratique de nutrition: L’alimentation préventive et curative, édition de Boecks, 2009.
[20]
S. Sancheti, S. Sancheti, and S.-Y. Seo, “Chaenomeles sinensis: A potent α-and β-glucosidase inhibitor,” The American Journal of Pharmacology and Toxicology, vol. 4, no. 1, pp. 8–11, 2009.
[21]
N. Kambouche, B. Merah, A. Derdour et al., “Hypoglycemic and antihyperglycemic effects of Anabasis articulata (Forssk) Moq (Chenopodiaceae), an Algerian medicinal plant,” African Journal of Biotechnology, vol. 8, no. 20, pp. 5589–5594, 2009.
[22]
B. I. Giner-Chavez, Condensed tannins in tropical forages [Ph.D. thesis], Cornell University, Ithaca, NY, USA, 1996.
[23]
T. Bahorun, “Substances naturelles actives: la flore mauricienne, une source dapprovisionnement potentielle,” in Proceedings of the 2nd Annual Meeting of Agricultural Scientists, J. A. Lalouette, D. Y. Bachraz, N. Sukurdeep, and B. D. Seebaluck, Eds., pp. 83–94, Food and Agricultural Research Council, 1998.
[24]
S. Dygert, L. H. Li, D. Florida, and J. A. Thoma, “Determination of reducing sugar with improved precision,” Analytical Biochemistry, vol. 13, no. 3, pp. 367–374, 1965.
[25]
M. Naczk and F. Shahidi, “Extraction and analysis of phenolics in food,” Journal of Chromatography A, vol. 1054, no. 1-2, pp. 95–111, 2004.
[26]
A. Andrade-Cetto, J. Becerra- Jiménez, and R. Càrdenas-Vàzquez, “Alpha-glucosidase-inhibiting activity of some Mexican plants used in the treatment of type II diabetes,” Ethnopharmacology, vol. 116, pp. 27–32, 2007.
[27]
S. P. Kalidas and P. McCue, “Inhibitory effects of rosmarinic acid extracts on porcine pancreatic amylase in vitro,” Asia Pacific Journal of Clinical Nutrition, vol. 13, no. 1, pp. 101–106, 2004.
[28]
E. Apostolidis, Y. I. Kwon, and K. Shetty, “Inhibitory potential of herb, fruit, and fungal-enriched cheese against key enzymes linked to type 2 diabetes and hypertension,” Innovative Food Science and Emerging Technologies, vol. 8, no. 1, pp. 46–54, 2007.
[29]
S. S. Ali, N. Kasoju, A. Luthra et al., “Indian medicinal herbs as sources of antioxidants,” Food Research International, vol. 41, no. 1, pp. 1–15, 2008.
[30]
X. Han, T. Shen, and H. Lou, “Dietary polyphenols and their biological significance,” International Journal of Molecular Sciences, vol. 8, no. 9, pp. 950–988, 2007.
[31]
A. Djeridane, M. Yousfi, J. M. Brunel, N. Vidal, E. H. Ajandouz, and P. Stocker, “Inhibition of porcine liver carboxylesterase by a new flavone glucoside isolated from Deverra scoparia,” Chemico-Biological Interactions, vol. 172, no. 1, pp. 22–26, 2008.
[32]
A. Djeridane, M. Yousfi, B. Nadjemi, S. Maamri, F. Djireb, and P. Stocker, “Phenolic extracts from various Algerian plants as strong inhibitors of porcine liver carboxylesterase,” Journal of Enzyme Inhibition and Medicinal Chemistry, vol. 21, no. 6, pp. 719–726, 2006.
[33]
I. Khacheba, A. Djeridane, A. Kameli, and M. Yousfi, “he inhibitory effect of some algerian plants phenolics extracts on the -glucosidase and -amylase activities and their antioxidant activity,” Current Enzyme Inhibition, vol. 10, pp. 59–68, 2014.
[34]
P. Tiwari, B. Kumar, M. Kaur, G. Kaur, and H. Kaur, “Phytochemical screening and extraction: a review,” Internationale Pharmaceutica Sciencia, vol. 1, no. 1, pp. 98–106, 2011.
[35]
B. L. Sampaio, M. T. F. Bara, P. H. Ferri, S. da Costa Santos, and J. R. de Paula, “Influence of environmental factors on the concentration of phenolic compounds in leaves of Lafoensia pacari,” Brazilian Journal of Pharmacognosy, vol. 21, no. 6, pp. 1127–1137, 2011.
[36]
M. Richardson, Methods in Biochemistry, vol. 5, Academic Press, 1991.
[37]
L. Octivio and D. Rigden, “Activity of wheat α-amylase inhibitors towards bruchid α-amylases and structural explanation of observed specificities,” European Journal of Biochemistry, vol. 267, pp. 2166–2173, 2000.
[38]
J. Kim, C. Kwon, and K. H. Son, “Inhibition of Alpha-glucosidase and Amylase by Luteolin, a Flavonoid,” Bioscience, Biotechnology and Biochemistry, vol. 64, no. 11, pp. 2458–2461, 2000.
[39]
T. Matsui, T. Ueda, T. Oki, K. Sugita, N. Terahara, and K. J. Matsumoto, “Alpha-glucosidas inhibition isolated anthocyanins,” Journal of Agricultural and Food Chemistry, vol. 49, pp. 1948–1951, 2001.
