Inhibitory Effect of Phallusia Nigra (Savigny, 1816) Extract on Activity of Alpha –Amylase
Subject Areas :
Journal of Animal Biology
Asmae Tajik
1
,
Mousa Keshavarz
2
,
Ahmad Homaei
3
1 - Department of Marine Biology, Faculty of Marine Science and Technology, University of Hormozgan, BandarAbbas, Iran
2 - Department of Marine Biology, Faculty of Marine Science and Technology, University of Hormozgan, BandarAbbas, Iran
3 - Department of Marine Biology, Faculty of Marine Science and Technology, University of Hormozgan, BandarAbbas, Iran
Received: 2021-08-26
Accepted : 2021-09-11
Published : 2022-05-22
Keywords:
IC50,
Antidiabetic,
Alpha-amylase,
DNSA,
Phallusia nigra,
Acarbose,
Abstract :
Increased blood sugar levels play an important role in the development of diabetes. Thus, inhibition of alpha-amylase enzyme inhibits the conversion of polysaccharides to glucose or reduces it. In diabetics, this enzyme can be effective in absorbing glucose from the gastrointestinal tract and preventing a rapid rise in blood sugar. Ascidians are known as a group of marine fauna rich in bioactive secondary metabolites. This study was aimed at evaluating the inhibitory effect of alpha-amylase activity on Phallusia nigra. Specimens of P. nigra belonged to Qeshm and Hormoz islands. Under vacuum, using a rotary evaporator, the samples were extracted from polarity, i.e. ethyl acetate, methanol and water-methanol, respectively. Moreover, the percentage of alpha-amylase inhibitor activity was evaluated based on DNSA method in vitro and acarbose was used as a positive control. The results revealed that among all extracts, the highest inhibitory percentage was related to acarbose at a concentration of 2000 µg/ml equal to 69.65% and the lowest value was related to water-methanolic extract at a concentration of 500 µg/ml and equal to 15.39%. The highest inhibitory activity was observed as acarbose>ethyl acetate>methanol>water-methanol. Furthermore, the results showed a direct relationship between the level of enzyme inhibition and the concentration of extracts. In this study, ethyl acetate extract had the highest inhibitory effect of alpha-amylase enzyme with IC50 equal to 1327.244 µg/ml, followed by methanolic extract with IC50 equal to 1529.68 µg/ml. Water-methanolic extract had the lowest inhibitory effect with IC50 and equal to 2334.01 µg/ml. The inhibitory percentage of acarbose was higher than other extracts (IC50=1158.40 µg/ml). Due to the inhibitory power of P. nigra extracts, they can be used in the future in the production of anti-diabetic drugs with minimal or no adverse side effects.
References:
Afrisham R., Aberomand M., Ghaffari M. A., Siahpoosh, A., Jamalan M. 2015. Inhibitory Effect of Heracleum persicum and Ziziphus jujuba on Activity of Alpha-Amylase. Journal of Botany, 2015: 1-8.
Akkarachiyasit S., Charoenlertkul P., Yibchok-Anun S., Adisakwattana S. 2010. Inhibitory activities of cyanidin and its glycosides and synergistic effect with acarbose against intestinal α-glucosidase and pancreatic α-amylase. International Journal of Molecular Sciences, 11(9): 3387-3396.
Ali H., Anwar M., Ahmad T., Chand N. 2006. Diabetes mellitus from antiquity to present scenario and contribution of Greco-Arab physicians. Jishim, 5(10): 46-50.
Baharmiyan Nasab S. 2018. Evaluation of antidiabetic and inhibitory effects of zinc oxide nanoparticles and extracts of two species of sea Algae Gracilaria corticata and Sargassum angustifolium on alpha-amylase activity. M.Sc. Thesis in Marine biology. University of Hormozgan, (In Persian)
Bhandari M.R., Jong-Anurakkun N., Hong G., Kawabata J. 2008. α-Glucosidase and α-amylase inhibitory activities of Nepalese medicinal herb Pakhanbhed (Bergenia ciliata, Haw.). Food Chemistry, 106(1): 247-252.
Ceriello A. 2005. Postprandial hyperglycemia and diabetes complications: is it time to treat? Diabetes. 54(1): 1-7.
Choudhary D.K., Mishra A. 2017. In vitro and in silico interaction of porcine α-amylase with Vicia faba crude seed extract and evaluation of antidiabetic activity. Bioengineered, 8(4): 393-403.
Des Gachons C.P., Breslin P.A. 2016. Salivary amylase: digestion and metabolic syndrome. Current Diabetes Reports, 16(10): 1-7.
Funke I., Melzig M.F. 2006. Traditionally used plants in diabetes therapy: phytotherapeutics as inhibitors of alpha-amylase activity. Revista Brasileira de Farmacognosia, 16(1): 1-5.
Groop L., Pociot F. 2014. Genetics of diabetes–are we missing the genes or the disease? Molecular and cellular endocrinology, 382(1): 726-739.
Huvet A., Béguel J.P., Cavaleiro N.P., Thomas Y., Quillien V., Boudry P., Alunno-Brusciaa M., Fabioux C. 2015. Disruption of amylase genes by RNA interference affects reproduction in the Pacific oyster Crassostrea gigas. The Journal of Experimental Biology, 218(11): 1740-1747.
Izquierdo Muñoz A., Díaz Valdés M., Ramos-Esplá A.A. 2009. Recent non-indigenous ascidians in the Mediterranean Sea. Aquatic Invasions, 4(1): 59-64.
Karthikeyan M.M., Ananthan G., Ali A. J. 2009. Food and Feeding Habits of Herdmania pallida (Heller)(Urochordata: Ascidiacea) from Palk Strait, Southeast of India. World Journal of Fish and Marine Sciences, 1(3): 225-229.
Kazeem M.I., Adamson J.O., Ogunwande I.A. 2013. Modes of inhibition of α-amylase and α-glucosidase by aqueous extract of Morinda lucida Benth leaf. BioMed Research International, 2013: 1-6.
Khadayat K., Marasini B.P., Gautam H., Ghaju S., Parajuli N. 2020. Evaluation of the alpha-amylase inhibitory activity of Nepalese medicinal plants used in the treatment of diabetes mellitus. Clinical Phytoscience, 6(34): 1-8.
Kim J.C., Simmins P.H., Mullan B.P., Pluske J.R. 2005. The digestible energy value of wheat for pigs, with special reference to the post-weaned animal. Animal Feed Science and Technology, 122(3-4): 257-287.
Kim J.S., Kwon C.S., Son K.H. 2000. Inhibition of alpha-glucosidase and amylase by luteolin, a flavonoid. Bioscience, Biotechnology and Biochemistry, 64(11): 2458-2461.
Kott P. 2003. New syntheses and new species in the Australian Ascidiacea. Journal of Natural History, 37(13): 1611-1653.
Kwon Y.I., Jang H.D., Shetty K. 2006. Evaluation of Rhodiola crenulata and Rhodiola rosea for management of type II diabetes and hypertension. Asia Pacific Journal of Clinical Nutrition, 15(3): 425- 432.
Lambert G., Lambert C.C. 1987. Spicule formation in the solitary ascidian, Herdmania momus. Journal of Morphology, 192(2): 145-159.
Lo Piparo E., Scheib H., Frei N., Williamson G., Grigorov M., Chou C.J. 2008. Flavonoids for controlling starch digestion: structural requirements for inhibiting human α-amylase. Journal of Medicinal Chemistry, 51(12): 3555-3561.
Manach C., Scalbert A., Morand C., Rémésy C., Jiménez L. 2004. Polyphenols: food sources and bioavailability. The American Journal of Clinical Nutrition, 79(5): 727-747.
Matull W.R., Pereira S.P., O’donohue J.W. 2006. Biochemical markers of acute pancreatitis. Journal of Clinical Pathology, 59(4): 340-344.
Mikami N., Hosokawa M., Miyashita K. 2010. Effects of sea squirt (Halocynthia roretzi) lipids on white adipose tissue weight and blood glucose in diabetic/obese KK-Ay mice. Molecular Medicine Reports, 3(3): 449-453.
Momina S.S., Rani V.S. 2020. In vitro Studies on α-Amylase and α-Glucosidase Inhibitory Activity of Some Bioactive Extracts. Journal of Young Pharmacists, 12(2): 72-75.
26. Monniot C. Monniot F. 2001. Ascidians from the tropical western Pacific. Zoosystema, 23(2): 201-383.
27. Muthukrishnan S. 2014. In silico docking studies of cholesterol esterase inhibitory activity of commercially available flavonoids. International Journal of Pharmacy Education and Research, 1(2): 1-7.
Muthukrishnan S., Sivakkumar T. 2017. In vitro studies to assess the antidiabetic potential of Schleichera oleosa (Lour) oken leaves. Asian Journal of Pharmaceutical and Clinical Research, 10(7): 280-283.
Nair S.S., Kavrekar V., Mishra A. 2013. In vitro studies on alpha amylase and alpha glucosidase inhibitory activities of selected plant extracts. European Journal of Experimental Biology, 3(1): 128-132.
30. Nater U.M., Rohleder N. 2009. Salivary alpha-amylase as a non-invasive biomarker for the sympathetic nervous system: current state of research. Psychoneuroendocrinology, 34(4): 486-496.
Oyedemi S., Koekemoer T., Bradley G., Van de Venter M., Afolayan A. 2013. In vitro anti-hyperglycemia properties of the aqueous stem bark extract from Strychnos henningsii (Gilg). International Journal of Diabetes in Developing Countries, 33(2): 120-127.
Park M.K., Jung U., Roh C. 2011. Fucoidan from marine brown algae inhibits lipid accumulation. Marine Drugs, 9(8): 1359-1367.
Prabhu A.S., Ananthan G. 2014. Alpha-amylase inhibitory activities of ascidians in the reatment of diabetes mellitus. Bangladesh Pharmacological Society, 9(4): 498-500.
Priya D.S., Christy H.K.S., Sankaravadivu S. 2016. Quality and quantitative estimations of chemical constituents in a simple Ascidian Phallusia nigra. World Journal of Pharmaceutical Research, 5(02): 1492-1497.
Robyt J.F. 2005. Inhibition, activation, and stabilization of α-amylase family enzymes. Biologia Bratislava, 60(16):17-26.
Rocha R.M., Faria S.B., Moreno, T.R. 2005. Ascidians from Bocas del Toro, Panama. I. Biodiversity. Caribbean Journal of Science, 41(3): 600-612.
Rohn S., Rawel H.M., Kroll J. 2002. Inhibitory effects of plant phenols on the activity of selected enzymes. Journal of Agricultural and Food Chemistry, 50(12): 3566-3571.
Safamansouri H., Nikan M., Amin G., Sarkhail P., Gohari A.R., Kurepaz-Mahmoodabadi M., Saeidnia S. 2014. α-Amylase inhibitory activity of some traditionally used medicinal species of Labiatae. Journal of Diabetes and Metabolic Disorders, 13(1): 1-5.
Sarhadizadeh N., Afkhami M., Ehsanpour M. 2014. Evaluation of antibacterial, antifungal and cytotoxic agents of Ascidian Phallusia nigra (Savigny, 1816) from Persian Gulf. European Journal of Experimental Biology, 4(1): 250-253.
Shobana S., Sreerama Y.N., Malleshi N. G. 2009. 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, 115(4): 1268-1273.
Shukla R.K., Painuly D., Shukla A., Singh J., Porval A., Vats S. 2014. In vitro biological activity and total phenolic content of Morus nigra seeds. Journal of Chemical and Pharmaceutical Research, 6(11): 200-210.
Sivashanmugam T., Muthukrishnan S., Umamaheswari M., Asokkumar K., Subhadradevi V., Jagannath P., Madeswaran A. 2013. Discovery of potential cholesterol esterase inhibitors using in silico docking studies. Bangladesh Journal of Pharmacology, 8(3): 223-229.
Tiwari S.P., Srivastava R., Singh C.S., Shukla K., Singh R.K., Singh P., Singh R., Singh N.L., Sharma R. 2015. Amylases: an overview with special reference to alpha amylase. Journal of Global Biosciences, 4(1): 1886-1901.
Vandepas L.E., Oliveira L.M., Lee S. S., Hirose E., Rocha R.M., Swalla B.J. 2015. Biogeography of Phallusia nigra: is it really black and white?. The Biological Bulletin, 228(1): 52-64.
Wickramaratne M.N., Punchihewa J.C., Wickramaratne D.B.M. 2016. In-vitro alpha amylase inhibitory activity of the leaf extracts of Adenanthera pavonina. BMC complementary and alternative medicine, 16(1): 1-5.
World Health Organization. WHO global strategy on diet, physical activity and health: European regional consultation meeting report. 2003.
Wu X., Ruan Y., Chen T., Yu Z., Huo D., Li X., Wu F., Jiang X., Ren C. 2020. First echinoderm alpha-amylase from a tropical sea cucumber (Holothuria leucospilota): Molecular cloning, tissue distribution, cellular localization and functional production in a heterogenous E. coli system with codon optimization. PloS One, 15(9): 1-18.
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