Assessment of In-Vitro inhibitory effect of khaya tea infusion on porcine pancreatic lipase activity

Paper Details

Research Paper 15/03/2015
Views (741)
current_issue_feature_image
publication_file

Assessment of In-Vitro inhibitory effect of khaya tea infusion on porcine pancreatic lipase activity

Mache André Gilles, Ngando Ebongue Georges Frank, Léopold Tatsadjieu, Njintang Yanou Nicolas, Carl Moses F. Mbofung
Int. J. Biosci. 6(6), 1-9, March 2015.
Copyright Statement: Copyright 2015; The Author(s).
License: CC BY-NC 4.0

Abstract

The inhibition of digestive lipases is a widely studied mechanism for the determination of the potential efficacy of natural products as anti-obesity agents. In this regard, the use of natural products might be an excellent alternative strategy for the development of safe and effective anti-obesity drugs that lack the unpleasant side effects of existing chemical drugs. The aim of this study was to assess the potential effect of Khaya tea in the treatment of obesity through the evaluation of its in vitro inhibitory effects on porcine pancreatic lipase activity. Extract was obtained by infusion of powder in water 4g/150 ml at 95°C for 10 min and was subjected to chemical analysis and kinetics studies. The in vitro inhibitory effect of Khaya tea on lipase activity was studied by assessing porcine pancreatic lipase activities at varying concentrations of khaya tea extract (0, 1, 2, 3, 4, 5 mg/ml). Results showed that Khaya tea induced a competitive inhibition (85±2%) of the porcine pancreatic lipase activity in the hydrolysis of substrate emulsified with gum arabic : I.C (inhibition Concentration)50 = 0.96 ± 0.03 mg of Khaya tea /ml. These in vitro inhibition results suggest that Khaya tea could be a potential therapeutic alternative in the treatment of obesity caused by fat-rich diets.

Aoubala M, De la Fourniere L, Douchet I, Abousalham A, Daniel C, Hirn M, Gargouri Y, Verger R, De Caro A. 1995. Human pancreatic lipase. Importance of the hinge region between the two domains, as revealed by monoclonal antibodies. Journal of Biological Chemistry 270, 3932–3937. http://www.jbc.org/content/270/8/3932.full

Berit S, Dieterhartmann Bengt B, Kenilsson 2002. Degree of in vivo inhibition of human gastric and pancreatic lipases by Orlistat (Tetrahydrolipstatin, THL) in the stomach and small intestine. Clinical Nutrition, Volume 21(5), 395–402. http://dx.doi.org/10.1054/clnu.2002.0565

Birari RB, Bhutani KK. 2007. Pancreatic lipase inhibitors from natural sources: unexplored potential. Drug Discovery. Today 12, 879-889. http://www.ncbi.nlm.nih.gov/pubmed/17933690/

Carriere F, Renou C, Ransac S, Lopez V, De Caro J, Ferrato F, De Caro A, Fleury A, Sanwald-Ducray P, Lengsfeld H, Beglinger C, Hadvary P, Verger R, Laugier R. 2001. Inhibition of gastrointestinal lipolysis by Orlistat during digestion of test meals in healthy volunteers. American Journal of Physiology Gastrointestinal and Liver Physiology 281(1), G16-28. http://ajpgi.physiology.org/content/ajpgi/281/1/G16

Cudrey C, Van TH, Gargouri Y, Verger R. 1993. Inactivation of pancreatic lipases by amphiphilic reagents 5-(dodecyldithio)-2-nitrobezoic acid and tetrahydrolipstatin. Dependence upon partitioning between micellar and oil phases. Biochemistry 32, 13800–13808. http://dx.doi.org/10.1021/bi00213a008

Fernanda M, Tatiana M. Noso, Viviane B. Porto, Alline C, Alessandra G, Deborah HM, Bastos, Marcelo L. Ribeiro, Patrícia de O. Carvalho. 2009. Maté Tea inhibits in vitro pancreatic lipase activity and has hypolipidemic effect on high-fat diet-induced obese mice. Integrative physiology 18, 42–47. http://onlinelibrary.wiley.com/doi/10.1038/oby.200 9.189

Griffiths DW. 1986. The inhibition of digestive enzymes by polyphenolic compounds. Advances in Experimental Medicine and Biology 199, 509–516. http://dx.doi.org/10.1007/s13228-012-0022-0

Han LK, Kimura Y, Kawashima M. 2001. Antiobesity effects in rodents of dietary tea saponin, a lipase inhibitor. International Journal of Obesity and Related Metabolic Disorders 25, 1459-1464. http://www.nature.com/ijo/journal/v25/n10/full/08 01747a.html

Juhel C, Armand M, Pafumi Y, Rosier C, Vandermander J, Lairon D. 2000. Green tea extract (AR25) inhibits lipolysis of triglycerides in gastric and duodenal medium in vitro. Journal of Nutritional Biochemistry 11, 45–51. http://dx.doi.org/10.1016/S0955-2863(99)00070-4

Khalid SA, Friedrichsen GM, Kharazmi A, Theander TG, Olsen CE, Nakatani M, Abdelgaleil SA, Kassem SM, Takezak K, Okamura H, Iwagawa T, Doe M. 2002. Three new modified limonoids from Khaya senegalensis. Journal of Natural Products 65, 196-216.

Krebs M, Stingl H, Noworny P, Weghuber D, Bishof M, Waldhausl W, Rodeu M. 2000. Prevention of in vitro lipolysis by tetrahydrolipstatin. Clinical Chemistry 46, 950–954. http://www.ncbi.nlm.nih.gov/pubmed/10894838

Kumar A, Chauhan GS. 2010. Extraction and characterization of pectin from apple pomace and its evaluation as lipase (steapsin) inhibitor. Carbohydrate Polymers 82, 454–459.

Masaaki N, Yuko F, Sumio A, Yoshiko T, Takashi I, Hiroshi S, Tohru M, Fumio H,Moreau H, Moulin A, Gargouri Y, Noël J-P, Verger R. 1991. Inactivation of gastric and pancreatic lipases by diethyl p-nitrophenyl phosphate. Biochemistry 30, 1037–1041. http://dx.doi.org/10.1021/bi00218a022

Mukherjee M. 2003. Human digestive and metabolic lipases a brief review. Journal of Molecular Catalysis B Enzymatic 22, 369–376.

Nakai M, Fukui Y, Asami S, Toyoda-Ono Y, Iwashita T, Shibata H, Mitsunaga T, Hashimoto F, Kiso Y. 2005. Inhibitory effects of oolong tea polyphénols on pancreatic lipase in vitro. Journal of Agricultural and Food Chemistry 53, 4593–4598. http://dx.doi.org/10.1021/jf047814

Pieroni G, Gargouri Y, Sarda L, Verger R. 1990. Interactions of lipases with lipid monolayers. Facts and  questions.  Advances  in  Colloid  and  Interface Science 32, 341–378. http://dx.doi.org/10.1016/0001-8686(90)80023-S

Sarda L, Desnuelle P. 1958. Action de la lipase pancréatique sur les esters en émulsion. Biochimica et Biophysica Acta 30, 513-512. http://www.ncbi.nlm.nih.gov/pubmed/13618257

Zhi J, Mulligan T, Hauptman J. 1999. Long-term systemic exposure of Orlistat, a lipase inhibitor, and
its metabolites in obese patients. Journal of Clinical Pharmacoly 39, 41-46. http://dx.doi.org/10.1177/00912709922007543

Related Articles

Medicinal plants sold in Daloa markets: Traditional knowledge and Public health issues

Kouakou Yao Bertin, Kouakou Assoman Serge Alain, Kouame Yao Anicet Gervais, Malan Djah François, Bakayoko Adama, Int. J. Biosci. 27(2), 200-210, August 2025.

Agronomic performance and profitability of coffee wildlings using different soil media mixtures

Maribel L. Fernandez, Ricardo B. Casauay, Ronel A. Collado, Int. J. Biosci. 27(2), 189-199, August 2025.

Implications of aberrant glycosylation on age-related disease progression

Tahmid Ahmad Patwary, Mukramur Rahman, Md. Nafis Fuad Prottoy, Sayad Md. Didarul Alam, Int. J. Biosci. 27(2), 176-188, August 2025.

Design and development of solar powered water sprayer: A green technology innovation

Lorenzo V. Sugod, Int. J. Biosci. 27(2), 159-175, August 2025.

Knowledge, attitudes, practices, and social awareness regarding SARS-CoV-2 infection in the kyrgyz population in the post-pandemic period

Mirza Masroor Ali Beg, Haider Ali, Yahya Nur Ahmed, Yavuz Gunduz, Hafsa Develi, Tilekeeva UM, Int. J. Biosci. 27(2), 151-158, August 2025.

Tumor suppressing ability of myrtenal in DMBA-induced rat mammary cancer: A biochemical and histopathological evaluation

Manoharan Pethanasamy, Shanmugam M. Sivasankaran, Saravanan Surya, Raju Kowsalya, Int. J. Biosci. 27(2), 141-150, August 2025.

Assessing tree diversity in cashew plantations: Environmental and agronomic determinants in buffer zones of Mont Sangbé National Park, western Côte d’Ivoire

Kouamé Christophe Koffi, Kouakou Hilaire Bohoussou, Serge Cherry Piba, Naomie Ouffoue, Sylvestre Gagbe, Alex Beda, Adama Tondossama, Int. J. Biosci. 27(2), 122-133, August 2025.