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Inhibitory effects of extractives from leaves of Morus alba on human and rat small intestinal disaccharidase activity

Published online by Cambridge University Press:  08 March 2007

Tsuneyuki Oku*
Graduate School of Human Health Science, Siebold University of Nagasaki, Nagasaki, Japan
Mai Yamada
Tsusima Health Center of Nagasaki Prefecture, Japan
Mariko Nakamura
Graduate School of Human Health Science, Siebold University of Nagasaki, Nagasaki, Japan
Naoki Sadamori
Graduate School of Human Health Science, Siebold University of Nagasaki, Nagasaki, Japan
Sadako Nakamura
Graduate School of Human Health Science, Siebold University of Nagasaki, Nagasaki, Japan Graduate School of Biomedical Sciences, Nagaski University, Nagaski, Japan
*Corresponding author: Dr Tsuneyki Oku, fax +81 95 813 5211, email
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The inhibitory effect on human and rat intestinal disaccharidase by the extractive from the leaves ofMorus alba (ELM) containing 0·24% 1-deoxynojirimycin equivalent and its inhibitory activities were investigated by the modified Dahlqvist method. In the presence of 1000-fold diluted ELM solution, the sucrase activity of four human samples was inhibited by 96% and that of maltase and isomaltase by 95 and 99 %, respectively. The activities of trehalase and lactase were inhibited by 44 and 38 %, respectively. The human disaccharidase activities varied from sample to sample because the samples were obtained from different resected regions after surgery. However, the ratio of the inhibitory effect for sucrase, maltase, isomaltase, trehalase and lactase was very similar among the four samples, and also that of resembled rat intestinal disaccharides. The inhibitory constant of the 1-deoxynojirimycin equivalent for sucrase, maltase and isomaltase was 2·1× 10−4, 2·5 × 10−4 and 4·5 10−4μM, respectively, and these inhibitory activities were shown, using rat brush border membrane vesicles, to be competitive. These results demonstrate that digestion is inhibited when an appropriate amount of ELM is orally ingested with sucrose or polysaccharide in man. When ELM was orally administered in a sucrose solution to fasted rats, the elevation in blood glucose was significantly suppressed, depending on the concentration of ELM given. These results suggest that ELM could be used as an ingredient in health foods and in foods that help to prevent diabetes.

Research Article
Copyright © The Nutrition Society 2006


Asano, N, Oseki, K, Kizu, H& Matsui, KNitrogen-in-ring pyranoses: structural basis of inhibition of mammalian glycosidases. J Med Chem(1994a) 37, 37013706.CrossRefGoogle ScholarPubMed
Asano, N, Oseki, K, Kizu, H& Matsui, KN-containing sugars fromMorus albaand their glycosidase inhibitory activities. Carbohydr Res(1994b) 259, 243255.CrossRefGoogle Scholar
Bjarnason, I, Batt, R, Catt, S, Macpherson, AMaxton, D& Menzies, ISEvaluation of differential disaccharide excretion in urine for non-invasive investigation of altered intestinal disaccharidase activity caused by a-glucosidase inhibition, primary hypolactasia, and celiac disease. Gut 1996, 39, 374381.Google Scholar
Bradford, MMA rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976 72, 248258.CrossRefGoogle ScholarPubMed
Dahlqvist, AMethod of assay of intestinal disaccharidases. Anal Biochem 1964 7, 1825.CrossRefGoogle ScholarPubMed
Dehghan-Kooshkghazi, M& Mathers, JCStarch digestion, large-bowel fermentation and intestinal mucosal cell proliferation in rats treated with the ∝;-glucosidase inhibitor acarbose. Br J Nutr 2004 91, 357365.CrossRefGoogle ScholarPubMed
Dong, W, Jespersen, T, Blos, M, Skrydstrup, T& Sierks, MREvaluation of isofagomine and its derivatives as potent glycosidase inhibitor. Biochemistry 1996 35, 27882795.CrossRefGoogle Scholar
Drent, ML, Tollefsen, ATM, van Heusden, FHJA, Hoenderdos, EBM, Jonker, JJC& van der Veen, EADose-dependent efficacy of miglitol, an a-glucosidase inhibitor, in type 2 diabetic patients on diet alone: results of a 24-weeks double-blind placebo-controlled study. Diab Nutr Metab 2002 15, 152159.Google Scholar
Fuhrmann, U, Bause, E& Ploegh, HInhibitors of oligosaccharide processing. Biochim Biophys Acta 1985 825, 95110.Google Scholar
Holt, PP, Atillasoy, E, Lindenbaum Ho, JB, Lupton, JRMcMahon, D& Moss, SFEffects of acarbose on fecal nutrients, colonic pH, and short-chain fatty acids and rectal proliferative indices. Metabolism 1996 45, 11791187.CrossRefGoogle ScholarPubMed
Katsilambros, N, Philippides, PH, Toskas, A, Protopapas, J, Frangaki, D, Marangos, M, Siskoudis, PAnastasopoulou Xefteri, KH& Hillebrand, IA double-blind study on the efficacy and tolerance of a new a-glucosidase inhibitor in type-2 diabetics. Drug Res 1986 36, 11361138.Google Scholar
Kessler, M, Acuto, O, Strelli, C, Murer, H, Muller, MN, & Semenza, GA modified procedure for the rapid preparation of efficiently transporting vesicles from small intestinal brush border membranes. Biochem Biophys Acta 1978 506, 136154.CrossRefGoogle ScholarPubMed
Kimura, M, Chen, FJ, Nakashima, N, Kimura, I, Asano, N& Koya, SAntihyperglycemic effects on N-containing sugars derived from mulberry leaves in streptozocin induced diabetic mice. J Traditional Med 1995 12, 214219.Google Scholar
Mazzaferro, EM, Greco, DS, Turner, AS& Fettman, MJof ferine diabetes mellitus using an a-glucosidase inhibitor and diet. Feline Med Surg 2003 5, 183189.CrossRefGoogle Scholar
Miyahara, C, Miyazawa, M, Satoh, S, Sakai, A& Mizusaki, SInhibitory effects of mulberry leaf extract on postprandial hyperglycemia in normal rats. J Nutr Sci Vitaminol 2004 50, 161164.Google Scholar
Miyahara, C, Satoh, S, Miyazawa, M, Horiguchi, Y, Shimizu, A& Harada, MAntihyperglycemic effects of mulberry leaves in spontaneous diabetic rats. A report of a joint project on functional food materials (Kanagawa Prefecture) 1996 2, 5259.Google Scholar
Miyazawa, M, Miyahara, T, Sato, S& Sakai, ANinety-day dietary toxicity study of mulberry leaf extract in rats. Jpn J Food Hyg 2003 44, 191197[in Japanese].CrossRefGoogle ScholarPubMed
Oku, T, Konoshi, F& Hosoya, N\Mechanism of inhibitory effect of unavailable carbohydrate on intestinal calcium absorption. J Nutr 1982 112, 410415.CrossRefGoogle ScholarPubMed
Raimbaud, E, Buleon, A& Perez, S\Molecular modeling of acarviosine, the pseudo-disaccharide moiety of acarbose, and other inhibitors of a-amylases. Carbohydr Res 1992 227, 351363.Google Scholar
Taylor, RH, Barker, HM, Bowey, EA& Canfield, JERegulation of the absorption of dietary carbohydrate in man by two glycosidase inhibitors. Gut 1986 27, 14711478.Google Scholar
Trinder, P. Determination of blood glucose using an oxidaseperoxidase system with a non-carcinogenic chromogen. J Clin Pathol 1969 22, 158161.CrossRefGoogle ScholarPubMed
Yasuda, K, Shimowada, K, Uno, M, Odaka, H, Adachi, T& Shihara, NLong-term therapeutic effects of voglibose, a potent intestinal a-glucosidase inhibitor, in spontaneous diabetic GK rats. Diabetes Res Clin Pract 2003 59, 113122.Google Scholar