An Evidence-Based Systematic Review of Amylase Inhibitors by the Natural Standard Research Collaboration

REFERENCES

• Bays HE. Current and investigational antiobesity agents and obesity therapeutic treatment targets. Obes Res. 2004;12(8):1197–1211.
   Google Scholar
• Bernhard, WR, Somerville CR. Coidentity of putative amylase inhibitors from barley and finger millet with phospholipid transfer proteins inferred from amino acid sequence homology. Arch Biochem Biophys. 1989;269(2):695–697.
   Google Scholar
• Boivin M, Flourie B, Rizza RA, Go VL, DiMagno EP. Gastrointestinal and metabolic effects of amylase inhibition in diabetics. Gastroenterology. 1988;94(2):387–394.
   Google Scholar
• Boivin M, Zinsmeister AR, Go VL, DiMagno EP. Effect of a purified amylase inhibitor on carbohydrate metabolism after a mixed meal in healthy humans. Mayo Clin Proc. 1987;62(4):249–255.
   PubMed Web of Science ®Google Scholar
• Bo-Linn GW, Santa Ana CA, Morawski SG, Fordtran JS. Starch blockers—their effect on calorie absorption from a high-starch meal. N Engl J Med. 1982 (December 2);307(23):1413–1416.
   PubMed Web of Science ®Google Scholar
• Brugge WR, Rosenfeld MS. Impairment of starch absorption by a potent amylase inhibitor. Am J Gastroenterol. 1987;82(8):718–722.
   Google Scholar
• Buse J. Combining insulin and oral agents. Am J Med. 2000 (April 17);108(Suppl 6a):23S–32S.
   PubMedGoogle Scholar
• Carlson GL, Li BU, Bass P, Olsen WA. A bean alpha-amylase inhibitor formulation (starch blocker) is ineffective in man. Science. 1983 (January 28);219(4583):393–395.
   Google Scholar
• Celleno L, Tolaini MV, D’Amore A, Perricone NV, Preuss HG. A Dietary supplement containing standardized Phaseolus vulgaris extract influences body composition of overweight men and women. Int J Med Sci. 2007;4(1):45–52.
   PubMedGoogle Scholar
• Chokshi D. Toxicity studies of Blockal, a dietary supplement containing Phase 2 Starch Neutralizer (Phase 2), a standardized extract of the common white kidney bean (Phaseolus vulgaris). Int J Toxicol. 2006;25(5):361–371.
   Google Scholar
• Chokshi D. Subchronic oral toxicity of a standardized white kidney bean (Phaseolus vulgaris) extract in rats. Food Chem Toxicol. 2007;45(1):32–40.
   PubMed Web of Science ®Google Scholar
• Choudhury A, Maeda K, Murayama R, DiMagno EP. Character of a wheat amylase inhibitor preparation and effects on fasting human pancreaticobiliary secretions and hormones. Gastroenterology. 1996;111(5):1313–1320.
   PubMed Web of Science ®Google Scholar
• Chougule NP, Giri AP, Hivrale VK, Chhabda PJ, Kachole MS. Identification of amylase inhibitor deficient mutants in pigeonpea (Cajanus cajan (L.) Millisp.). Biochem Genet. 2004;42(5–6):165–180.
   Google Scholar
• Dojczew D, Andrzejczuk-Hybel J, Kaczkowski J. The protein inhibitors of amylases and peptidases isolated from cereal grains. Nahrung. 1986;30(3–4):275–279.
   Google Scholar
• Garrow JS, Scott PF, Heels S, Nair KS, Halliday D. A study of “starch blockers” in man using 13C-enriched starch as a tracer. Hum Nutr Clin Nutr. 1983;37(4):301–305.
   Google Scholar
• Giri AP, Kachole MS. Amylase inhibitors of pigeonpea (Cajanus cajan) seeds. Phytochemistry. 1998;47(2):197–202.
   PubMed Web of Science ®Google Scholar
• Grossi de Sa MF, Chrispeels MJ. Molecular cloning of bruchid (Zabrotes subfasciatus) alpha-amylase cDNA and interactions of the expressed enzyme with bean amylase inhibitors. Insect Biochem Mol Biol. 1997;27(4):271–281.
   Google Scholar
• Gwynn JP, Douglas CW. Comparison of amylase-binding proteins in oral streptococci. FEMS Microbiol Lett. 1994 (December 15);124(3):373–379.
   Google Scholar
• Hansen WE, Schulz G. Soluble and bound amylase inhibitors in guar and other dietary roughage. Beitr Infusionther Klin Ernahr. 1983;12:144–150.
   Google Scholar
• Hollenbeck CB, Coulston AM, Quan R, Becker TR, Vreman HJ, Stevenson DK, Reaven GM. Effects of a commercial starch blocker preparation on carbohydrate digestion and absorption: in vivo and in vitro studies. Am J Clin Nutr. 1983;38(4):498–503.
   Google Scholar
• Jadad AR, Moore RA, Carroll D, Jenkinson C, Reynolds DJ, Gavaghan DJ, McQuay HJ. Assessing the quality of reports of randomized clinical trials: is blinding necessary? Controlled Clin Trials. 1996;17(1):1–12.
   PubMedGoogle Scholar
• Kataoka K, DiMagno EP. Effect of prolonged intraluminal alpha-amylase inhibition on eating, weight, and the small intestine of rats. Nutrition. 1999;15(2):123–129.
   Google Scholar
• Koike D, Yamadera K, DiMagno EP. Effect of a wheat amylase inhibitor on canine carbohydrate digestion, gastrointestinal function, and pancreatic growth. Gastroenterology. 1995;108(4):1221–1229.
   PubMedGoogle Scholar
• Lankisch M, Layer P, Rizza RA, DiMagno EP. Acute postprandial gastrointestinal and metabolic effects of wheat amylase inhibitor (WAI) in normal, obese, and diabetic humans. Pancreas. 1998;17(2):176–181.
   Google Scholar
• Layer P, Carlson GL, DiMagno EP. Partially purified white bean amylase inhibitor reduces starch digestion in vitro and inactivates intraduodenal amylase in humans. Gastroenterology. 1985;88(6):1895–1902.
   PubMed Web of Science ®Google Scholar
• Layer P, Zinsmeister AR, DiMagno EP. Effects of decreasing intraluminal amylase activity on starch digestion and postprandial gastrointestinal function in humans. Gastroenterology. 1986;91(1):41–48.
   PubMed Web of Science ®Google Scholar
• Liener IE, Donatucci DA, Tarcza JC. Starch blockers: a potential source of trypsin inhibitors and lectins. Am J Clin Nutr. 1984;39(2):196–200.
   Google Scholar
• Macri A, Parlamenti R, Silano V, Valfre, F. Adaptation of the domestic chicken, Gallus domesticus, to continuous feeding of albumin amylase inhibitors from wheat flour as gastro-resistant microgranules. Poult Sci. 1977;56(2):434–441.
   Google Scholar
• Maeda K, Hase T, Matsubara H. Complete amino acid sequence of an alpha-amylase inhibitor in wheat kernel. Biochim Biophys Acta. 1983 (February 28);743(1):52–57.
   Google Scholar
• Marshall JJ, Lauda CM. Purification and properties of phaseolamin, an inhibitor of alpha-amylase, from the kidney bean, Phaseolus vulgaris. J Biol Chem. 1975 (October 25);250(20):8030–8037.
   PubMed Web of Science ®Google Scholar
• McCue PP, Shetty K. Inhibitory effects of rosmarinic acid extracts on porcine pancreatic amylase in vitro. Asia Pac J Clin Nutr. 2004;13(1):101–106.
   PubMed Web of Science ®Google Scholar
• Morton RL, Schroeder HE, Bateman KS, Chrispeels MJ, Armstrong E, Higgins TJ. Bean alpha-amylase inhibitor 1 in transgenic peas (Pisum sativum) provides complete protection from pea weevil (Bruchus pisorum) under field conditions. Proc Natl Acad Sci USA. 2000 (April 11);97(8):3820–3825.
   PubMed Web of Science ®Google Scholar
• Mulimani VH, Supriya D. Alpha amylase inhibitors in sorghum (Sorghum bicolor). Plant Foods Hum Nutr. 1993;44(3):261–266.
   Google Scholar
• Rekha MR, Padmaja G. Alpha-amylase inhibitor changes during processing of sweet potato and taro tubers. Plant Foods Hum Nutr. 2002;57(3–4):285–294.
   Google Scholar
• Savelkoul FH, Van Der Poel AF, Tamminga S. The presence and inactivation of trypsin inhibitors, tannins, lectins and amylase inhibitors in legume seeds during germination. A review. Plant Foods Hum Nutr. 1992;42(1):71–85.
   PubMed Web of Science ®Google Scholar
• Shekib LA, el Iraqui SM, Abo-Bakr TM. Studies on amylase inhibitors in some Egyptian legume seeds. Plant Foods Hum Nutr. 1988;38(4):325–332.
   PubMed Web of Science ®Google Scholar
• Shiau YS, Horng SB, Chen CS, Huang PT, Lin C, Hsueh YC, Lou KL. Structural analysis of the unique insecticidal activity of novel mungbean defensin VrD1 reveals possibility of homoplasy evolution between plant defensins and scorpion neurotoxins. J Mol Recognit. 2006;19(5):441–450.
   Google Scholar
• Singh U. Antinutritional factors of chickpea and pigeonpea and their removal by processing. Plant Foods Hum Nutr. 1988;38(3):251–261.
   PubMed Web of Science ®Google Scholar
• Strumeyer DH, Fisher BR. Automated assay of alpha-amylase inhibitor proteins by continuous flow analysis. Anal Biochem. 1983 (April 15);130(2):506–513.
   Google Scholar
• Strumeyer DH, Malin MJ. Identification of the amylase inhibitors from seeds of Leoti sorghum. Biochim Biophys Acta. 1969 (September 2);184(3):643–645.
   Google Scholar
• Thom E. A randomized, double-blind, placebo-controlled trial of a new weight-reducing agent of natural origin. J Int Med Res. 2000;28(5):229–233.
   Google Scholar
• Titarenko E, Chrispeels MJ. cDNA cloning, biochemical characterization and inhibition by plant inhibitors of the alpha-amylases of the Western corn rootworm, Diabrotica virgifera virgifera. Insect Biochem Mol Biol. 2000;30(10):979–990.
   Google Scholar
• Tormo MA, Gil-Exojo I, Romero de Tejada, Campillo JE. Hypoglycaemic and anorexigenic activities of an alpha-amylase inhibitor from white kidney beans (Phaseolus vulgaris) in Wistar rats. Br J Nutr. 2004;92(5):785–790.
   Google Scholar
• Udani J, Hardy M, Madsen DC. Blocking carbohydrate absorption and weight loss: a clinical trial using Phase 2 brand proprietary fractionated white bean extract. Altern Med Rev. 2004;9(1):63–69.
   Google Scholar
• Umoren J, Kies C. Commercial soybean starch blocker consumption: impact on weight gain and on copper, lead and zinc status of rats. Plant Foods Hum Nutr. 1992;42(2):135–142.
   Google Scholar
• Valencia A, Bustillo AE, Ossa GE, Chrispeels MJ. Alpha-amylases of the coffee berry borer (Hypothenemus hampei) and their inhibition by two plant amylase inhibitors. Insect Biochem Mol Biol. 2000;30(3):207–213.
   Google Scholar
• Yamaguchi H, Funaoka H, Iwamoto H. Structures of sugar chains of the subunits of an alpha-amylase inhibitor from Phaseolus vulgaris white kidney beans. J Biochem. 1992;111(3):388–395.
   Google Scholar
• Young NM, Thibault P, Watson DC, Chrispeels MJ. Post-translational processing of two alpha-amylase inhibitors and an arcelin from the common bean, Phaseolus vulgaris. FEBS Lett. 1999 (March 5);446(1):203–206.
   Google Scholar
• Zoccatelli G, Dalla Pellegrina C, Mosconi S, Consolini M, Veneri G, Chignola R, Peruffo A, Rizzi C. Full-fledged proteomic analysis of bioactive wheat amylase inhibitors by a 3-D analytical technique: identification of new heterodimeric aggregation states. Electrophoresis. 2007;28(3):460–466.
   Google Scholar