JOURNAL OF THE CZECH PHARMACEUTICAL SOCIETY AND THE SLOVAK PHARMACEUTICAL SOCIETY

Čes. slov. farm. 2019, 68(4):148-156 | DOI: 10.36290/csf.2019.017

Plant α-amylase inhibitors and their effect on the utilization of polysaccharides contained in the diet

Slavomír Kurhajec1, Aleš Franc2,*
1 Department of Pharmacognosy and Botany, University of Veterinary Medicine and Pharmacy in Košice, Slovakia
2 Department of Pharmaceutics, Faculty of Pharmacy, University of Veterinary and Pharmaceutical Sciences, Brno, Czech Republic

Development of civilization diseases such as diabetes mellitus, metabolic syndrome or obesity, enforces the increasing effort to find new drugs, especially from natural sources. These include α-amylase inhibitors, which break down polysacharides into simple sugars in the body of a healthy person. As this cleavage affects the level of blood sugar, which is sought to be therapeutically influenced, there is a growing interest in these substances. This review maps the types of amylase inhibitors, including their natural resources.

Keywords: amylase inhibitors; α-amylase; inhibitors in plants; breakdown of starch

Received: July 7, 2019; Accepted: July 27, 2019; Published: April 1, 2019  Show citation

ACS AIP APA ASA Harvard Chicago Chicago Notes IEEE ISO690 MLA NLM Turabian Vancouver
Kurhajec S, Franc A. Plant α-amylase inhibitors and their effect on the utilization of polysaccharides contained in the diet. Čes. slov. farm. 2019;68(4):148-156. doi: 10.36290/csf.2019.017.
Download citation

References

  1. Bush D. S., Sticher L., Van Huystee R., Wagner D., Jones R. L. The calcium requirement for stability and enzymatic activity of two isoforms of barley aleurone alpha-amylase. J. Biol Chem. 1989; 32, 19392-19398. Go to original source...
  2. Suržin J., Ledvina M. Lekárska biochémia. Košice a Hradec Králové: Michal Vaško 2002.
  3. Preuss H. G. Bean amylase inhibitor and other carbohydrate absorption blockers: effects on diabesity and general health. J. Am. Coll. Nutr. 2009; 28, 266-276. Go to original source... Go to PubMed...
  4. Perry G. H., Dominy N. J., Claw K. G., Lee A. S., Fiegler H., Redon R., Carter N. P. Diet and the evolution of human amylase gene copy number variation. Nat. Genet. 2007; 39, 1256. Go to original source... Go to PubMed...
  5. Tan K., Tesar C., Wilton R., Keigher L., Babnigg G., Joachimiak A. Novel α-glucosidase from human gut microbiome: substrate specificities and their switch. Faseb. J. 2010; 24, 3939-3949. Go to original source... Go to PubMed...
  6. Bush D. S., Sticher L., van Huystee R., Wagner D., Jones R. L. The calcium requirement for stability and enzymatic activity of two isoforms of barley aleurone alpha-amylase. J. Biol. Chem. 1989; 32, 19392-19398. Go to original source...
  7. Boehlke C., Zierau O., Hannig C. Salivary amylase - the enzyme of unspecialized euryphagous animals. Arch. Oral. Biol. 2015; 60, 1162-1176. Go to original source... Go to PubMed...
  8. Kim M. J., Lee S. B., Lee H. S., Lee S. Y., Baek J. S., Kim D., Park K. H. Comparative study of the inhibition of α-glucosidase, α-amylase, and cyclomaltodextrin glucanosyltransferase by acarbose, isoacarbose, and acarviosine - glucose. Arch. Biochem. Biophys. 1999; 371, 277-283. Go to original source... Go to PubMed...
  9. Mahmud T., Tornus I., Egelkrout E., Wolf E., Uy C., Floss H. G., Lee S. Biosynthetic studies on the α-glucosidase inhibitor acarbose in actinoplanes sp.: 2-epi-5-epi-valiolone is the direct precursor of the valienamine moiety. JACS 1999; 121, 6973-6983. Go to original source...
  10. Chiasson J. L., Josse R. G., Gomis R., Hanefeld M., Karasik A., Laakso M. Acarbose for prevention of type 2 diabetes mellitus: the stop-niddm randomised trial. Lancet 2002; 9323, 2072-2077. Go to original source... Go to PubMed...
  11. Laube H. Acarbose. Clin. Drug Investig. 2002; 22, 141-156. Go to original source...
  12. Truscheit E., Frommer W., Junge B., Müller L., Schmidt D. D., Wingender W. Chemistry and biochemistry of microbial α-glucosidase inhibitors. Angew. Chem. Int. Ed. Engl. 1981; 20, 744-761. Go to original source...
  13. Geng P., Qiu F., Zhu Y., Bai G. Four acarviosin-containing oligosaccharides identified from streptomyces coelicoflavus zg0656 are potent inhibitors of α-amylase. Carbohydr. Res. 2008; 343, 882-892. Go to original source... Go to PubMed...
  14. Kuhlmann J., Pils J. Oral antidiabetics. Berlin: Springer 1996. Go to original source...
  15. Agnieszka S. Food biofortification technologies. Boca Raton, Florida: CRC Press 2017.
  16. Barbosa A. E., Albuquerque É. V., Silva M. C., Souza D. S., Oliveira-Neto O. B., Valencia A., Grossi-De-Sá M. F. α-amylase inhibitor-1 gene from Phaseolus vulgaris expressed in coffea arabica plants inhibits α-amylases from the coffee berry borer pest. BMC Biotechnol. 2010; 10, 44. Go to original source... Go to PubMed...
  17. Jbilou R., Amri H., Bouayad N., Ghailani N., Ennabili A., Sayah F. Insecticidal effects of extracts of seven plant species on larval development, α-amylase activity and offspring production of Tribolium castaneum. Bioresour. Technol. 2008; 99, 959-964. Go to original source... Go to PubMed...
  18. Sales P. M., Souza P. M., Simeoni L. A., Magalhães P. O., Silveira D. α-amylase inhibitors: a review of raw material and isolated compounds from plant source. J. Pharm. Pharm. Sci. 2012; 15, 143-183. Go to original source... Go to PubMed...
  19. Nagaraj R. H., Pattabiraman T. N. Purification and properties of an α-amylase inhibitor specific for human pancreatic amylase from proso (panicium miliaceum) seeds. J. Biosci. 1985; 7, 257-268. Go to original source...
  20. Franco O. L., Rigden D. J., Melo F. R., Grossi-de-Sá M. F. Plant α-amylase inhibitors and their interaction with insect α-amylases: structure, function and potential for crop protection. Eur. J. Biochem. 2002; 269, 397-412. Go to original source... Go to PubMed...
  21. Tadera K., Minami Y., Takamatsu K., Matsuoka T. Inhibition of α-glucosidase and α-amylase by flavonoids. J. Nutr. Sci. Vitaminol. 2006; 52, 149-153. Go to original source... Go to PubMed...
  22. Lo Piparo, E., Scheib H., Frei N., Williamson G., Grigorov M., Chou C. J. Flavonoids for controlling starch digestion: structural requirements for inhibiting human α-amylase. J. Med. Chem. 2008; 51, 3555-3561. Go to original source... Go to PubMed...
  23. Buchtová E., Šturdíková M. Mikrobiálne produkované inhibítory hydroláz a ich terapeutický potenciál. Chem. Listy 2013; 107, 30-36.
  24. Kim Y. M., Wang M. H., Rhee H. I. A novel α-glucosidase inhibitor from pine bark. Carbohydr. Res. 2004; 339, 715-717. Go to original source... Go to PubMed...
  25. Shpatov A. V., Popov S. A., Salnikova O. I., Kukina T. P., Shmidt E. N., Um B. H. Composition and bioactivity of lipophilic metabolites from needles and twigs of korean and siberian pines (Pinus koraiensis siebold & Pucc. and Pinus sibirica du tour). Chem. Biodivers 2017; 14, e1600203. Go to original source... Go to PubMed...
  26. Arabshahi-D S., Devi D. V., Urooj A. Evaluation of antioxidant activity of some plant extracts and their heat, ph and storage stability. Food Chem. 2007; 100, 1100-1105. Go to original source...
  27. Martin J., Dušek, J. Inhibice α-amylázy a α-glukosidázy přírodními látkami. Prakt. Lékárenství 2009; 5, 92-95.
  28. Zheng H. Z., Hwang I.. W., Kim, S. K., Lee S. H., Chung S. K. Optimization of carbohydrate-hydrolyzing enzyme aided polyphenol extraction from unripe apples. J. Korean Soc. Appl. Biol. Chem. 2010; 53, 342-350. Go to original source...
  29. Ujwala T. K., Tomy S., Celine S., Chander J. S. J. U., Udaya S. J. A systematic review of some potential anti-diabetic herbs used in india characterized by its hypoglycemic activity. Int. J. Pharm. Sci. Res. 2015; 12, 4940-4957.
  30. Kania M., Baraniak J. Wybrane właściwości biologiczne i farmakologiczne zielonej herbaty (Camellia sinensis L. O. Kuntze). Post. Fitoter. 2011; 1, 34-40.
  31. Jiménez-Ferrer E., Alarcón-Alonso J., Aguilar-Rojas A., Zamilpa A., Tortoriello J., Herrera-Ruiz M. Diuretic effect of compounds from hibiscus sabdariffa by modulation of the aldosterone activity. Planta Med. 2012; 78, 1893-1898. Go to original source... Go to PubMed...
  32. Alarcon-Aguilar F. J., Zamilpa A., Perez-Garcia M. D., Almanza-Perez J. C., Romero-Nunez E., Campos-Sepulveda E. A., Roman-Ramos R. Effect of hibiscus sabdariffa on obesity in msg mice. J. Ethnopharmacol. 2007; 114, 66-71. Go to original source... Go to PubMed...
  33. Mozaffari-Khosravi H., Jalali-Khanabadi B. A., Afkhami-Ardekani M., Fatehi F. Effects of sour tea (hibiscus sabdariffa) on lipid profile and lipoproteins in patients with type ii diabetes. J. Altern. Complement. Med. 2009; 15, 899-903. Go to original source... Go to PubMed...
  34. Chang H. C., Peng C. H., Yeh D. M., Kao E. S., Wang C. J. Hibiscus sabdariffa extract inhibits obesity and fat accumulation, and improves liver steatosis in humans. Food Funct. 2014; 5, 734-739. Go to original source... Go to PubMed...
  35. Darvesh A., Aggarwal B., Bishayee A. Curcumin and liver cancer: a review. Curr. Pharm. Biotechnol. 2012; 13, 218-228. Go to original source... Go to PubMed...
  36. Ponnusamy S., Zinjarde S., Bhargava S., Rajamohanan P. R., RaviKumar A. Discovering bisdemetoxycurcumin from curcuma longa rhizome as a potent small molecule inhibitor of human pancreatic α-amylase, a target for type-2 diabetes. Food Chem. 2012; 135, 2638-2642. Go to original source... Go to PubMed...
  37. Kalve N. D., Lomate P. R., Hivrale, V. K. A proteinaceous thermo labile α-amylase inhibitor from albizia lebbeck with inhibitory potential toward insect amylases. Arthropod Plant Interact. 2012; 6, 213-220. Go to original source...
  38. Pusztai A., Bardocz S. Lectins: biomedical perspectives. London: Tylor & Francis 1995. Go to original source...
  39. Fabre C., Causse H., Mourey L., Koninkx J., Rivière M., Hendriks H., Rougé P. Characterization and sugar-binding properties of arcelin-1, an insecticidal lectin-like protein isolated from kidney bean (Phaseolus vulgaris L. Cv. Raz-2) seeds. Biochem. J. 1998; 329, 551-560. Go to original source... Go to PubMed...
  40. Kluh I., Horn M., Hýblová J., Hubert J., Dolečková-Marešová L., Voburka Z., Mareš M. Inhibitory specificity and insecticidal selectivity of α-amylase inhibitor from Phaseolus vulgaris. Phytochem. 2005; 66, 31-39. Go to original source... Go to PubMed...
  41. Le Berre-Anton V., Bompard-Gilles C., Payan F., Rouge P. Characterization and functional properties of the α-amylase inhibitor (alpha;-AI) from kidney bean (Phaseolus vulgaris) seeds. BBA. Prot. St. 1997; 1343(1), 31-40. Go to original source... Go to PubMed...
  42. Bellincampi D., Camardella L., Delcour J. A., Desseaux V., D'Ovidio R., Durand A., Sǿrensen J. F. Potential physiological role of plant glycosidase inhibitors. Biochim. Biophys Acta Proteins Proteom. 2004; 1696, 265-274. Go to original source... Go to PubMed...
  43. Pusztai A., Grant, G., Duguid T., Brown, D. S., Peumans W. J., van Damme E. J., Bardocz S. Inhibition of starch digestion by α-amylase inhibitor reduces the efficiency of utilization of dietary proteins and lipids and retards the growth of rats. J. Nutr. 1995; 125, 1554-1562.
  44. Barrett M. L., Udani J. K. A proprietary alpha-amylase inhibitor from white bean (Phaseolus vulgaris): a review of clinical studies on weight loss and glycemic control. J Nutr. 2011; 10, 24. Go to original source... Go to PubMed...
  45. Kumar S., Verma A. K., Das M., Jain S. K., Dwivedi P. D. Clinical complications of kidney bean (Phaseolus vulgaris L.) Consumption. Nutrition 2013; 29, 821-827. Go to original source... Go to PubMed...
  46. Confalonieri M., Bollini R., Berardo N., Vitale A., Allavena A. Influence of phytohemagglutinin on the agronomic performance of beans (Phaseolus vulgaris L.). Plant Breeding 1992; 109, 329-334. Go to original source...
  47. Feng G. H., Richardson M., Chen M. S., Kramer K. J., Morgan T. D., Reeck G. R α-amylase inhibitors from wheat: amino acid sequences and patterns of inhibition of insect and human α-amylases. Insect Biochem. Mol. Biol. 1996; 26, 419-426. Go to original source... Go to PubMed...
  48. Celleno L., Tolaini M. V., D'Amore A., Perricone N. V., Preuss, H. G. A dietary supplement containing standardized Phaseolus vulgaris extract influences body composition of overweight men and women. Int. J. Med. Sci. 2007; 4, 45. Go to original source... Go to PubMed...
  49. Lu S., Deng P., Liu X., Luo J., Han R., Gu X., Patthy A. Solution structure of the major α-amylase inhibitor of the crop plant amaranth. J. Biol. Chem. 1999; 274, 20473-20478. Go to original source... Go to PubMed...
  50. Carugo O., Lu S., Luo J., Gu X., Liang S., Strobl S., Pongor S. Structural analysis of free and enzyme-bound amaranth α-amylase inhibitor: classification within the knottin fold superfamily and analysis of its functional flexibility. Protein Eng. 2001; 14, 639-646. Go to original source... Go to PubMed...
  51. Heidari R., Zareae S., Heidarizadeh M. Extraction, purification, and inhibitory effect of alpha-amylase inhibitor from wheat (Triticum aestivum var. Zarrin). Pakistan. J. Nutr. 2005; 4, 101-105. Go to original source...
  52. Strobl S., Maskos K., Wiegand G., Huber R., Gomis-Rüth F. X., Glockshuber R. A novel strategy for inhibition of α-amylases: yellow meal worm α-amylase in complex with the ragi bifunctional inhibitor at 2.5 å resolution. Struct. 1998; 6, 911-921. Go to original source... Go to PubMed...
  53. Wang J., Yang L., Zhao X., Li J., Zhang D. Characterization and phylogenetic analysis of allergenic tryp alpha amyl protein family in plants. J. Agric. Food. Chem. 2013; 62, 270-278. Go to original source... Go to PubMed...
  54. Franco O. L., Rigden D. J., Melo F. R., Bloch Jr, C., Silva C. P., Grossi-de-Sá M. F. Activity of wheat α-amylase inhibitors towards bruchid α-amylases and structural explanation of observed specificities. Eur. J. Biochem. 2000; 267, 2166-2173. Go to original source... Go to PubMed...
  55. Yamagata H., Kunimatsu K., Kamasaka H., Kuramoto T., Iwasaki T. Rice bifunctional α-amylase/subtilisin inhibitor: characterization, localization, and changes in developing and germinating seeds. Biosci. Biotechnol. Biochem. 1998; 62, 978-985. Go to original source... Go to PubMed...
  56. Nielsen P. K., Bønsager B. C., Fukuda K., Svensson B. Barley α-amylase/subtilisin inhibitor: structure, biophysics and protein engineering. BBA-Proteins. Proteom. J. 2004; 1696, 157-164. Go to original source... Go to PubMed...
  57. Liu J. J., Sturrock R., Ekramoddoullah A. K. The superfamily of thaumatin-like proteins: its origin, evolution, and expression towards biological function. Plant Cell Reports 2010; 29, 419-436. Go to original source... Go to PubMed...
  58. Batalia M. A., Monzingo A. F., Ernst S., Roberts W., Robertus J. D. The crystal structure of the antifungal protein zeamatin, a member of the thaumatin-like, pr-5 protein family. Nat. Struct. Mol. Biol. 1996; 3, 19. Go to original source... Go to PubMed...
  59. Colilla F. J., Rocher A., Mendez E. Γ-purothionins: amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm. FEBS Lett. 1990; 270, 191-194. Go to original source... Go to PubMed...
  60. Kotkar H. M., Sarate P. J., Tamhane V. A., Gupta V. S., Gir A. P. Responses of midgut amylases of helicoverpa armigera to feeding on various host plants. J. Insect Physiol. 2009; 55, 663-670. Go to original source... Go to PubMed...
  61. Mehrabadi M., Franco O. L., Bandani A. R. Plant proteinaceous alpha-amylase and proteinase inhibitors and their use in insect pest control. In new perspectives in plant protection. Intechopen. 2012; 11, 230-246. Go to original source...




Czech and Slovak Pharmacy

Madam, Sir,
please be aware that the website on which you intend to enter, not the general public because it contains technical information about medicines, including advertisements relating to medicinal products. This information and communication professionals are solely under §2 of the Act n.40/1995 Coll. Is active persons authorized to prescribe or supply (hereinafter expert).
Take note that if you are not an expert, you run the risk of danger to their health or the health of other persons, if you the obtained information improperly understood or interpreted, and especially advertising which may be part of this site, or whether you used it for self-diagnosis or medical treatment, whether in relation to each other in person or in relation to others.

I declare:

  1. that I have met the above instruction
  2. I'm an expert within the meaning of the Act n.40/1995 Coll. the regulation of advertising, as amended, and I am aware of the risks that would be a person other than the expert input to these sites exhibited


No

Yes

If your statement is not true, please be aware
that brings the risk of danger to their health or the health of others.