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

Česká verzia

Authors: Slavomír Kurhajec; Aleš Franc
Published in the journal: Čes. slov. Farm., 2019; 68, 148-156
Category: Přehledy a odborná sdělení

Summary

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

Zdroje

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.

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.

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.

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.

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.

7. Boehlke C., Zierau O., Hannig C. Salivary amylase – the enzyme of unspecialized euryphagous animals. Arch. Oral. Biol. 2015; 60, 1162–1176.

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.

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.

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.

11. Laube H. Acarbose. Clin. Drug Investig. 2002; 22, 141–156.

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.

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.

14. Kuhlmann J., Pils J. Oral antidiabetics. Berlin: Springer 1996.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

35. Darvesh A., Aggarwal B., Bishayee A. Curcumin and liver cancer: a review. Curr. Pharm. Biotechnol. 2012; 13, 218–228.

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.

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.

38. Pusztai A., Bardocz S. Lectins: biomedical perspectives. London: Tylor & Francis 1995.

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.

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.

41. le Berre-Anton V., Bompard-Gilles C., Payan F., Rouge P. Characterization and functional properties of the α-amylase inhibitor (α-AI) from kidney bean (Phaseolus vulgaris) seeds. BBA. Prot. St. 1997; 1343(1), 31–40.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.