Novel isoforms of proteinaceous a-amylase inhibitor (a-AI) from seed extract of Albizia lebbeck

• Autorzy: Shaikh F K , Gadge P. P. , Shinde A. A. , Jaiwal B. V. , Shinde K. D. , Padul M. V. , Kachole M. S.
• Języki publikacji: EN

Abstrakty

EN

Proteinaceous inhibitors of digestive α-amylase occur naturally in leguminous seeds and find applications in agriculture and clinical studies. We have detected and isolated eight novel α-amylase inhibitor isoforms in the seed extract of Albizia lebbeck. They are designated as ALαAI- 1 to AL-αAI-8. These isoforms specifically inhibit human salivary a-amylase and porcine pancreatic α-amylase. The occurrence and profile of α-amylase inhibitor isoforms were revealed by 7 % native-PAGE containing 0.1 % starch. The apparent molecular weights of native bands of AL-αAIs were 97.4, 68.6, 61.0, 57.2, 56.0, 54.7, 51.1, and 47.7 kDa, respectively. Partial purification of potent a-amylase inhibitor was achieved using ammonium sulfate fractionation and gel filtration chromatography on G-100 Sephadex column followed by preparative gel electrophoresis. SDS-PAGE analysis of partially purified AL-αAI showed two polypeptide bands of *35.8 and *32.6 kDa. All these isoforms showed effective resistance to in vitro proteolysis by pepsin, trypsin, and chymotrypsin. These inhibitors are stable over a wide range of pH and temperature and have optimum activity at pH 7 and at 37 C. The finding and information obtained in the present investigation about novel isoforms of α-amylase inhibitors from A. lebbeck could be important and may find applications in clinical studies to modulate starch digestion and glycemic index.

• Wydawca: -
• Czasopismo: Acta Physiologiae Plantarum
• Rocznik: 2013
• Tom: 35
• Numer: 03
• Opis fizyczny: p.901-909,fig.,ref.

Twórcy

autor

Shaikh F K

• Department of Biochemistry, Dr. Babasaheb Ambedkar Marathwada University, Aurangabad, India

autor

Gadge P. P.

• Department of Biochemistry, Dr. Babasaheb Ambedkar Marathwada University, Aurangabad, India

autor

Shinde A. A.

• Department of Biochemistry, Dr. Babasaheb Ambedkar Marathwada University, Aurangabad, India

autor

Jaiwal B. V.

• Department of Biochemistry, Dr. Babasaheb Ambedkar Marathwada University, Aurangabad, India

autor

Shinde K. D.

• Department of Biochemistry, Dr. Babasaheb Ambedkar Marathwada University, Aurangabad, India

autor

Padul M. V.

• Department of Biochemistry, Dr. Babasaheb Ambedkar Marathwada University, Aurangabad, India

autor

Kachole M. S.

• Department of Biochemistry, Dr. Babasaheb Ambedkar Marathwada University, Aurangabad, India

Bibliografia

• Anthonamma K, Prasad SHKR, Rajasekhar D, Swapna NL, prasad M (2010) In vitro antimicrobial efficacy of solvent extracts of seeds of Albizzia lebbeck (L.) Benth. Int J Adv Pharm Sci 1:281–283
• Baruah CC, Gupta PP, Patnaik GK, Misra-Bhattacharya S, Goel RK, Kulshreshtha DK, Dubey MP, Dhawan BN (2000) Immunomodulatory effect of Albizzia Lebbeck. Pharm Biol 38(3):161–166
• Bernfeld P (1955) a-amylases, alpha and beta. In: Colowick SP, Kaplan NO (eds) Methods in enzymology, vol 1. Academic Press, New York, pp 149–158
• Carlson GL, Li BU, Bass P, Olsen WA (1983) A bean alpha-amylase inhibitor formulation (starch blocker) is ineffective in man. Science 219(4583):393–395
• Celleno L, Tolaini MV, Damore A, Perricone NV, Preuss HG (2007) A dietary supplement containing standardized Phaseolus vulgaris extract influences body composition of overweight men and women. Int J Med Sci 41:45–52
• Chintawar SD, Somani RS, Kasture VS, Kasture SB (2002) Nootropic activity of Albizzia lebbeck in mice. MAPA 24(6):3451
• Chokshi D (2006) 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 25:361–371
• Davis BJ (1964) Disc electrophoresis-II. Method and application to human serum proteins. Ann NY Acad Sci 121:404–427
• Dayler CSA, Mendes PAM, Prates MV, Bloch C Jr, Franco OL, Grossi-de-Sa MF (2005) Identification of a novel bean aamylase inhibitor with chitinolytic activity. FEBS Lett 579: 5616–5620
• Fontanini D, Capocchi A, Saviozzi F, Galleschi L (2007) Simplified electrophoretic assay for human salivary a-amylase inhibitor detection in cereal seed flours. J Agric Food Chem 55:4334–4339
• Fowler MJ (2007) Diabetes treatment part 2: oral agents for glycemic management. Clin Diabetes 25:134–144
• Franco OL, Rigden DJ, Melo FR, Bloch C Jr, Silva CP, Grossi-de-Sa MF (2000) Activity of wheat alpha amylase inhibitors towards bruchid alpha amylases and structural explanation of observed specificities. Eur J Biochem 267:1466–1473
• Franco DLR, Melo FR, Grossi-de Sa´ MF (2002) α-Amylase inhibitors and their interaction with insect α-amylase. Structure, function and potential crop protection. Eur J Biochem 269:397–412
• Gibbs B, Ali I (1998) Characterization of a purified alpha-amylase inhibitor from white kidney beans (Phaseolus vulgaris). Food Res Int 31:217–225
• Giri AP, Kachole MS (1998) α-Amylase inhibitors of pigeonpea (Cajanus Cajan) seeds. Phytochemistry 47:197–202
• Gupta RS, Chaudhary R, Yadav RK, Verma SK, Dobhal MP (2005) Effect of Saponins of Albizia lebbeck Benth. Bark on the reproductive system of male albino rats. J Ethnopharmacol 96(1–2):31–36
• Guzman-Partida AM, Jatomea-Fino O, Robles-Burgueno MR, Ortega-Nieblas M, Vazquez-Moreno L (2007) Characterization of α-amylase inhibitor from Palo Fierro seeds. Plant Physiol Biochem 45:711–715
• Huang WY, Teita NW (1982) Determinations of a-amylase isoenzymesin serum by use of a selective inhibitor. Clin Chem 28:1525–1527
• Ishimoto M, Kitamura K (1989) Growth inhibitory effects of an aamylase inhibitor from kidney bean, Phaseolus vulgaris (L.) on three species of bruchids (Coleoptera: bruchidae). Appl Entomol Zool 24:281–286
• Kim YM, Jeong YK, Wang MH, Lee WY, Rhee HI (2005) Inhibitory effect of pine extract on alpha-glucosidase activity and postprandial hyperglycemia. Nutrition 21:756–761
• Kluh I, Horn M, Hyblova J, Hubert J, Doleckova- Maresova L, Voburka Z, Kudlikova I, Kocourek F, Mares M (2005) Inhibitory specificity and insecticidal selectivity of a-amylase inhibitor from Phaseolus vulgaris. Phytochem 66:31–39
• Krishna BB, Patrı´cia BP, Rau´l AL, Maria FG, Carlos B Jr, Jorge ATM, Betania FQ, Eliane FN, Octa´vio LF (2007) Molecular identification of four different a-amylase inhibitors from Baru (Dipteryx alata) seeds with activity toward insect enzymes. J Biochem Mol Biol 40(4):494–500
• Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of Bacteriophage T4. Nature 227:680–685
• Layer P, Carlson GL, DiMagno EP (1985) Partially purified white bean amylase inhibitor reduces starch digestion in vitro and inactivates intraduodenal amylase in humans. Gastroenterology 88:1895–1902
• LeBerre-Anton V, Bompard-Gilles C, Payan F, Rouge P (1997) Characterization and functional properties of the alpha-amylase inhibitor (alpha A-1) from kidney bean (Phaseolus vulgaris) seeds. Biochim Biophys Acta 1343:31–40
• Leiner IE, Donatrucci DA, Tarcza JC (1984) Starch blockers: a potential source of trypsin inhibitors and lectins. Am J Clin Nutr 39:196–200
• Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275
• Marshall JJ, Lauda CM (1975) Purification and properties of phaseolamine, an inhibitor of a-amylase, from the kidney bean, Phaseolus vulgaris. J Biol Chem 250:8030–8037
• Matsui T, Tanaka T, Tamura S, Toshima A, Miyata Y, Tanaka K et al (2007) Alpha-glucosidase inhibitory profile of catechins and theaflavins. J Agric Food Chem 55:99–105
• Nagaraj RH, Pattabiraman TN (1985) Purification and properties of aamylase inhibitor specific for human pancreatic amylase from proso (Panicium miliaceum) seeds. J Biosci 7(3 & 4):257–268
• Ndemanisho E, Kimoro B, Mtengeti E, Muhikambele V (2006) The potential of Albizia lebbeck as a supplementary feed for goats in Tanzania. Agrofor Syst 67:85–91
• O’Donnell MD, FitzGerald O, McGeeney KF (1977) Differential serum a-amylase determination by use of an inhibitor, and design of a routine procedure. Clin Chem 23:560–566
• Obiro WC, Zhang T, Jiang B (2009) Starch blocking stability of the Phaseolus vulgaris alpha-amylase inhibitor (a-AI1). Am J Food Tech 1:9–19
• Octavio L, Rigden D (2002) Plant a-amylase inhibitors and their interaction with -a-amylases. Eur J Biochem 269:397–412
• Olorunsanya AO, Egbewande OO, Ibrahim H, Adeyemo MM (2010) Growth Performance and Carcass Analysis of Broiler Chickens Fed Graded Levels of Toasted Albizia lebbeck Seed Meal. Pak J Nutr 9(9):873–876
• Payan F (2004) Structural basis for the inhibition of mammalian and insect alpha-amylases by plant protein inhibitors. Biochim Biophys Acta 1696:171–180
• Pratibha N, Saxena VS, Amit A, D’Souza P, Bagchi M, Bagchi D (2004) Anti inflammatory activities of Aller-7, a novel polyherbal formulation for allergic rhinitis. Int J Tissue React 26(1–2):43–51
• Qian M, Nahoum V, Bonicel J, Bischoff H, Henrissat B, Payan F (2001) Enzyme-catalyzed condensation reaction in a mammalian α-amylase highresolution structure analysis of an enzymeinhibitor complex. Biochemistry 40:7700–7709
• Resmi CR, Venukumar MR, Latha MS (2006) Antioxidant activity of Albizzia lebbeck (Linn.) Benth in alloxan rats. Indian J Physiol Pharma 50(3):297–302
• Richardson M (1991) Methods in Plant Biochemistry. In: Rogers LJ (ed), vol 5. Academic Press, New York, pp 259–305
• Saha A, Ahmed M (2009) The analgesic and anti-inflammatory activities of the extract of Albizia lebbeck in animal model. Pak J Pharm Sci 22(1):74–77
• Schroeder HE, Gollasch S, Moore AE, Tabe LM, Craig S, Hardie DC, Chrispeels MJ, Spencer D, Higgins TJV (1995) Bean a-amylase inhibitor confers resistance to the pea weevil (Bruchus pisorum) in transgenic peas (Pisum satiVum L.). Plant Physiol 107:1233–1239
• Sitthipong P (2005) Amylase, maltase and sucrase inhibitors from red kidney bean (Phaseolus vulgaris). Prince of Songkla University, Faculty of Science
• Sopade PA, Gidley MJ (2009) A rapid in vitro digestibility assay based on glucometry for investigating kinetics of starch digestion. Starch/Sta¨rke 61:245–255
• Svensson B, Fukuda K, Nielsen PK, Bønsager BC (2004) Proteinaceous α-amylase inhibitors. Biochim Biophys Acta 1696:145–156
• Tormo MA, Gil-Exojo I, Romero de Tejada A, Campillo JE (2004) Hypoglycaemic and anorexigenic activities of a-amylase inhibitor from white kidney beans (Phaseolus vulgaris) in Wistar rats. Br J Nutr 92:785–790
• Valencia-Jimenez JA, Bustillo AE, Ossa GA, Chrispeels MJR (2000) Amylases of the coffee berry borer (Hypothenemus hampei) and their inhibition by two plant amylase inhibitors. Insect Biochem Mol Biol 30:207–213
• Xiaoyan H, Jiangui L, Qiughua S, Jusong Z, Xiaoling H, Hao M (2009) Characterization of a novel legumin alpha amylase inhibitor from chickpea (Cicer arietinum L.) seeds. Biosci Biotechnol Biochem 73(5):1200–1202
• Yamada T, Hattori K, Ishimoto M (2001) Purification and characterization of two a-amylase inhibitors from seeds of tepary bean (Phaseolus acutifolius A. Gray). Phytochemistry 58:59–66
• Yoshikawa H, Kotaru M, Tanaka C, Ikeuchi T, Kawabata M (1999) Characterization of kintoki bean (Phaseolus vulgaris) alphaamylase inhibitor: inhibitory activities against human salivary and porcine pancreatic alpha-amylases and activity changes by proteolytic digestion. J Nutr Sci Vitaminol 45:797–802

Uwagi

rekord w opracowaniu