Portal de Periódicos da CAPES

Identification of ?-amylase inhibitors in triticale grain

1999; Wiley; Volume: 79; Issue: 12 Linguagem: Inglês

10.1002/(sici)1097-0010(199909)79

1097-0010

Armando Burgos-Hern�ndez, Carina Rosas‐Burgos, Benjam�n Ram�rez-Wong, Ángel A. Carbonell‐Barrachina, Francisco J. Cinco‐Moroyoqui,

Phytase and its Applications

Journal of the Science of Food and AgricultureVolume 79, Issue 12 p. 1671-1675 Paper Identification of α-amylase inhibitors in triticale grain Armando Burgos-Hernández, Corresponding Author Armando Burgos-Hernández Departamento de Investigación y Posgrado en Alimentos de la Universidad de Sonora, AP 1658, Hermosillo, Sonora, MéxicoRosales y Blvd Luis Encinas Johnson s/n Col. Centro, Apartado Postal 1658, Hermosillo, Sonora, México C P 83000Search for more papers by this authorCarina Rosas-Burgos, Carina Rosas-Burgos Departamento de Investigación y Posgrado en Alimentos de la Universidad de Sonora, AP 1658, Hermosillo, Sonora, MéxicoSearch for more papers by this authorBenjamín Ramírez-Wong, Benjamín Ramírez-Wong Departamento de Investigación y Posgrado en Alimentos de la Universidad de Sonora, AP 1658, Hermosillo, Sonora, MéxicoSearch for more papers by this authorAngel A Carbonell-Barrachina, Angel A Carbonell-Barrachina Departamento de Investigación y Posgrado en Alimentos de la Universidad de Sonora, AP 1658, Hermosillo, Sonora, MéxicoSearch for more papers by this authorFrancisco J Cinco-Moroyoqui, Francisco J Cinco-Moroyoqui Departamento de Investigación y Posgrado en Alimentos de la Universidad de Sonora, AP 1658, Hermosillo, Sonora, MéxicoSearch for more papers by this author Armando Burgos-Hernández, Corresponding Author Armando Burgos-Hernández Departamento de Investigación y Posgrado en Alimentos de la Universidad de Sonora, AP 1658, Hermosillo, Sonora, MéxicoRosales y Blvd Luis Encinas Johnson s/n Col. Centro, Apartado Postal 1658, Hermosillo, Sonora, México C P 83000Search for more papers by this authorCarina Rosas-Burgos, Carina Rosas-Burgos Departamento de Investigación y Posgrado en Alimentos de la Universidad de Sonora, AP 1658, Hermosillo, Sonora, MéxicoSearch for more papers by this authorBenjamín Ramírez-Wong, Benjamín Ramírez-Wong Departamento de Investigación y Posgrado en Alimentos de la Universidad de Sonora, AP 1658, Hermosillo, Sonora, MéxicoSearch for more papers by this authorAngel A Carbonell-Barrachina, Angel A Carbonell-Barrachina Departamento de Investigación y Posgrado en Alimentos de la Universidad de Sonora, AP 1658, Hermosillo, Sonora, MéxicoSearch for more papers by this authorFrancisco J Cinco-Moroyoqui, Francisco J Cinco-Moroyoqui Departamento de Investigación y Posgrado en Alimentos de la Universidad de Sonora, AP 1658, Hermosillo, Sonora, MéxicoSearch for more papers by this author First published: 18 August 1999 https://doi.org/10.1002/(SICI)1097-0010(199909)79:12 3.0.CO;2-DCitations: 7AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat Abstract In this study three complete triticales, three substituted (one gene from rye has been replaced by one gene from wheat) triticales, and parental wheat and rye were analysed for α-amylase inhibitory activity to evaluate whether the genetic modification influenced triticale α-amylase inhibitory activity. Gel filtration chromatography and thermostability analyses were performed to partially isolate and characterize α-amylase inhibitors. Results demonstrated that substituted triticales and wheat had higher α-amylase inhibitory activities and higher water-soluble protein contents than complete triticales and rye. Sodium dodecylsulfate-PAGE-electrophoresis showed that all triticales, irrespective of their classification, inherited the water-soluble protein patterns from their parents: wheat and rye. In a substituted triticale (Pony 'S'), two peaks with α-amylase inhibitory activity were resolved by gel filtration chromatography; they were designated T1 and T2 according to their order of elution. T1 showed a higher inhibitory activity but a lower thermostability at 70 °C than T2; T1 apparently comes from wheat, whereas T2 presumably comes from rye. © 1999 Society of Chemical Industry REFERENCES 1Bushuk W, Proteins of triticale: Chemical and physical characteristics,, in Triticale: First Man-made Cereal, ed by C C Tsen, American Association of Cereal Chemists, Inc, Saint Paul, MN. pp 291–296 (1974). Google Scholar 2 National Research Council, Triticale. A Promising Addition to the World's Cereal Grains, National Academy Press, Washington, DC. pp 11–28 (1989). Google Scholar 3Varughese G, Barker T and Saari E, Triticale. CIMMyT, Mexico, DF. 32 pp (1987). Google Scholar 4Chang C R and Tsen C C, Isolation of trypsin inhibitors from rye, triticale, and wheat samples. Cereal Chem 58: 207–210 (1981). CASWeb of Science®Google Scholar 5Shainkin R and Birk Y, Alpha-amylase inhibitors from wheat: Isolation and characterization. Biochim Biophys Acta 221: 502–513 (1984). 10.1016/0005-2795(70)90221-7 PubMedWeb of Science®Google Scholar 6Petrucci T, Tomasi M, Cantagalli P and Silano V, Comparison of wheat albumin inhibitors of alpha-amylase and trypsin. Phytochem 13: 2487–2495 (1974). 10.1016/S0031-9422(00)86925-3 CASWeb of Science®Google Scholar 7O'Donnell M D and McGeeney K F, Purification and properties of an alpha-amylase inhibitor from wheat. Biochim Biophys Acta 422: 159–169 (1976). 10.1016/0005-2744(76)90016-4 CASPubMedWeb of Science®Google Scholar 8Granum P E, Purification and characterization of an alpha-amylase inhibitor from rye (Secale cereale) flour. J Food Biochem 2: 103–120 (1978). 10.1111/j.1745-4514.1978.tb00607.x CASWeb of Science®Google Scholar 9Blanco-Labra A and Iturbe-Chinas F A, Purification and characterization of an alpha-amylase inhibitor from maize (Zea mays). J Food Biochem 5: 1–17 (1981). 10.1111/j.1745-4514.1981.tb00658.x CASWeb of Science®Google Scholar 10Hejgaard J, Svedsen I and Mundy J, Barley alpha-amylase/subtilisin inhibitor. II. N-terminal amino acid sequence and homology with inhibitors of the soybean trypsin inhibitor (Kunitz) family. Carlsberg Res Comm 48: 91–94 (1983). 10.1007/BF02906172 CASWeb of Science®Google Scholar 11Feng G, Chen M, Kramer K J and Reeck G R, α-Amylase inhibitors from rice: Fractionation and selectivity toward insect, mammalian, and bacterial α-amylases. Cereal Chem 68: 516–521 (1991). CASWeb of Science®Google Scholar 12Unrau A M and Jenkins B C, Investigations on synthetic cereal species. Milling, baking, and some compositional characteristics of some 'triticale' and parental species. Cereal Chem 41: 365–375 (1964). Web of Science®Google Scholar 13Chen C H and Bushuk W, Nature of proteins in triticale and its parental species. I. Solubility characteristics and amino acid composition of endosperm proteins. Can J Plant Sci 50: 9–14 (1970). 10.4141/cjps70-002 CASWeb of Science®Google Scholar 14Masojc P and Larsson-Raznikiewicz M, Variations of the levels of α-amylase and endogenous α-amylase inhibitor in rye and triticale grain. Swedish J Agric Res 21: 3–9 (1991). CASWeb of Science®Google Scholar 15Bernfeld P, Amylases α and β,, in Methods in Enzymology, Vol 1, ed by S P Colowick and N O Kaplan, Academic Press, New York. pp 40–58 (1955). Google Scholar 16Frels J M and Rupnow J H, Purification and partial characterization of two α-amylase inhibitors from black bean (Phaseolus vulgaris). J Food Biochem 8: 281–287 (1984). 10.1111/j.1745-4514.1984.tb00329.x CASWeb of Science®Google Scholar 17Strumeyer D H, A modified starch for use in amylase assays. Anal Biochem 19: 61–71 (1967). 10.1016/0003-2697(67)90134-0 CASPubMedWeb of Science®Google Scholar 18Lowry O H, Rosebrough N J, Farr A L and Randall R J, Protein measurement with the Folin phenol reagent. J Biol Chem 193: 265–275 (1951). 10.1016/S0021-9258(19)52451-6 CASPubMedWeb of Science®Google Scholar 19Hartree E F, Determination of protein: A modification of the Lowry procedure that gives a linear photometric response. Anal Biochem 48: 422–427 (1972). 10.1016/0003-2697(72)90094-2 CASPubMedWeb of Science®Google Scholar 20Laemmli U K, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 226: 680–685 (1972). Google Scholar 21 SAS (Statistical Analysis System), SAS User's Guide: Statistics, 5th edn, SAS Institute, Inc, Cary, NC. pp 956 (1984). Google Scholar 22Powers J R and Cultbertson J D, In-vitro effect of bean amylase inhibitor on insect amylases. J Food Protec 45: 655–657 (1982). 10.4315/0362-028X-45.7.655 CASWeb of Science®Google Scholar 23Applebaum S W and Konijn A M, The utilization of starch by larvae of the flour beetle, Tribolium castaneum. J Nutr 85: 275–282 (1965). CASPubMedWeb of Science®Google Scholar 24Applebaum S W and Konijn A M, Factors affecting the development of Tribolium castaneum (Herbst) on wheat. J Stored Prod Res 2: 323–329 (1967). 10.1016/0022-474X(67)90078-1 Google Scholar 25Kneen E and Sandstedt R M, An amylase inhibitor from certain cereals. J Am Chem Soc 65: 1247 (1943). 10.1021/ja01246a512 CASWeb of Science®Google Scholar 26Cantaglli P, Di Giorgio G, Morisi G, Pocchiari F and Silano V, Purification and properties of three albumins from Triticum aestivum seeds. J Sci Food Agric 22: 256–259 (1971). 10.1002/jsfa.2740220510 CASWeb of Science®Google Scholar 27Friedman M, Nutritional and toxicological significance of enzyme inhibitors in foods, in Advances in Experimental Medicine and Biology, Plenum Press, New York. pp 199–483 (1987). Google Scholar Citing Literature Volume79, Issue12September 1999Pages 1671-1675 ReferencesRelatedInformation