Seed protein characterisation of eleven species of amaranthus
DOI:
https://doi.org/10.3989/gya.2007.v58.i1.8Keywords:
Amaranth, Amino acid composition, Protein profile, SeedsAbstract
The protein profile and the amino acid composition of eleven amaranth species have been studied. The following species were taken into account: A. viridis, A. powellii, A.muricatus, A. deflexus, A. graecizans, A. blitoides, A. retroflexus, A. blitum, A. albus, A. cruentus and A. hypochondriacus. Seed samples were obtained from wild populations located in the southwest of Spain. The protein profile was studied by gel filtration chromatography and denaturing electrophoresis. Profiles were similar in all taxa, with small variations in the molecular weights and amounts of the main seed proteins. Thus, after gel filtration chromatography six main fractions of around 300 kDa, 180 kDa, 120 kDa, between 40 and 50 kDa, 20 and 30 kDa and below 10 kDa were observed. On the other hand, the electrophoretic analysis showed peptides grouped into three main fractions, between 50 and 64 kDa, 33 and 37 kDa and 18 and 25 kda. The most balanced amino acid compositions were observed in the wild taxa A. muricatus, A. blitum and A. powellii showed the most equilibrated amino acid composition. A. hypochondriacus and A. graecizans showed the most deficient amino acid composition with limitations in five essential amino acids. These results show the potential of wild amaranthus taxa for their introduction as crops or their use in the improvement by hybridization mechanisms of other crops such as A. hypochondriacus.
Downloads
References
Alaiz M, Navarro J L, Giron J, Vioque E. 1992. Amino acid analysis by high-performance liquid chromatography after derivatization with diethylethoxymethylenemalonate. J. Cromatogr. 591, 181–186. doi:10.1016/0021-9673(92)80236-N
Barba de la Rosa A P, Gueguen J, Paredes-López O, Viroben G. 1992. Fractionation procedures, electrophoretic characterization, an amino acid composition of amaranth seed proteins. J. Agric. Food Chem. 40, 931-936. doi:10.1021/jf00018a002
Becker R, Wheelr E L, Lorenz K, Stafford A E, Grosjean O K, Betschart A A, Saunders R.M. 1981. A composition study of amaranth grain. J. Food Sci. 46,1175-1180. doi:10.1111/j.1365-2621.1981.tb03018.x
Bradford M M. 1976. Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding. Anal. Biochem. 72, 248-254. doi:10.1016/0003-2697(76)90527-3
Bressani R. 1989. The proteins of grain amaranth. Food Rev. Int. 5, 13-38.
Bressani R, García-Vela L A. 1990. Protein fractions in amaranth grain and their chemical characterization. J. Agric. Food Chem. 38, 1205-1209. doi:10.1021/jf00095a010
Búcaro-Segura M E, Bressani R. 2002. Distribución de la proteína en fracciones físicas de la molienda y tamizado del grano del amaranto. Archivos Latinoamericanos de Nutrición 52(2), 167-171.
Cai Y Z, Sun M, Corke H. 1998 a. Colorant properties and stability of Amaranthus betacyanin pigments. J. Agric. Food Chem. 46, 4491-4495. doi:10.1021/jf980457g
Cai Y Z, Sun M, Wu H X, Huang R H, Corke H. 1998 b. Characterization and quantification of betacyanin pigments from diverse Amaranthus species. J. Agric. Food Chem. 46, 2063-2070. doi:10.1021/jf9709966
Chan K F, Sun M. 1997. Genetic diversity and relationships detected by isozyme and RAPD analysis of crop and wild species of Amaranthus. Theor. Appl. Genet. 95, 865-873. doi:10.1007/s001220050637
Costea M, Weaver S E, Tardif F J. 2004. The biology of Canadian weeds. 130. Amaranthus retroflexus L., A. powellii S.Watson and A. hybridus L. Can. J. Plant Sci. 84, 631-668.
Facciola S. 1990. Cornucopia - A Source Book of Edible Plants. Kampong Publications.
FAO/WHO. 1991. Protein quality evaluation. Report of a join FAO/WHO expert consultation. FAO Food and Nutrition Paper n° 51, 66 pages. Food and Agriculture Organization of the United Nations. Rome.
Galili G, Larkins B A. 1999. Enhancing the content of the essential amino acids lysine and threonine in plants en Singh B K. (Ed.), Plant amino acids biochemistry and biotechnology, 487-507. Marcel Dekker, Inc., New York.
Gorinstein S, Moshe R, Greene L, Arruda P. 1991. Evaluation of four Amaranthus species through protein electrophoretic patterns and their amino acid composition. J. Agric. Food. Chem. 39, 8851-854.
Kunkel G. 1984. Plant for Human Consumption, Koeltz Scientific Books.
Lehmann J W. 1996. Case history of grain amaranth as an alternative crop. Cereal Foods World 41, 399-411.
Lorenz K. 2003. Triticale en Caballero B, Trugo L, Finglas P. (Eds.) Encyclopedia of Food Science and Nutrition, 5873-5878. Academic Press Inc., Orlando.
Mahe S, Gausseres N, Tome D. 1994. Legume proteins for human requirements. Grain Legumes (AEP) 7, 15-17.
Martinez E N, Castellani O F, Añón M C. 1997. Common molecular features among amaranth storage proteins. J. Agric. Food Chem. 45, 3832-3839. doi:10.1021/jf9700384
Moerman D. 1998. Native American Ethnobotany, Timber Press. Oregon.
Mosyakin S L, Robertson K R. 1996. New infrageneric taxa and combinations in Amaranthus (Amaranthaceae). Ann. Bot. Fennici 33, 275-281.
Schägger H, von Jagow G. 1987. Tricine-sodium dodecyl sulfate- polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379. doi:10.1016/0003-2697(87)90587-2
Stallknecht G F, Schulz-Schaeffer J R. 1993. Amaranth rediscovered en Janick J, Simon J E (Eds.) New crops, 211-218. Willey, New York.
Uphof J C Th. 1959. Dictionary of Economic Plants. Ed. Lubrecht & Cramer Ltd.Weinheim.
Usher G. 1974. A Dictionary of Plants Used by Man. Londres, Ed. Constable and Company.
Zheleznov A V, Solonenko L P, Zheleznova N B. 1997. Seed proteins of the wild and the cultivated Amaranthus species. Euphytica 97, 177-182. doi:10.1023/A:1003073804203
Downloads
Published
How to Cite
Issue
Section
License
Copyright (c) 2007 Consejo Superior de Investigaciones Científicas (CSIC)
This work is licensed under a Creative Commons Attribution 4.0 International License.
© CSIC. Manuscripts published in both the printed and online versions of this Journal are the property of Consejo Superior de Investigaciones Científicas, and quoting this source is a requirement for any partial or full reproduction.All contents of this electronic edition, except where otherwise noted, are distributed under a “Creative Commons Attribution 4.0 International” (CC BY 4.0) License. You may read here the basic information and the legal text of the license. The indication of the CC BY 4.0 License must be expressly stated in this way when necessary.
Self-archiving in repositories, personal webpages or similar, of any version other than the published by the Editor, is not allowed.