IDENTIFICATION OF PROTEINS ISOLATE FROM AMARANTH (AMARANTHUS CAUDATUS) BY SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS WITH WATER AND NACL 0.1 M SOLVENTS
Abstract
ABSTRACT
Objective: The aim of this study was to obtain protein isolate from amaranth using alkaline method at extraction pH 8 and extraction pH 12 with
different precipitation pHs and to analyze protein isolate with electrophoresis.
Methods: Amaranth protein isolates were obtained using isoelectric precipitation method at different pHs. Proteins were analyzed using sodium
dodecyl sulfate-polyacrylamide gel electrophoresis.
Results: A yield of 20.52% of protein isolate of defatted amaranth at pH 4.0 was obtained. The content of protein isolate was higher than 53% in all
pH assays. Globulins and albumins in protein isolate at different pHs were observed. A band with 50 kDa corresponding to 7S globulin was found. The
bands 36-38 kDa and 18-20 kDa correspond to 11S globulin. Bands less to 14.4 kDa correspond to albumins.
Conclusions: Amaranth protein isolate is possible to obtain in extreme conditions of pH. The treatment with water was optimum to obtain amaranth
protein isolate.
Keywords: Amaranth, Globulins, Albumins, Proteinisolate, Sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
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References
Montoya-RodrÃguez A, Milán-Carrillo J, Dia VP, Reyes-Moreno C,
González de MejÃa E. Pepsin-pancreatin protein hydrolysates
fromextruded amaranth inhibit markers ofatherosclerosis
in LPS-induced THP-1macrophages-like human cells by
reducingexpression of proteins in LOX-1 signaling pathway. Proteome
Sci 2014;12:1-13.
Osuna-Castro JA, Rascón-Cruz Q, Napier J, Fido RJ, Shewry PR,
Paredes-López O. Overexpression, purification, and in vitro refolding
of the 11S globulin from amaranth seed in Escherichia coli. J Agric
Food Chem 2000;48(11):5249-55.
Ventureira J, MartÃnez NE, Añón MC. Stability of oil: Water emulsions
of amaranth proteins. Effect of hydrolysis and pH. Food Hydrocoll
;24:551-9.
Vega-Gálvez A, Miranda M, Vergara J, Uribe E, Puente L, MartÃnez EA.
Nutrition facts and functional potential of quinoa (Chenopodium
quinoa willd.), an ancient Andean grain: A review. J Sci Food Agric
;90(15):2541-7.
Abugoch LE, Romero N, Tapia CA, Silva J, Rivera M. Study of some
physicochemical and functional properties of quinoa (Chenopodium
quinoa willd) protein isolates. J Agric Food Chem 2008;56(12):4745-50.
AOAC. Official Methods of Analysis. Washington, DC, USA:
Association of Official Analytical Chemists; 2012.
MartıÃnez NE, Añón MC. Composition and structural characterization
of amaranth protein isolates. An electrophoretic and calorimetric study.
J Agric Food Chem 1996;44:2523-30.
Gornall AG, Bardawill CJ, David MM. Determination of serum proteins
by means of the biuret reaction. J Biol Chem 1949;177(2):751-66.
Laemmli UK. Cleavage of structural proteins during the assembly of
the head of bacteriophage T4. Nature 1970;227(5259):680-5.
Tandang-Silvas MR, Cabanos CS, Carrazco Peña LD, De la Rosa AP,
Osuna-Castro JA, Utsumi S, et al. Crystal structure of a major seed
storage protein, 11S proglobulin, from Amaranthus hypochondriacus:
Insight into its physico-chemical properties. Food Chem
;135(2):819-26.
Marcone MF, Kakuda Y, Yada RY. Salt-soluble seed globulins of
variousdicotyledonous and monocotyledonous plants-I.Isolation/
purification and characterization. Food Chem 1998;62:27-47.
Srivastava R, Roy B. Proteomic analysis of different extracts from
amaranth (Amaranthus tricolor) grains. Asian J Pharm Clin Res
;6:37-9.
Romero-zepeda H, Paredes-Lopez O. Isolation and characterizaton
of amaranthine. The 11S amaranth seed globulin. J Food Chem
;19:329-39.
López-MejÃa O, López-Malo A, Palou E. Antioxidant capacity of
extracts from amaranth (Amaranthus hypochondriacus L.) seeds or
leaves. Ind Crops Prod 2014;53:55-9.
Kaur S, Singh N, Rana JC. Amaranthus hypochondriacus and
Amaranthus caudatus germplasm: Characteristics of plants, grain and
flours. Food Chem 2010;123:1227-34.
Achouri A, Nail V, Boye JI. Sesame protein isolate: Fraction, secondary
structure and functional properties. Food Res Int 2012;46:360-9.
Achouri A, Boye JI. Thermal processing, salt and high pressure
treatment effects on molecular structure and antigenicity of sesame
protein isolate. Food Res Int 2013;53:240-51.
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