Composition, solubility, and gel electrophoretic properties of proteins isolated from Florunner (Arachis hypogaea) peanut seeds

Sm, Basha; Al–Wandawi, Hussain

doi:10.1021/jf60204a058

Cited by 64 publications

(46 citation statements)

References 24 publications

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“…Each of these globulins consists of several polypeptide species, which are thought to exist together as subunits of large multimeric complexes. In addition, many of the polypeptides appear to have similar molecular weights (2,20). In this study I (2).…”

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confidence: 99%

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Identification of Cultivar Differences in Seed Polypeptide Composition of Peanuts (Arachis hypogaea L.) by Two-Dimensional Polyacrylamide Gel Electrophoresis

Basha¹

1979

Plant Physiol.

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Seed polypeptides from several cultivars of peanut (Arachis hypogaea L.) have been compared by means of a two-dimensional polyacrylamide gel electrophoresis. Protein was extracted from the defatted peanut meal by homogenizing in 5 millimolar K2CO3-9.5 molar urea. After addition of Nonidet P40 (2%, v/v) The peanut (Arachis hypogaea L.) is an economically important source of vegetable protein, but is relatively low in its content of methionine, lysine and tryptophan (1, 11). There are a few reports suggesting that certain genotypes exist within the species that contain a better balance of nutritionally important amino acids than found in commercial cultivars (1,3,11).Current methods for screening variants for differences in protein composition are generally tedious and often inaccurate. For example, one-dimensional polyacrylamide gel electrophoresis, although widely employed, resolves only a limited number of polypeptides (4,8,10,11,19). In the peanut, the proteins are very poorly defmed and are contained mainly in two major globulin fractions, arachin and conarachin, which together constitute 97% of the protein of the meal. Each of these globulins consists of several polypeptide species, which are thought to exist together as subunits of large multimeric complexes. In addition, many of the polypeptides appear to have similar molecular weights (2, 20). In this study I have characterized the proteins of peanut meal using a two-dimensional electrophoretic technique which separates the 'This research was supported in part by National Science Foundation Grant PCM 76-81071 to R. M. Roberts. polypeptides according to their isoelectric point in the first dimension and by subunit size in the second. The method has been employed to distinguish different cultivars according to their polypeptide composition. It also allows application of up to 500 ,ug of protein on a single slab gel, thus providing the potential for purifying significant quantities of individual polypeptide components. MATERIALS AND METHODS SEED MATERIALSeeds from the following peanut (A. hypogaea L.) cultivars were provided by A. J. Norden of the University of Florida from their breeding lines: Florunner, Florigiant, Early Bunch, Jenkins Jumbo Runner, Altika, UF 75102, UF 77318, 439-16-10-3, 439-16-10-3-1, 439-16-10-3-2, and 439-16-10-1-1. After removal of skins and embryonic axes, the cotyledons were ground in a mortar with a pestle. The ground material was then defatted with cold ethyl ether by repeated extractions until the peanut meals were essentially fat-free. The defatted meals were stored at -20 C. CHEMICALS SDS (specially pure) was from British Drug House, Poole, UK.; ampholines were purchased from LKB, Uppsala, Sweden; urea was bought from Pierce Chemical Co., Rockford, Ill., Nonidet P-40 was obtained from Particle Data Laboratories, Ehmhurst, Ill. Coomassie brilliant blue R-250 and N,N'diallyltartardiamide (DATD) were products of Bio-Rad Laboratories, Richmond, Calif. Protein standards and agarose were from Sigma Chemical Co. Reagents f...

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confidence: 99%

“…In addition, many of the polypeptides appear to have similar molecular weights (2,20). In this study I (2).…”

mentioning

confidence: 99%

Identification of Cultivar Differences in Seed Polypeptide Composition of Peanuts (Arachis hypogaea L.) by Two-Dimensional Polyacrylamide Gel Electrophoresis

Basha¹

1979

Plant Physiol.

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“…Ferreyra et al (2007) and Kim et al (1992) also reported higher proportions in the contents of glutamic acid and amino acids in the peanut flour and peanut protein isolates, respectively. Other authors (Neucere, 1969;Dawson, 1971;Basha and Cherry, 1976;Kim et al, 1992) reported peanut seed proteins with high percentages of aspartic acid, glutamic acid, arginine and glycine and low percentages of cysteine and methionine. The contents of acid and basic amino acids correspond to 31-32 g and 15-16 g per 100 g peanut protein, respectively (Neucere, 1969;Dawson, 1971;Basha and Cherry, 1976;Kim et al, 1992).…”

Section: Amino Acid Composition In Peanut Oil-cake and Protein Concenmentioning

confidence: 98%

“…Rhee et al (1973) and Basha and Cherry (1976) reported that the largest amounts of soluble proteins extracted in water and sodium phosphate buffer were at pH 9 and 10. At pH values above 10, protein levels in different extraction media decreased slightly as a result of alkaline denaturation.…”

Section: Extraction Temperature Of Proteins From Peanut Oil-cake Flourmentioning

confidence: 99%

Optimization of the protein concentration process from residual peanut oil-cake

Gayol¹,

Pramparo²,

Nepote³

et al. 2013

Grasas y Aceites

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The objective of this study was to find the best process conditions for preparing protein concentrate from residual peanut oil-cake (POC). The study was carried out on POC from industrial peanut oil extraction. Different protein extraction and precipitation conditions were used: water/ flour ratio (10:1, 20:1 and 30:1), pH (8, 9 and 10), NaCl concentration (0 and 0.5 M), extraction time (30, 60 and 120 min), temperature (25, 40 and 60 °C), extraction stages (1, 2 and 3), and precipitation pH (4, 4.5 and 5). The extraction and precipitation conditions which showed the highest protein yield were 10:1 water/flour ratio, extraction at pH 9, no NaCl, 2 extraction stages of 30 min at 40 °C and precipitation at pH 4.5. Under these conditions, the peanut protein concentrate (PC) contained 86.22% protein, while the initial POC had 38.04% . POC is an alternative source of protein that can be used for human consumption or animal nutrition. Therefore, it adds value to an industry residue.

El objetivo de este trabajo fue encontrar las mejores condiciones para obtener un concentrado de proteínas a partir de la torta residual de maní (POC). El estudio se llevó a cabo en POC provenientes de la extracción industrial de aceite de maní. Se utilizaron distintas condiciones para la extracción y precipitación de proteínas: relación agua / harina (10:1, 20:1 y 30:1), pH de extracción (8, 9 y 10), concentración de NaCl (0 y 0,5 M), tiempo de extracción (30, 60 y 120 min), temperatura (25, 40 y 60 °C), número de etapas de extracción (1, 2 y 3), y el pH de precipitación (4, 4,5 y 5). Las condiciones de extracción y de precipitación que mostraron mayor rendimiento de proteína fueron: relación de 10:1 en agua / harina, pH de extracción de 9, en ausencia de NaCl, 2 etapas de extracción de 30 min cada una a 40 °C y el pH de precipitación de 4,5. En estas condiciones, el concentrado de proteína de maní (PC) fue de 86,22%, mientras que el porcentaje de proteínas de la POC inicial fue de 38,04%. Las POC son una fuente alternativa de proteínas que pueden ser utilizadas para el consumo humano o la alimentación animal. De esta manera, se le puede dar un valor agregado extra a un residuo de la industria del aceite del maní

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“…Mnembuka and Eggum (1993) identified in the groundnut the presence of proteins with molecular weights 12.0, 13.2, 18.6, 33.1, and 39.8 kDa. Basha and Cherry (1976) reported proteins of 84 kDa. In winged bean protein, of weights 12.3, 14.7 (Sathe & Salunkhe, 1981), 67.0, and 82.0 kDa (Meng & Ma, 2001) have also been reported.…”

Section: Componentmentioning

confidence: 99%

Partial evaluation ofDipteryx lacuniferaseed kernel as a nutritional food Evaluación parcial de la almendra del fruto deDipteryx lacuniferacomo alimento nutritivo

Queiroga-Neto

Bora

Diniz

et al. 2009

CyTA - Journal of Food

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Composition, solubility, and gel electrophoretic properties of proteins isolated from Florunner (Arachis hypogaea) peanut seeds

Cited by 64 publications

References 24 publications

Identification of Cultivar Differences in Seed Polypeptide Composition of Peanuts (Arachis hypogaea L.) by Two-Dimensional Polyacrylamide Gel Electrophoresis

Identification of Cultivar Differences in Seed Polypeptide Composition of Peanuts (Arachis hypogaea L.) by Two-Dimensional Polyacrylamide Gel Electrophoresis

Optimization of the protein concentration process from residual peanut oil-cake

Partial evaluation ofDipteryx lacuniferaseed kernel as a nutritional food Evaluación parcial de la almendra del fruto deDipteryx lacuniferacomo alimento nutritivo

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