Physicochemical Properties of Oilseed Protein

Prakash, Ved; Rao, M. S. Narasinga

doi:10.3109/10409238609083736

Cited by 119 publications

(88 citation statements)

References 322 publications

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“…Total protein isolate studied showed good solubility at alkaline pH and in the presence of salts, which was an important characteristic in food formulations [20]. Prakash and Narasinga [21] reported similar observations.…”

Section: Protein Content Fractionation and Solubilitysupporting

confidence: 67%

“…WBP had a water-holding capacity of 4.20 mL H 2 O/g protein that is higher than that reported by Prakash and Narasinga [21] and out of the range of the commercial values of protein concentrates (1.90-2.20) as reported by Lin and Zayas [22]. This is likely due to the fact that the WBP had a great ability to swell because it contained arabinoxylans as well as crude fiber, which could be responsible for the increased water-holding capacity [5].…”

Section: Water-and Oil-holding Capacitycontrasting

confidence: 44%

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Fractionation, solubility and functional properties of wheat bran proteins as influenced by pH and/or salt concentration

Idris

Babiker²,

Tinay

2003

Nahrung

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The content, fractionation, solubility and functional properties of wheat bran proteins as well as the effects of pH and/or NaCl concentration on some of these functional properties were investigated. The protein content of the bran was found to be 16.80%. Albumin and glutelin are the major fractions of wheat bran proteins. The minimal protein solubility was observed at pH 5.5, the maximum at pH 11.5. The emulsifying capacity, activity and emulsion stability as well as foaming capacity and foam stability were greatly affected by pH and salt concentrations. Lower values were observed at acidic pH and high salt concentration. The least gelation concentration of wheat bran proteins was found to be 16% when the proteins were dissolved in 1.0 M NaCl. The total protein was highly viscous and dispersable with water-holding capacity of 4.20 mL H2O/g protein, oil-holding capacity of 1.70 mL oil/g protein and bulk density of 0.29 g/mL while dispensability was found to be 77.30%.

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Section: Protein Content Fractionation and Solubilitysupporting

confidence: 67%

Section: Water-and Oil-holding Capacitycontrasting

confidence: 44%

Fractionation, solubility and functional properties of wheat bran proteins as influenced by pH and/or salt concentration

Idris

Babiker²,

Tinay

2003

Nahrung

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“…The results of this work give further evidence for the idea that there exists a "homology" among oilseed high molecular mass protein fractions with respect to their structural properties as pointed out by PRAKASH et al [2,14,151 and PLIETZ et al [16]. …”

Section: Circular Dichroism Spectroscopysupporting

confidence: 62%

Characterization of the major protein fraction carmin from safflower seeds (Carthamus tinctorius L.) by dynamic light scattering and circular dichroism spectroscopy

Zirwer

Prakash

Raab

et al. 1989

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Hydrodynamic parameters of the major protein fraction carmin from safflower seed were determined by means of dynamic light scattering. The results indicated a translational diffusion coefficient of (3.81 f 0.06) x cm2 s-l and a STOKES radius of (5.6 f 0.06) nm. The calculated molecular mass M,, was (3.1 f 0.1) x lo5 g/mol and the frictional ratio was 1.25 & 0.05. Evaluation of secondary structure from CD spectra using the method of PROVENCHER and GL~CKNER gave 8 % a-helix, 45 % 8-sheet and 47 % aperiodic structure.These results are discussed in view of structural homology of oilseed proteins.

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“…The band intensities were measured by densitometry. Activities are expressed as mg or /xmol of substrate digested in 24 h, assuming that the extinction coefficients at AW are the same for the acidic and basic chains and are those of the native glycinin (Easo 196 of glycinin is 8.1 [Parakash and Narasinga Rao, 1986]). …”

Section: Proteolysis Of Other Legume Storage Proteins By Protease C Lmentioning

confidence: 99%

Characterization of a Soybean [beta]-Conglycinin-Degrading Protease Cleavage Site

Chen

Wilson

et al. 1994

Plant Physiol.

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Protease C1, an enzyme from soybean (Glycine max [L.] Merrill cv Amsoy 71) seedling cotyledons, was previously determined to be the enzyme responsible for the initial degradation of the a' and a subunits, but not the 8 subunit, of 8-conglycinin storage protein.l h e sizes of the proteolytic products generated by the action of protease C1 suggest that the cleavage sites on the a' and a subunits of j3-conglycinin may be located in their N-terminal domain, which is not found in the j3 subunit of 8-conglycinin. To check this hypothesis, storage proteins from other plant species that are homologous to either the a'/a or the j3 subunit of j3-conglycinin were tested as substrates. As expected, the convicilin from pea (Pisum sativum), a protein homologous to the a ' and a subunits of 8-conglycinin, was digested by protease C1. l h e vicilins from pea as well as vicilins from adzuki bean (Vigna angularis), garden bean (Phaseolus vulgaris), black-eyed pea (Vigna unguiculata), and mung bean (Vigna radiata), storage proteins that are homologous to the 19 subunit of soybean 8-conglycinin, were not degraded by protease C1. Degradation of soybean 8-conglycinin involves a sequential attack of the a subunit at multiple sites, culminating in the formation of a stable intermediate of 53.5 kD and a final product of 48.0 kD. The cleavage sites resulting in this formation of the intermediates and final product were determined by Nterminal analysis. lhese were compared to the known amino acid sequences of the three j3-conglycinin subunits. Results showed these two polypeptides to be generated by proteolysis of the a subunit at regions bearing long strings of acidic amino acid residues.Proteolysis of seed storage protein is a crucial process during early growth because it provides the seedling with amino acids until the seed becomes fully autotrophic. Soybean seeds (Glycine max) contain large amounts of storage proteins, particularly of glycinin and P-conglycinin. Glycinin has six subunits, each consisting of an acidic and a basic polypeptide linked by a single disulfide bond (Nielsen, 1985). 0-Conglycinin is composed of three subunits, a', a, and 0, associated in various combinations by noncovalent interactions Shibasaki, 1977, 1978). The greatest difference in the amino acid sequences of the three subunits of 8-conglycinin is in a segment of 179 amino acids at the N terminus of both the a' and the a subunits that is lacking in the / 3 subunit (Sebastiani et al., 1990). During early growth, Supported by National Science Foundation grants PCM 8301202Present address: Department of Food Science, Rutgers University, and DCB 9017420. Newark, NJ.* Corresponding author; fax 1-607-777-6521. 127these proteins have been shown to undergo limited proteolysis, yielding discrete intermediates. The limited proteolysis is subsequently followed by more extensive and rapid degradation of those intermediates (Wilson et al., 1986). We have previously described the purification and characterization of a soybean Ser protease, protease C1, which catalyze...

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Physicochemical Properties of Oilseed Protein

Cited by 119 publications

References 322 publications

Fractionation, solubility and functional properties of wheat bran proteins as influenced by pH and/or salt concentration

Fractionation, solubility and functional properties of wheat bran proteins as influenced by pH and/or salt concentration

Characterization of the major protein fraction carmin from safflower seeds (Carthamus tinctorius L.) by dynamic light scattering and circular dichroism spectroscopy

Characterization of a Soybean [beta]-Conglycinin-Degrading Protease Cleavage Site

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