Functional properties of glycosylated derivatives of the 11S storage protein from pea (Pisum sativum L.)

Baniel, Alain; Caer, Daniele.; Colas, Bernard; Guéguen, Jacques

doi:10.1021/jf00014a007

Cited by 39 publications

(48 citation statements)

References 28 publications

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“…Large numbers of native globular proteins have [g] values in the range of 2.5-6.0 ml g À1 (Baniel et al, 1992;Hahn and Aragon, 2006;Kumar et al, 1980;Lee and Tripathi, 2005;Monkos, 1997aMonkos, , 2000Monkos, , 2004Monkos, , 2005aSchwenke et al, 1986;Tanford, 1955). However, salt addition, pH adjustment, and denaturation could increase [g] value, by altering shape or charge of proteins (Bohidar, 1998;Britten and Giroux, 2001;Curvale et al, 2008;Vardhanabhuti and Foegeding, 1999;Wilcox and Swaisgood, 2002), or inducing the formation of asymmetric aggregation (Bohidar, 1998;Lonetti et al, 2004) or random coil-like structure (Batista et al, 2005).…”

Section: Resultsmentioning

confidence: 99%

Rheological behavior of wheat gliadins in 50% (v/v) aqueous propanol

Sun

Song

Zheng

2009

Journal of Food Engineering

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Section: Resultsmentioning

confidence: 99%

Rheological behavior of wheat gliadins in 50% (v/v) aqueous propanol

Sun

Song

Zheng

2009

Journal of Food Engineering

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“…The technological functional properties performed by legumes such as soy bean, lentil, fababean, pea and cowpea, among others, includes high molecular weight, solubility in a wide range pH, emulsification, viscosity, gelification and foaming (Baniel, Caer, Colas, & Gueguen, 1992;Maltais, Remondetto, & Subrade, 2008;Pedrosa, Trisciuzzi, & Ferreira, 1997;Rangel, Domont, Pedrosa, & Ferreira, 2003;Sosulski et al, 1976). Studies have demonstrated several applications of legume proteins in the development of varied food products, such as cakes, sausages, gelled food, fermented food and others (Geervani, Vimala, Pradeep, & Devi, 1996;Gomez, Oliete, Rosell, Pando, & Fernandez, 2008;Nassar, Mubarak, & El-Beltagy, 2008;Nunes, Raymundo, & Sousa, 2006).…”

Section: Introductionmentioning

confidence: 99%

Legumes seeds protein isolates in the production of ascorbic acid microparticles

Pereira

Saraiva

Carvalho

et al. 2009

Food Research International

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“…Emulsifying and foaming properties of different chemically modified proteins are widely described in the literature. Chemical treatments were used in the following ways: to improve the flexibility of proteins either by reduction of disulfide bonds (12) or glycosylation (13); to increase their solubility by either deamidation (14) or grafting polar molecules (15); and to enhance the hydrophobicity of proteins by either dissociation and reduction (16) or grafting hydrophobic groups by esterification (17), mainly by acylation and succinylation of amino groups (18)(19)(20).…”

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confidence: 99%

Emulsifying and foaming properties of native and chemically modified peptides from the 2S and 12S proteins of rapeseed (Brassica napus L.)

Malabat

nchez-Vioque

Rabiller³

et al. 2001

J Americ Oil Chem Soc

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The 2S and 12S proteins of rapeseed were isolated and subsequently hydrolyzed by pepsin or a combination of pepsin plus trypsin. The resulting hydrolysates had a 15% degree of hydrolysis and were purified by gel filtration chromatography in order to obtain homogeneous peptide fractions. Three major fractions, having an average peptide chain length of 7.5-11 amino acids, were recovered. Purified peptide fractions were acylated with butyric anhydride and sulfamidated with ptoluenesulfonyl chloride. The degree of modification was always higher than 90%. Emulsifying and foaming properties of native and chemically modified peptides were studied and compared to those of sodium dodecyl sulfate (SDS) as standard. A peptide fraction from the 15% hydrolysis of the 12S protein exhibited the best foaming properties. After sulfamidation, this peptide fraction showed a foam formation similar to that of SDS. Whereas the attachment of toluene groups generally improved the surface properties, the incorporation of an aliphatic chain of four atoms of carbon was detrimental in most of the cases. On the other hand, none of the native or hydrophobized peptide fractions was able to form a stable emulsion.Paper no. J9679 in JAOCS 78, 235-241 (March 2001). KEY WORDS:Chemical modification of peptides, cruciferin, enzymatic hydrolysis of proteins, foaming and emulsifying properties, napin.Proteins are recognized to be much more than a simple source of nutrients. Because of their amphiphilic nature, proteins are also involved in functional aspects of foods, such as the formation of emulsions and foams. Proteins can be adsorbed at oil-water and air-water interfaces, decreasing surface tension values, and, hence facilitating the formation of emulsions and foams. This adsorption is believed to occur in three distinct steps. First, protein molecules diffuse to the subsurface just below the interface; second, they are adsorbed; and finally, they unfold at the interface to adopt a thermodynamically optimized conformation. In addition, proteins form a continuous viscoelastic film around the oil droplets or air bubbles that stabilize emulsions and foams (1). Therefore, the formation of a stable foam or emulsion is a complex phenomenon that depends on the physicochemical characteristics of the protein, such as net charge, solubility, hydrophobicity, flexibility, etc.(2). Protein structure can be intentionally modified in order to improve these surface properties. Such protein modifications can be easily performed by enzymatic or chemical treatments. Enzymatic hydrolysis improves the solubility of proteins, even if the degree of hydrolysis is low. The increase of ionic groups after hydrolysis makes the peptides more soluble with respect to the original protein throughout the pH range (3,4), and consequently enhances the diffusion of the protein and facilitates the formation of emulsions (5). In addition, enzymatic hydrolysis can increase the surface hydrophobicity of peptides by exposing hydrophobic groups that are generally buried in the core of nat...

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Functional properties of glycosylated derivatives of the 11S storage protein from pea (Pisum sativum L.)

Cited by 39 publications

References 28 publications

Rheological behavior of wheat gliadins in 50% (v/v) aqueous propanol

Rheological behavior of wheat gliadins in 50% (v/v) aqueous propanol

Legumes seeds protein isolates in the production of ascorbic acid microparticles

Emulsifying and foaming properties of native and chemically modified peptides from the 2S and 12S proteins of rapeseed (Brassica napus L.)

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