Effect of dissociation and conformational changes on the surface behavior of pea legumin

Subirade, Muriel; Guéguen, Jacques; Schwenke, K. D.

doi:10.1016/0021-9797(92)90045-n

Cited by 54 publications

(42 citation statements)

References 23 publications

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“…Although systematic studies dealing with pea-protein-adsorption at the air-water and oil-water interfaces have been published [17][18][19] , the kinetics of acidtreated-pea-proteins adsorption have not been systematically studied so far. So, in this work, we complement previous studies on dynamic properties of adsorbed pea proteins films and emulsifying characteristics of acid-treated pea proteins aqueous solutions.…”

Section: Introductionmentioning

confidence: 99%

Interfacial and Emulsifying Characteristics of Acid-treated Pea Protein

et al. 2009

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This work presents equilibrium and dynamic aspects for the adsorption at the oil-water interface of pea (Pisum sativum L.) protein isolate (PPI). Dynamic interfacial tension, γ, and surface viscoelasticity modulus, ε, were determined using pendant-drop method. Adsorption kinetics studies revealed that pea proteins adsorb faster at pH 7.0 than at acidic pH (pH 2.4). On the other hand, the measured ε is lower at pH 7.0. This is probably due to fast adsorption, leading to the formation of inhomogeneous film structures. In fact, compared with pHs above the isoelectric point (pI4.3), acidic conditions slow down the adsorption, but the modulus is increased. Pea-protein-stabilized emulsions are more stable to creaming at acidic pH and their particle-size distributions are more homogeneous in these conditions. Effect of pH on interfacial properties and on properties of oil-in-water emulsions stabilized by PPI was interpreted in terms of pea protein solubility, globulin dissociation, and oil-droplet surface electrostatic charge. We propose that at acidic conditions, adsorbed dissociated globulins form stronger and denser viscoelastic networks when adsorbed at oil-water interface. Consequently, the pH-dependence of pea-globulin-stabilized emulsions properties could be of great interest to tune barrier properties of oil/water interfacial membranes for several applications such as encapsulation and controlled release of lipophilic bioactive components within the food, medical, and pharmaceutical industries.

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Section: Introductionmentioning

confidence: 99%

Interfacial and Emulsifying Characteristics of Acid-treated Pea Protein

et al. 2009

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“…In the other fractions with lower foam stability these are most likely associated into quaternary protein structures. Similar positive effects of dissociation of multichain proteins have been described for legume proteins (Subirade, Guéguen, & Schwenke, 1992;Wagner & Guéguen, 1995). From pH 6 downwards, foam stabilities decreased for all fractions and in the pH range 3e4 no stable foams can be produced with any fraction after removal of the precipitated protein by centrifugation.…”

Section: Effect Of Ph On the Stability Of Foams Stabilized With The Dmentioning

confidence: 56%

Effect of charged polysaccharides on the techno-functional properties of fractions obtained from algae soluble protein isolate

et al. 2014

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“…Schwenke and Linow [15] could observe a dissociation of the 12S globulin from rapeseed into the 7S half molecules at pH 8.0 and I L 0. Subirade et al observed also a decreasing CAC after pH induced dissociation of pea legumin [16].…”

Section: Discussionmentioning

confidence: 92%

“…In previous experiments the relaxation process was found to level to constant surface pressures within 10 min [16]. Therefore the stress relaxation was monitored here within 10 min too.…”

Section: Surface Pressure Measurements and Stress Relaxationmentioning

confidence: 98%