Effect of thermal treatment on interfacial properties of β-lactoglobulin
TL;DR: The changes in the secondary conformation and surface hydrophobicity of β-lactoglobulin subjected to different thermal treatments were characterized at pH values of 7, 5.5 and 4 using circular dichroism (CD) and hydrophobic dye binding as discussed by the authors.
About: This article is published in Journal of Colloid and Interface Science.The article was published on 2005-05-01. It has received 144 citations till now. The article focuses on the topics: Thermal treatment.
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TL;DR: In this paper, the authors reviewed the literature on the formation and the structure of β-lactoglobulin and whey protein isolate (WPI) aggregates in aqueous solution induced by heating.
481 citations
TL;DR: Fixation of BPB to myofibrils increased with heating time and temperature, strongly suggesting that it may be closely related to protein hydrophobicity.
340 citations
TL;DR: The authors summarizes the principal new developments reported in the research literature from 2000 (inclusive) to the present date, on the topic of foam and bubble stabilization, in the context of foods.
Abstract: This review summarizes the principal new developments reported in the research literature from 2000 (inclusive) to the present date, on the topic of foam and bubble stabilization, in the context of foods. The main areas covered are novel foamed products, processes and foaming agents; new methods of study; protein adsorption and competitive adsorption; surface rheology; particle-stabilized systems; modelling, simulation and theory.
298 citations
TL;DR: This review is to present a comprehensive summary of the knowledge about emulsifying and interfacial properties of soy proteins, achieved during the past decades, and to provide an insight in understanding the role of conformational flexibility in their emulsification properties.
Abstract: Soy proteins as important food ingredients exhibit a great potential to be widely applied in food formulations, due to their good nutrition, functional properties and health effects. The knowledge about the structure-function relationships of these proteins is crucial for their applications, but still very scant, especially that on their molecular mechanism of emulsification. The purpose of this review is to present a comprehensive summary of the knowledge about emulsifying and interfacial properties of soy proteins, achieved during the past decades, and particularly to provide an insight in understanding the role of conformational flexibility in their emulsifying properties. The interplays between the emulsifying and interfacial properties are also elucidated. For these proteins, the conformational flexibility rather than the surface hydrophobicity is the crucial parameter determining their emulsification performance. On the other hand, evidence is fast growing to indicate that because of the insoluble nature, soy proteins are a kind of unique materials to perform as food-grade Pickering stabilizers. The knowledge about the Pickering emulsion stabilization is distinctly different from that for conventional emulsions stabilized by soy proteins. Thus, different strategies should be employed to develop soy proteins into a kind of effective emulsifiers, depending on the preference of emulsification performance or emulsion stability.
232 citations
Cites background from "Effect of thermal treatment on inte..."
...In this regard, Kim et al. (2005) had made an interesting investigation on native and heated b-lactogloublin-coated oil droplets, and found that heating improved the interfacial surface elasticity and viscosity, and the improvement was closely related to the increased resistance to coalescence of…...
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TL;DR: The interfacial behaviors of heated protein may be mainly associated with more flexible conformation and high free sulfhydryl group, even if some exposed hydrophobic groups are involved in the formation of aggregates.
Abstract: We evaluated the influence of heat treatment on interfacial properties (adsorption at the oil-water interface and dilatational rheology of interfacial layers) of soy protein isolate. The related structural properties of protein affecting these interfacial behaviors, including protein unfolding and aggregation, surface hydrophobicity, and the state of sulfhydryl group, were also investigated. The structural and interfacial properties of soy protein depended strongly on heating temperature (90 and 120 °C). Heat treatment at 90 °C induced an increase in surface hydrophobicity due to partial unfolding of protein, accompanied by the formation of aggregates linked by disulfide bond, and lower surface pressure at long-term adsorption and similar dynamic interfacial rheology were observed as compared to native protein. Contrastingly, heat treatment at 120 °C led to a higher surface activity of the protein and rapid development of intermolecular interactions in the adsorbed layer, as evidenced by a faster increase of surface pressure and dilatational modulus. The interfacial behaviors of this heated protein may be mainly associated with more flexible conformation and high free sulfhydryl group, even if some exposed hydrophobic groups are involved in the formation of aggregates. These results would be useful to better understand the structure dependence of protein interfacial behaviors and to expand utilization of heat-treated protein in the formulation and production of emulsions.
221 citations
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TL;DR: The effective hydrophobicity determined fluorometrically showed significant correlations with interfacial tension and emulsifying activity of the proteins studied.
1,238 citations
TL;DR: In this paper, the mean residue ellipticity, [theta], at any wavelength, lambda, of a protein in aqueous solution is expressed as ε = fH[theta]H infinity(1-k/n) + f beta[thet]beta + ft[thetea]t + fR[ theta]R with two constraints: 1 > or = fj > 0 and sigma fj = 1.
1,042 citations
TL;DR: In this paper, the rates of change of film pressure (π) and surface concentration (Γ) of protein during adsorption of β-casein, bovine serum albumin (BSA), and lysozyme at the air-water interface have been monitored by the Wilhelmy plate and surface radioactivity methods, respectively.
773 citations
01 Jul 1979
TL;DR: In this paper, the molecular structures of β-casein, bovine serum albumin (BSA), and lysozyme films at the air-water and oil-water interfaces were determined.
Abstract: The adsorption data presented in the preceding paper (Part II of this series) have been used to deduce the molecular structures of β-casein, bovine serum albumin (BSA), and lysozyme films at the air-water and oil-water interfaces. The hydrophobic, disordered β-casein molecules are more surface-active than the globular BSA and lysozyme molecules. β-Casein is in an all-train configuration at low surface pressures (π 10−2 wt%) giving films thicker than 100 A. Although the primary layer is irreversibly adsorbed, molecules in subsequent layers are reversibly adsorbed. Lysozyme molecules are denatured at low π values (π < 8 mN m−1), and at higher values essentially native molecules (which are reversibly adsorbed) coexist in the surface film. Much residual native structure remains even in the denatured film because lysozyme is very resistant to denaturation. At the oil-water interface, the adsorbed lysozyme molecules are denatured to a greater extent than those at the air-water interface; native molecules are not stable at this interface. The adsorbed BSA molecules contain residual native structure, but there is no abrupt conformational change in the film at a particular packing density. The structure at the air-water interface is intermediate to those of lysozyme and β-casein. BSA has the same π-A curve as lysozyme at the oil-water interface.
616 citations
TL;DR: Adsorption isotherms for the three proteins β-casein, bovine serum albumin, and lysozyme at the air-water and oil-water interfaces have been determined independently using ellipsometry and surface radioactivity methods; the surface pressure and surface potential were also monitored as mentioned in this paper.
440 citations