Food Biophysics of Protein Gels: A Challenge of Nano and Macroscopic Proportions

Foegeding, E. Allen

doi:10.1007/s11483-005-9003-y

Cited by 101 publications

(72 citation statements)

References 71 publications

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“…Depending on parameters such as pH or the nature and species of ions in the protein solutions, the resulting heat-induced gels may be translucent fine-stranded networks or opaque particulate gels, each with distinctive rheological properties [11]. Research is required to study the "food biophysics" of protein gels [8], and Raman spectroscopy can be a useful tool to detect molecular structural changes that may distinguish fine-stranded and particulate gels [11,12]. Figure 1A shows the Raman spectra of β-lactoglobulin in solution (at pH 7.0, no added salt) and the translucent finestranded gel obtained after heating the solution at 80…”

Section: Heat-induced Fine-stranded and Particulate Gelsmentioning

confidence: 99%

Vibrational spectroscopy applied to the study of milk proteins

Li‐Chan¹

2007

Lait

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-Vibrational spectroscopy is a versatile tool for analysis of foods including dairy products. This paper provides an overview of techniques that may be useful to study structural properties and interactions of milk proteins. Specific examples of recent research conducted in our laboratory using Raman, micro-Raman and FT-Raman spectroscopy will be described to illustrate their applications for investigating protein-protein, protein-lipid, and protein-polysaccharide interactions, and for elucidating structure-function relationships of whey proteins and peptides. Raman spectroscopy was used to discriminate between structural changes of β-lactoglobulin in transparent fine-stranded versus particulate gels. Formation of particulate gel structures led to a more hydrophilic or exposed microenvironment around tryptophan residues, compared to a more hydrophobic microenvironment in translucent gels. A decrease in the α-helical content was more pronounced in translucent gels, while both types of gels retained considerable β-sheet structures, consistent with the known heat-resistance of the β-barrel structure of β-lactoglobulin. Principal component similarity analysis demonstrated that heat treatment and heat-κ-carrageenan interactions were the most influential factors affecting whey protein structure as monitored by spectral changes. Raman micro-spectroscopy was applied to investigate protein-lipid interactions at the interface between bovine serum albumin solution and mineral or corn oil. While Raman bands assigned to aromatic and aliphatic residues inferred involvement of hydrophobic interactions at the oil-water interface, the secondary structure was not significantly altered. Temperature-dependent changes in the Raman C-H stretching region of liposomes composed of phospholipids with varying headgroups and acyl chains were influenced by the presence of bovine lactoferricin. This approach may be useful to elucidate the interactions of cationic antimicrobial peptides with bacterial versus host cell membranes. A diverse range of other applications as well as new developments in techniques are emerging in the literature, indicating the potential for increasing use of vibrational spectroscopy in the analysis of milk and milk products. Résumé -Spectroscopie vibrationnelle appliquée à l'étude des protéines. La spectroscopie vibrationnelle est un outil adéquat pour l'analyse des aliments, dont des produits laitiers. Cet article présente une revue des techniques qui peuvent être utiles pour étudier les propriétés structurales et les interactions entre protéines laitières. Des exemples spécifiques de recherches récentes conduites dans notre laboratoire utilisant la spectroscopie Raman, micro-Raman et FT-Raman sont décrites pour illustrer leurs applications dans l'étude des interactions protéines/protéines, protéines/lipides et protéines/polysaccharides, et dans l'élucidation des relations structure/fonction des protéines et peptides du lactosérum. La spectroscopie Raman a été utilisée pour faire la distinction entre les c...

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Section: Heat-induced Fine-stranded and Particulate Gelsmentioning

confidence: 99%

Vibrational spectroscopy applied to the study of milk proteins

Li‐Chan¹

2007

Lait

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“…The driving force for gelation can be a physical process, such as heat or pressure, or a chemical process, such as acid, ionic, or enzymatic reaction (Stokes 2012;Dissanayake et al 2013). Among these, the most common method for forming food gels with globular proteins is by heating (Foegeding 2006;Nicolai et al 2011). It is known that heating at relatively high temperatures (>60 °C) results in thermal denaturation of globular whey proteins (Pereira et al 2011;Nicolai and Durand 2013).…”

Section: Introductionmentioning

confidence: 99%

Production of Whey Protein-Based Aggregates Under Ohmic Heating

Pereira

Rodrigues

Ramos

et al. 2015

Food Bioprocess Technol

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Formation of whey protein isolate protein aggregates under the influence of moderate electric fields upon ohmic heating (OH) has been monitored through evaluation of molecular protein unfolding, loss of its solubility, and aggregation. To shed more light on the microstructure of the protein aggregates produced by OH, samples were assayed by transmission electron microscopy (TEM). Results show that during early steps of an OH thermal treatment, aggregation of whey proteins can be reduced with a concomitant reduction of the heating charge-by reducing the comeup time (CUT) needed to reach a target temperature-and increase of the electric field applied (from 6 to 12 V cm −1 ). Exposure of reactive free thiol groups involved in molecular unfolding of β-lactoglobulin (β-lg) can be reduced from 10 to 20 %, when a CUT of 10 s is combined with an electric field of 12 V cm −1 .Kinetic and multivariate analysis evidenced that the presence of an electric field during heating contributes to a change in the amplitude of aggregation, as well as in the shape of the produced aggregates. TEM discloses the appearance of small fibrillar aggregates upon the influence of OH, which have recognized potential in the functionalization of food protein networks. This study demonstrated that OH technology can be used to tailor denaturation and aggregation behavior of whey proteins due to the presence of a constant electric field together with the ability to provide a very fast heating, thus overcoming heat transfer limitations that naturally occur during conventional thermal treatments.

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“…heating), which will help to unfold native structure of protein molecule, exposing it to further reactions. Despite these gelation methods being often used in combination, the most common used to form food gels with globular proteins is heating (Foegeding, 2006). Thermal gelation is a phenomenon that typically encompasses three stages: primary aggregation through covalent (e.g.…”

Section: Gelationmentioning

confidence: 99%

Design of whey protein nanostructures for incorporation and release of nutraceutical compounds in food

Ramos

Pereira

Martins

et al. 2017

Critical Reviews in Food Science and Nutrition

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Whey proteins are widely used as nutritional and functional ingredients in formulated foods because they are relatively inexpensive, generally recognized as safe (GRAS) ingredient, and possess important biological, physical, and chemical functionalities. Denaturation and aggregation behavior of these proteins is of particular relevance toward manufacture of novel nanostructures with a number of potential uses. When these processes are properly engineered and controlled, whey proteins may be formed into nanohydrogels, nanofibrils, or nanotubes and be used as carrier of bioactive compounds. This review intends to discuss the latest understandings of nanoscale phenomena of whey protein denaturation and aggregation that may contribute for the design of protein nanostructures. Whey protein aggregation and gelation pathways under different processing and environmental conditions such as microwave heating, high voltage, and moderate electrical fields, high pressure, temperature, pH, and ionic strength were critically assessed. Moreover, several potential applications of nanohydrogels, nanofibrils, and nanotubes for controlled release of nutraceutical compounds (e.g. probiotics, vitamins, antioxidants, and peptides) were also included. Controlling the size of protein networks at nanoscale through application of different processing and environmental conditions can open perspectives for development of nanostructures with new or improved functionalities for incorporation and release of nutraceuticals in food matrices.

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Food Biophysics of Protein Gels: A Challenge of Nano and Macroscopic Proportions

Cited by 101 publications

References 71 publications

Vibrational spectroscopy applied to the study of milk proteins

Vibrational spectroscopy applied to the study of milk proteins

Production of Whey Protein-Based Aggregates Under Ohmic Heating

Design of whey protein nanostructures for incorporation and release of nutraceutical compounds in food

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