scispace - formally typeset
Search or ask a question
Journal ArticleDOI

Controlled food protein aggregation for new functionality

TL;DR: In this article, the authors discuss how the formation of aggregates with different morphologies is related to the creation of either particulate or fine stranded gels, and make a distinction between primary aggregation leading to roughly spherical particles or more or less flexible strands and secondary aggregation leads to fractal clusters, gels or precipitates.
Abstract: Globular proteins are an important component of many food products. Heat-induced aggregation of globular proteins gives them new properties that can be useful in food products. In order to optimize functionality, the aggregation process needs to be controlled, which in turn requires good understanding of the mechanism. Heating aqueous solutions of globular proteins leads to the formation of aggregates with one of four distinctly different morphologies: spherical particles, flexible strands, semi-flexible fibrils, and fractal clusters. We review recent research in this area focusing on the parameters that control the morphology including the influence of hydrolysis. The aggregation mechanism and the effect of the morphology on the functionality will be addressed. A distinction is made between primary aggregation leading to roughly spherical particles or more or less flexible strands and secondary aggregation leading to fractal clusters, gels or precipitates. We will discuss how the formation of aggregates with different morphologies is related to the formation of either particulate or fine stranded gels.
Citations
More filters
Journal ArticleDOI
TL;DR: A recent review as discussed by the authors describes recent advances in the stabilization of emulsions and foams by edible particles of nanoscale and micro-scale dimensions, including common food proteins such as whey protein, soy protein and gelatin.

326 citations

Journal ArticleDOI
TL;DR: The biological fate and the potential toxicity mechanisms of food amyloid fibrils are discussed, and an experimental protocol for their health safety validation is proposed in the concluding part of the review.

238 citations

Journal ArticleDOI
TL;DR: This review article focuses on versatile mechanisms for gelation of globular proteins and highlights the current studies on whey and soy protein hydrogels as two key animal and herbal proteins used in fabricating coating materials.
Abstract: Background Bioactive molecules are mostly amenable to degradation at processing, storage, and harsh digestion conditions. Hence, high-throughput encapsulation bodies must be designed in a way to protect them from destructive circumstances and to enhance their bioavailability. Scope and approach This review article focuses on versatile mechanisms for gelation of globular proteins and highlights the current studies on whey and soy protein hydrogels as two key animal and herbal proteins used in fabricating coating materials. Moreover, different categories of hydrogels, such as aerated hydrogels, hydrogels made from aggregated forms of proteins, hydrogels originated from food-grade materials, and hydrogels with nano scale dimensions are discussed. Key findings and conclusions The gelation and particulation method have dramatic effects on the liberation features as well as the bioactivity of the wrapped ingredients. Therefore, different approaches are needed to be considered in order to increase the bioavailability of nutraceuticals and drugs accommodated within protein hydrogels. Accordingly, there is a growing trend for developing innovative modes of gelation and immobilizing bioactive materials into the hydrogel network.

237 citations

Journal ArticleDOI
TL;DR: This review attempts to give a concise overview of recent progress made in mechanistic understanding of protein aggregation, particulate formation and protein solution rheology and highlights some areas of controversy and debate that need further attention from the scientific community.
Abstract: In this review, we attempt to give a concise overview of recent progress made in mechanistic understanding of protein aggregation, particulate formation and protein solution rheology. Recent advances in analytical techniques and methods for characterizing protein aggregation and the formed protein particles as well as advancements, technique limitations and controversies in the field of protein solution rheology are discussed. The focus of the review is primarily on biotherapeutics and proteins/antibodies that are relevant to that area. As per the remit of Current Opinion in Colloid and Interface Science, here we attempt to stimulate interest in areas of debate. While the field is certainly not mature enough that all problems may be considered resolved and accepted by consensus, we wish to highlight some areas of controversy and debate that need further attention from the scientific community.

220 citations


Cites background from "Controlled food protein aggregation..."

  • ...Understanding and controlling aggregation kinetics is another key aspect to gaining insights into the aggregation mechanism and the resulting final aggregate microstructure[6,41]....

    [...]

  • ...In food based systems, the food protein selfassembly, microstructure and resulting rheological properties must be characterized and controlled in order to ensure optimized textural/sensory experiences for the consumer and ensure issue-free processing [5, 6]....

    [...]

Journal ArticleDOI
TL;DR: In this article, the effect of polymer-surfactant interactions on the rheology of emulsion gel systems is explained, and irreversible and reversible clustering of oil droplets as the basis of making emulsion particulate gels is deliberated.
Abstract: Background Emulsion gels are a class of soft solid-like materials. These composite materials are structurally either a polymeric gel matrix into which emulsion droplets are incorporated (emulsion-filled gels), or a network of aggregated emulsion droplets (emulsion particulate gels). Emulsion gels are increasingly used in pharmaceutics, cosmetics and food industries. Scope and approach This article reviews fabrication methods of emulsion gels, and describes factors that influence gel properties and functionality. Effect of polymer-surfactant interactions on the rheology of emulsion gel systems is explained. Then, irreversible and reversible clustering of oil droplets as the basis of making emulsion particulate gels is deliberated. Key Findings and Conclusions Oil droplets depending on their interfacial composition act as either active or inactive fillers in an emulsion-filled gel. Actively functioning oil droplets can increase gel modulus, whereas, inactive oil droplets typically weaken gel texture. Interactions between surfactants and polymers, which influences filler affinity to gel matrix, have significant consequences on emulsion gel rheology. For protein-based emulsion gels, surfactant may also influence proteins unfolding and aggregation. In situ gelation of an emulsion can be triggered by environmental factors such as temperature changes during processing and storage or by physiological stimuli such as acidic pH in the stomach. The clustering approach, which is used to form emulsion particulate gels may be utilized to control digestibility of lipids in the gastrointestinal tract. The capability of encapsulating two or more different lipophilic components within a single delivery system may be achieved via heteroaggregation technique.

178 citations

References
More filters
Journal ArticleDOI
TL;DR: The relative importance of the common main-chain and side-chain interactions in determining the propensities of proteins to aggregate is discussed and some of the evidence that the oligomeric fibril precursors are the primary origins of pathological behavior is described.
Abstract: Peptides or proteins convert under some conditions from their soluble forms into highly ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging from neurodegenerative disorders to systemic amyloidoses. In this review, we identify the diseases known to be associated with formation of fibrillar aggregates and the specific peptides and proteins involved in each case. We describe, in addition, that living organisms can take advantage of the inherent ability of proteins to form such structures to generate novel and diverse biological functions. We review recent advances toward the elucidation of the structures of amyloid fibrils and the mechanisms of their formation at a molecular level. Finally, we discuss the relative importance of the common main-chain and side-chain interactions in determining the propensities of proteins to aggregate and describe some of the evidence that the oligomeric fibril precursors are the primary origins of pathological behavior.

5,897 citations

Journal ArticleDOI
TL;DR: In this paper, a review describes developments in the formation and properties of food-grade emulsion systems based on traditional edible dispersed particles (fat crystals), commercial nanoparticles (silica nanoparticles), and novel particles of biological origin (starch microparticles, chitin nanocrystals).
Abstract: Solid particles of nanoscale and microscale dimensions are becoming recognized for their potential application in the formulation of novel dispersed systems containing emulsified oil or water droplets. This review describes developments in the formation and properties of food-grade emulsion systems based on traditional edible dispersed particles (fat crystals), commercial nanoparticles (silica nanoparticles), and novel particles of biological origin (starch microparticles, chitin nanocrystals). The special features characterizing the properties of particle-stabilized droplets are highlighted in comparison with those of conventional protein-stabilized emulsions. Complexities arising from synergistic interactions of particles with other surface-active ingredients are discussed.

494 citations

Journal ArticleDOI
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

Journal ArticleDOI
TL;DR: In this paper, the effects of pH on the gel network structure have been characterized by means of different microscopy techniques, and the results of the microstructure correlated with previously published data on fracture properties.

401 citations

Journal ArticleDOI
TL;DR: This review will focus on integrating the colloidal/polymer and biological aspects of protein functionality using foams and gels to illustrate colloidal-polymer aspects and bioactive peptides and allergenicity to demonstrate biological function.

329 citations