Chaperone-like food components: from basic concepts to food applications

Abstract

The significance of chaperones in preventing protein aggregation including amyloid fibril formation has been extensively documented in the biological field, but there is limited research on the potential effect of chaperone-like molecules on food protein functionality and food quality. This review is intended to extend the potential of chaperone and chaperone-like molecules in the prevention of food protein aggregation and amyloid fibril formation. The common features of chaperone molecules responsible for suppressing aggregation and amyloid fibril formation are firstly presented. Then, the function and applicability of chaperone and chaperone-like molecules in food products, in particular high-protein beverages where aggregation and fibril formation are undesirable, are extensively discussed. Protein aggregation in high-protein beverages can be prevented by chaperone or chaperone-like components, such as caseins, heme-containing proteins, specific peptide fragments, phospholipids and polyphenols. The diversity of chaperone-like components and mechanisms might provide the flexibility in taking advantage of their potential applications in different food products.

Casein as a Modifier of Whey Protein Isolate Gel: Sensory Texture and Rheological Properties

“…It is possible that caseins are not interacting with WPs and just acting as particles dispersed in the aqueous phase. Alternatively, the casein could be acting as holdase chaperones and altering aggregation and gel network formation of WPs (Akbari et al., ). Attempts to differentially stain caseins and WPs did not show conclusive results (data not show), so the composition of the network was not identified.…”

“…When milk is heated, denatured β‐lactoglobulin aggregates with κ‐casein to form appendages at the casein micelle surface (Mottar, Bassier, Joniau, & Baert, ) via hydrophobic interactions (Haque, Kristjansson, & Kinsella, ) and disulfide bonding (Jang & Swaisgood, ). Alternatively, when the concentration of WP is higher than casein, isolated β‐ and α s1 ‐ and α s2 ‐caseins exhibit holdase chaperone activity by forming complexes with denatured WP and, thereby, inhibiting aggregation (Akbari, Bamdad, & Wu, ; Bhattacharyya & Das, ; Kehoe & Foegeding, ; Yong & Foegeding, , ). Also, casein‐based ingredients, such as sodium caseinate, can produce a similar effect (Guyomarc'h, Nono, Nicolai, & Durand, ).…”

Inhibition of heat‐induced protein aggregation by zirconium phthalocyanines

“…Recent studies revealed that specific proteins found in food sources (such as peas, soy, kidney beans, milk, meat, and eggs) have aggregation propensities and form high‐stable filamentous structures—amyloid fibrils 5 . Protein aggregation can lead to undesirable turbidity, precipitation, and higher viscosity of high‐protein beverage products for patients during long‐term hospitalization 6 . It was also recently shown that feeding mice with amyloid fibrils resulted in the amyloid deposition in the gastrointestinal tract, heart, and liver 5 .…”

“…This is why several compounds are studied as agents suppressing aggregation and amyloid fibril formation of BLG and other food proteins. It was shown that protein aggregation in protein‐containing food could be prevented by heme‐containing proteins and polyphenolic compounds 6 …”

“…5 Protein aggregation can lead to undesirable turbidity, precipitation, and higher viscosity of high-protein beverage products for patients during long-term hospitalization. 6 It was also recently shown that feeding mice with amyloid fibrils resulted in the amyloid deposition in the gastrointestinal tract, heart, and liver. 5 Amyloid fibrils of some food proteins could remain intact as they pass the gastrointestinal tract due to their resistance to proteolysis.…”