Phospholipid/Fatty Acid-Induced Secondary Structural Change in <i>β</i>-Lactoglobulin during Heat-Induced Gelation

Ikeda, Shinya; Ea, Foegeding; Cc, Hardin

doi:10.1021/jf990434h

Cited by 21 publications

(13 citation statements)

References 36 publications

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“…The effect of phosphatidylcholine (PC) and fatty acids (butyrate, oleate, and palmitate) on heat‐induced aggregation of β‐Lg is influenced by the presence of salt (Ikeda and others ). In the absence of salt, both lipid types increased the storage modulus (G′) of heat‐induced gels, but they prevented heat‐induced loss of α‐helix structure which occurs during denaturation.…”

Section: Approaches To Reduce Aggregation Of Whey Proteinsmentioning

confidence: 99%

Stability of Whey Proteins during Thermal Processing: A Review

Wijayanti

Bansal

Deeth

2014

Comp Rev Food Sci Food Safe

297

186

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Whey proteins have many benefits due to their high nutritional value and their various applications in food products. A drawback of whey proteins is their instability to thermal processing, which leads to their denaturation, aggregation, and, under some conditions, gelation. As thermal processing is a major treatment in the processing of milk and milk products, its influence on whey proteins has been extensively studied. Understanding the mechanisms involved during each stage of denaturation and aggregation of whey proteins is critical to devising ways of improving their stability. These aspects are reviewed in this paper. Also covered are approaches to preventing or reducing heat-induced aggregation of whey proteins. Inhibition of aggregate formation has considerable potential for alleviating the problems that arise from the instability of whey proteins.

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Section: Approaches To Reduce Aggregation Of Whey Proteinsmentioning

confidence: 99%

Stability of Whey Proteins during Thermal Processing: A Review

Wijayanti

Bansal

Deeth

2014

Comp Rev Food Sci Food Safe

297

186

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“…The latter reactions are known to occur in milk upon heating. Protein -fatty acid interactions can also change the secondary structure of b-Lg upon heating or even at room temperature with oleic acid (Ikeda et al 2000). Since some b-Lg can be present at the lipid interface in homogenized milk, such interactions can occur and their effect on protein allergenicity needs to be investigated, regardless of heat treatments.…”

Section: Milk Allergymentioning

confidence: 99%

On the supposed influence of milk homogenization on the risk of CVD, diabetes and allergy

Michalski

2007

Br J Nutr

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Commercial milk is homogenized for the purpose of physical stability, thereby reducing fat droplet size and including caseins and some whey proteins at the droplet interface. This seems to result in a better digestibility than untreated milk. Various casein peptides and milk fat globule membrane (MFGM) proteins are reported to present either harmful (e.g. atherogenic) or beneficial bioactivity (e.g. hypotensive, anticarcinogenic and others). Homogenization might enhance either of these effects, but this remains controversial. The effect of homogenization has not been studied regarding the link between early cow's milk consumption and occurrence of type I diabetes in children prone to the disease and no link appears in the general population. Homogenization does not influence milk allergy and intolerance in allergic children and lactose-intolerant or milk-hypersensitive adults. The impact of homogenization, as well as heating and other treatments such as cheesemaking processes, on the health properties of milk and dairy products remains to be fully elucidated.

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“…Glycation by the Maillard reaction is a ubiquitous reaction of condensation of a reducing sugar with the amino groups of proteins. 48 PC protected BLG from degradation under duodenal conditions and altered the pattern of the digestion products. The glycosylation of BLG in Maillard reaction under mild conditions does not alter the protein structure, except a slight increase in its Stokes radius and an increase in the temperature of denaturation.…”

Section: Chemical Modificationsmentioning

confidence: 99%

The modifications of bovine β-lactoglobulin: Effects on its structural and functional properties

Stanić-Vučinić

Veličković

2013

J Serb Chem Soc

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Due to its excellent techno-functional properties, high nutritional value and low cost, β-lactoglobulin (BLG), the main protein in whey, is a frequently used additive in wide range of food products. It is also considered as an acid-resistant drug carrier for the delivery of pharmaceutical and nutraceutical agents. However, BLG is the main allergen of milk. A variety of methods has been explored for the modification of BLG in attempts to improve its functional properties and to decrease its allergenicity. Due to its compact globular structure, BLG is relatively resistant to modifications, especially under mild conditions. BLG can be modified by physical, chemical and enzymatic treatments. Although chemical modifications offer efficient routes to the alteration of the structural and functional properties of proteins, they are associated with safety concerns. In the last decade, there is a tendency for application of novel non-thermal physical processing methods, as well as enzymes in order to obtain BLG derivatives with desirable properties. The objective of this review is to overview the chemical, physical and enzymatic processing techniques utilized to modify BLG and their effects on the structural and functional properties of BLG.

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Phospholipid/Fatty Acid-Induced Secondary Structural Change in β-Lactoglobulin during Heat-Induced Gelation

Cited by 21 publications

References 36 publications

Stability of Whey Proteins during Thermal Processing: A Review

Stability of Whey Proteins during Thermal Processing: A Review

On the supposed influence of milk homogenization on the risk of CVD, diabetes and allergy

The modifications of bovine β-lactoglobulin: Effects on its structural and functional properties

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