Enzyme-Induced Formation of β-Lactoglobulin Fibrils by AspN Endoproteinase

Akkermans, C.; Venema, Paul; Goot, Atze Jan van der; Boom, R.M.; Linden, Erik van der

doi:10.1007/s11483-008-9094-3

Cited by 39 publications

(26 citation statements)

References 15 publications

(20 reference statements)

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“…However, monomers and large peptides have been found in amyloid‐like β‐LG fibrils after microwave heating at 80 °C and pH 2.0 (Hettiarachchi, Melton, Gerrard, & Loveday, ). Fibrils can also be formed at room temperature and pH 2.0 from a peptide mixture obtained by hydrolysis of β‐LG with AspN endoproteinase (Akkermans, Venema, van der Goot, Boom, & van der Linden, ). Ghadami, Khodarahmi, Ghobadi, Ghasemi, and Pirmoradi () suggested that some of the lysine residues in β‐LG are of critical importance in the aggregation process.…”

Section: Bovine Milk Proteinsmentioning

confidence: 99%

Conditions Governing Food Protein Amyloid Fibril Formation. Part II: Milk and Legume Proteins

Lambrecht

Jansens

Rombouts

et al. 2019

Comp Rev Food Sci Food Safe

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Both intrinsic and extrinsic factors impact amyloid formation of food proteins. We here review the impact of various conditions and food constituents on amyloid fibrillation of milk and legume proteins. Much less is known about casein and legume protein amyloid‐like fibril formation than about that of whey proteins such as β‐lactoglobulin, α‐lactalbumin, and bovine serum albumin. Proteins of both sources are often studied after heating under strong acidic (pH < 3) conditions. The latter induces changes in protein conformation and often peptide hydrolysis. At higher pH values, alcohols, chaotropic and/or reducing agents induce the conformational changes required to enhance fibrillation. Different types of food proteins can impact each other's fibrillation. Also, the presence of other food constituents can enhance or reduce it. No general conclusions on the mechanisms or impact of different food constituents on food proteins can be made. Optimal conditions for AF formation, that is, heating for several days at low pH, are rare in food processing. However, this does not exclude the possibility of AF formation in food products. For example, slow cooking of hydrolyzed proteins may enhance it. Future research should focus on the prevalence of AFs in complex food systems or model systems relevant for food processing.

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Section: Bovine Milk Proteinsmentioning

confidence: 99%

Conditions Governing Food Protein Amyloid Fibril Formation. Part II: Milk and Legume Proteins

Lambrecht

Jansens

Rombouts

et al. 2019

Comp Rev Food Sci Food Safe

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show abstract

“…These can be made by heating an acidic protein or peptide solution under some stirring, which leads to both hydrolysis and fibril assembly at the same time, albeit at a different rate. The fibril length depends on reaction-time and shear rate (Akkermans et al 2008), and they have been used to reinforce microcapsules (Kroes-Nijboer et al 2012, Rossier-Miranda et al 2010. Recently, β-LG fibrils were found not only to provide a more elastic interface compared to native β-LG, but also a better oxidative stability to encapsulated fish oil core (Serfert et al 2014).…”

Section: Biopolymersmentioning

confidence: 99%

Food-grade micro-encapsulation systems that may induce satiety via delayed lipolysis: A review

Corstens

Berton‐Carabin

Vries

et al. 2015

Critical Reviews in Food Science and Nutrition

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The increasing prevalence of overweight and obesity requires new, effective prevention and treatment strategies. One approach to reduce energy intake is by developing novel foods with increased satiating properties, which may be accomplished by slowing down lipolysis to deliver substrates to the ileum, thereby enhancing natural gut-brain signaling pathways of satiety that are normally induced by meal intake. To develop slow release food additives, their processing in the gastrointestinal tract has to be understood; therefore, we start from a general description of the digestive system and relate that to in vitro modeling, satiety, and lipolytic mechanisms. The effects of physicochemical lipid composition, encapsulation matrix, and interfacial structure on lipolysis are emphasized. We give an overview of techniques and materials used, and discuss partitioning, which may be a key factor for encapsulation performance. Targeted release capsules that delay lipolysis form a real challenge because of the high efficiency of the digestive system; hardly any proof was found that intact orally ingested lipids can be released in the ileum and thereby induce satiety. We expect that this challenge could be tackled with structured o/w-emulsion-based systems that have some protection against lipase, e.g., by hindering bile salt adsorption and/or delaying lipase diffusion.

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“…In that case both gelation and hydrolysis took place at pH 8. Enzymatic hydrolysis was also induced in the case of β -lactoglobulin, but at pH 7, and electron microscopy reveals fi bril formation only after the pH was changed to 2 [20] . Thus, the pH is important in the aggregation and thought to affect the interaction between the according peptides before fi brillization.…”

Section: Protein -Based Fibrilsmentioning

confidence: 99%

Enzyme-Induced Formation of β-Lactoglobulin Fibrils by AspN Endoproteinase

Cited by 39 publications

References 15 publications

Conditions Governing Food Protein Amyloid Fibril Formation. Part II: Milk and Legume Proteins

Conditions Governing Food Protein Amyloid Fibril Formation. Part II: Milk and Legume Proteins

Food-grade micro-encapsulation systems that may induce satiety via delayed lipolysis: A review

Food Functionality and the Physics of Bionanotechnology: Some Examples and Challenges

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