Re-formation of Fibrils from Hydrolysates of β-Lactoglobulin Fibrils during in Vitro Gastric Digestion

Bateman, Libei; Ye, Aiqian; Singh, Harjinder

doi:10.1021/jf2020057

Cited by 40 publications

(21 citation statements)

References 33 publications

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“…Hydrolysis and reaggregation were supposed as a synchronous process. Equilibrium existed between the dissociation of the peptides from the original fibrils and the self‐assembly of β ‐lactoglobulin peptides into the new fibrils after pepsin treatment (Bateman et al ., ). However, the reforming mechanism of β ‐conglycinin fibrils was somewhat different from that of β ‐lactoglobulin fibrils.…”

Section: Resultsmentioning

confidence: 99%

Effects of pepsin hydrolysis on the soy β‐conglycinin aggregates formed by heat treatment at different pH

Yang

Zhang

2014

Int J of Food Sci Tech

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Summary The effects of pepsin hydrolysis on the β‐conglycinin aggregates formed by heat treatment at different pH were investigated. Results showed that fibrils were still observed, whereas the random aggregates were easily to be digested in the simulated gastric fluid. Electrophoresis and molecular weight analysis indicated that large aggregates still existed after pepsin treatment for fibrils. Hydrolysis resulted in changes in the apparent viscosity (ηapp) of 6% fibril solutions. The ηapp at the shear rate range (0–30 s−1) increased in the order of fibrils < fibrils with pepsin for 60 min < fibrils with pepsin for 30 min. Smaller peptide/fibril fragments were generated, and additional aggregates were reformed during the hydrolysis process, as evidenced by thioflavin T and atomic force microscopy images. The native β‐conglycinin hydrolysates comprised a mixture of polypeptides enriched in about 47 kDa. These findings would provide valuable information about effects of enzymatic hydrolysis on plant oligometric globulin aggregates.

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Section: Resultsmentioning

confidence: 99%

Effects of pepsin hydrolysis on the soy β‐conglycinin aggregates formed by heat treatment at different pH

Yang

Zhang

2014

Int J of Food Sci Tech

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“…It has been reported that amyloid fibrils formed from bovine milk derived b-lactoglobulin are readily digested in vitro by pepsin (Bateman, Ye, & Singh, 2010) and that the hydrolysates themselves are able to reform new fibrils with different morphologies (Bateman, Ye, & Singh, 2011). These intriguing results stand in some contrast to one of the hallmarks of true amyloid fibrils, that is the high resistance towards hydrolysis by proteases such as trypsin and Proteinase K (Watts et al, 2011).…”

Section: Abbreviationsmentioning

confidence: 99%

Evaluation of protease resistance and toxicity of amyloid-like food fibrils from whey, soy, kidney bean, and egg white

et al. 2016

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“…In addition, the increase in aggregate size detected using nanopore detection is in good agreement with literature. [13] The pepsin cleaves highly hydrophobic amino acid and aromatic amino acid residues of β-lactoglobulin amyloid (e.g., leucine, isoleucine, phenylalanine, valine, and tryptophan). It also has a preferential tendency toward the cleavage of peptide bonds adjacent to leucine residues, that is, LX (or XL) bonds.…”

Section: Pepsin Enzymatic Degradation Of β-Lactoglobulin Amyloidsmentioning

confidence: 99%

Characterization of Food Amyloid Protein Digestion by Conical Nanopore

et al. 2020

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from β-lactoglobulin show several interesting features, such as the high aspect ratio (length vs diameter) making them a structuring agent in foods, stabilizers of foam and in emulsions as well as building blocks of microcapsules. [8] The applications of β-lactoglobulin fibrils in food products require a deep understanding of fibril digestion processes occurring during passage through the stomach and the intestine. [9] Indeed, certain amyloids such as tau, α-synuclein or β-peptides are involved in neurodegenerative diseases. [10] The protein fibril digestion can cleave the fibrils to oligomers with a potential increased pathogenic [11,12] or contribute to the formation of new fibrils as seeds. [13] To date, the investigation of the nondisease-related amyloid-like fibrils degradation combining kinetic and identification of species are difficult due to the difficulty to obtain both information using the same technique. Nanopore technology is one of the most promising approaches to protein sensing. [14,15] It allows single molecule detection providing information about the size, shape as well as charge. [16,17,18] Nanopores are also a platform to characterize the protein conformational change including folding/ unfolding. [19] Biological nanopores take advantage of their precise structure, allowing the characterization of polypeptide length and the identification of amino-acids, [20] opening a new avenue for protein sequencing. [21,22] On the other hand, they were used to detect small oligomers of peptides [23] and antibody prion interactions. [24] Solid-state nanopores and nanopipettes allow the characterization of the protein and peptide oligomerization giving also information on their morphology. [25] This makes them a candidate to develop new analytical tools for amyloid sensing. [26] However, their diameter and their short lifetime don't allow protofibril detection nor long time analysis. We recently reported that conical track-etched nanopore is likely the most suitable candidate to investigate the protein aggregation from small aggregates to protofibrils scale. [27] In this report, β-lactoglobulin aggregation was studied, discriminating between oligomer and protofibril populations. In addition, the long nanopore lifetime and the possibility to perform long time experiments, is suitable to analyze the digestion of β-lactoglobulin aggregates. The most relevant physiological proteases in digestion process are pepsin (stomach) and trypsin (small intestine). β-lactoglobulin aggregates are used as structuring agents in food processing. Their enzymatic degradation follows different pathways depending on the enzyme and the pH. The transient species produced during the degradation process are difficult to characterize under continuous measurement. Here, conical track-etched nanopores are used to investigate the β-lactoglobulin degradation by pepsin (pH 2) and trypsin (pH 9). Before enzyme addition, two distinct populations, oligomers and protofibrils, are identified. Just after enzyme addition, the aggregate size decr...

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Re-formation of Fibrils from Hydrolysates of β-Lactoglobulin Fibrils during in Vitro Gastric Digestion

Cited by 40 publications

References 33 publications

Effects of pepsin hydrolysis on the soy β‐conglycinin aggregates formed by heat treatment at different pH

Effects of pepsin hydrolysis on the soy β‐conglycinin aggregates formed by heat treatment at different pH

Evaluation of protease resistance and toxicity of amyloid-like food fibrils from whey, soy, kidney bean, and egg white

Characterization of Food Amyloid Protein Digestion by Conical Nanopore

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