Hydrolysis of β‐casein by gastric proteases

Guillou, Hervé; Miranda, Guy; Pélissier, J.P.

doi:10.1111/j.1399-3011.1991.tb00766.x

Cited by 31 publications

(4 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the case of the native 8-casein, 26 peptides were collected and identified. The determination of 23 bonds cleaved by pepsin have been achieved, 12 of them being previously reported by Guillou et al (28). Cleavage at bonds Glu2-Leu3, Leu140-Gln141 and Metl56-Phe 157 shown by Guillou was not confirmed in this study.…”

Section: Hydrolysis Of 8-casein and P-caseiti Derivativesmentioning

confidence: 46%

“…The Leu198-Gly199 cleavage site was observed during the hydrolysis of the both ester derivatives. The hydrolysis of the bond Met156-Phe157 by pepsin in ethyl derivative was already obtained in native 8-casein by Guillou et al (28).…”

Section: Hydrolysis Of 8-casein and P-caseiti Derivativesmentioning

confidence: 80%

“…Multiple p-casein peptic peptides have been identified by (iuillou etal. (28) and Chobert et al (29). Tryptic hydrolysis of 8-casein has been studied by Chobert et al (30) and Leonil eta].…”

mentioning

confidence: 95%

See 2 more Smart Citations

Peptic proteolysis of esterified β‐casein and β‐lactoglobulin

Briand¹,

Chobert²,

Haertlé³

1995

International Journal of Peptide and Protein Research

View full text Add to dashboard Cite

Moderate esterification induces slight secondary structure changes in two major milk proteins, β‐lactoglobulin and β‐casein. Esterification of β‐lactoglobulin prompts its tertiary structure‘melting′, opening it to peptic cleavage. Twenty‐two new cleavage sites were characterised in β‐lactoglobulin and five in β‐casein. Some of them are due to esterification‐improved peptide bond accessibility, some to the bias of pepsin specificity by glutamate and aspartate esters. The resulting fragmentation yields original and partially amphiphilic peptide populations.

show abstract

Section: Hydrolysis Of 8-casein and P-caseiti Derivativesmentioning

confidence: 46%

Section: Hydrolysis Of 8-casein and P-caseiti Derivativesmentioning

confidence: 80%

See 1 more Smart Citation

Peptic proteolysis of esterified β‐casein and β‐lactoglobulin

Briand¹,

Chobert²,

Haertlé³

1995

International Journal of Peptide and Protein Research

View full text Add to dashboard Cite

show abstract

“…In addition to the cleavage of κ-CN into para-κ-CN and caseinomacropeptide (CMP), it has also been demonstrated that chymosin has a proteolytic action on α S1 -and α S2 -CNs [20,21], as well as on β-casein [10]. In addition to studying the effect of short time pasteurisation on milk protein composition, it would also be interesting to separate and identify chymosin-produced cleavage products in milk by use of proteome analysis.…”

Section: Introductionmentioning

confidence: 99%

Different proteomic profiles of sweet whey and rennet casein obtained after preparation from raw versus heat-treated skimmed milk

Larsen

Wedholm-Pallas

Lindmark-Månsson³

et al. 2010

Dairy Sci. Technol.

View full text Add to dashboard Cite

-Proteomic profiles of sweet whey and rennet casein fractions prepared from raw or pasteurised (72°C for 15 s), skimmed milk were studied by proteomics coupled with the detection of protein spots by MALDI TOF mass spectrometry. Proteins were analysed by a modification of the traditional, two-dimensional gel electrophoresis (2-DGE) method under non-reducing running conditions, which potentially permits the visualisation of disulphide-linked protein complexes formed in response to pasteurisation. Separated proteins were stained with Coomassie blue. The relative spot volumes obtained after 2-DGE of fractions from raw or pasteurised milk were compared. A number of different spots in the rennet casein and sweet whey fractions were found to vary in response to pasteurisation. Some of these represented higher molecular mass complexes that increased in the chymosin-precipitated casein fraction, and they were identified by mass spectrometry to contain α S1 -casein. Certain fragments of α S1 -casein, probably generated as a result of chymosin cleavage, increased in the whey after pasteurisation. The whey content of proteose peptone component 3 (PP3) or lactophorin decreased after pasteurisation, which could indicate increased association of PP3 with for example the milk fat globule membrane after pasteurisation. This shows that gel-based proteome analysis can be used in the characterisation of subtle variations in protein composition of milk fractions that occur as a consequence of pasteurisation.proteome analysis / sweet whey / rennet casein / pasteurisation Article published by EDP SciencesRésumé -Différents profils protéomiques obtenus à partir de lactosérum doux et de caséine présure issus de laits écrémés crus ou traités thermiquement. Les profils protéomiques de fractions obtenus à partir de lactosérum doux et de caséine présure de lait écrémé cru ou pasteurisé (72°C, 15 s) ont été étudiés par des analyses protéomiques couplées à une détection des spots protéiques par spectrométrie de masse MALDI TOF. Les protéines ont été analysées par électro-phorèse sur gel bidimensionnelle (EG-2D) avec une modification de la méthode classique, sous conditions non réductrices, permettant la visualisation des complexes de protéines liées par ponts disulphure formés en réponse à la pasteurisation. Les protéines séparées étaient colorées au bleu de Coomassie. Les volumes relatifs des spots obtenus après EG-2D des fractions obtenues à partir de lait cru ou pasteurisé ont été comparés. Un nombre de spots différents était trouvé dans les fractions de caséine présure et de lactosérum doux en réponse à la pasteurisation. Certains spots représen-taient des complexes de masse moléculaire plus élevée qui augmentaient dans la fraction de caséine obtenue par précipitation due à la chymosine et qui contenaient des caséines alpha S1 identifiées par spectrométrie de masse. Certains fragments de caséine alpha S1, probablement obtenus après clivage par la chymosine, augmentaient dans le lactosérum après pasteurisation. La teneur du lactos...

show abstract

Characterization of Food Amyloid Protein Digestion by Conical Nanopore

et al. 2020

View full text Add to dashboard Cite

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...

show abstract

Hydrolysis of β‐casein by gastric proteases

Cited by 31 publications

References 18 publications

Peptic proteolysis of esterified β‐casein and β‐lactoglobulin

Peptic proteolysis of esterified β‐casein and β‐lactoglobulin

Different proteomic profiles of sweet whey and rennet casein obtained after preparation from raw versus heat-treated skimmed milk

Characterization of Food Amyloid Protein Digestion by Conical Nanopore

Contact Info

Product

Resources

About