Effect of hydrolysis of casein by plasmin on the heat stability of milk

Crudden, Anthony; Afoufa-Bastien, Damien; Fox, Patrick F.; Brisson, G. J.; Kelly, Alan L.

doi:10.1016/j.idairyj.2004.11.001

Cited by 38 publications

(29 citation statements)

References 39 publications

(42 reference statements)

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“…The diff erences in protein composition between our data and data from our cited sources could be infl uenced by genetic factors and the feeding system (Barłowska et al, 2012;Brodziak at al., 2015;Król et al, 2011;Kuczyńska et al, 2012a;Kuczyńska et al, 2012b), and/or by partial hydrolysis of proteins, which was supported by the presence of peptides in the examined milk. This hydrolysis could be the result of native milk enzyme activity (plasmin) and/or proteases originating from incidental milk microfl ora (Crudden et al, 2005;Ismail and Nielsen, 2010;Yasser et al, 2010). During electrophoresis, as a result of hydrolysis, some peptides with a molecular mass similar to alpha-albumin could be produced, which, when the proteins were separated, was found in the same band.…”

Section: Resultsmentioning

confidence: 99%

“…It was observed that plasmin hydrolytic activity diminishes after pasteurisation, sometimes by more than dozens of percent, but the activator of plasminogen inhibitor denatures, which allows for the activation of plasminogen which in turn transforms into plasmin and the hydrolysis of casein continues. Plasmin most often shows the tendency to hydrolyse β-casein, but it was also observed that it acted against other caseins, with little or no activity against α-lactalbumin and β-lactoglobulin (Crudden et al, 2005;Ismail and Nielsen, 2010;Yasser et al, 2010). According to Lorenzen et al (2011) the content of proteins in pasteurised milk was not diff erent from that in raw milk, and only the ratios of individual proteins is changed as a result of denaturation and interactions between proteins.…”

Section: Resultsmentioning

confidence: 99%

“…The transformations of proteins are key to obtaining accurate information about the properties of dairy products such as cheeses and fermented drinks. Proteins can be also used by harmful or pathogenic microorganisms to support their metabolism, which has an adverse eff ect on the dairy product and sometimes leads to the creation of hydrolysed products which are harmful to humans Crudden et al, 2005;Ismail and Nielsen, 2010;Ng-Kwai-Hang, 2003;Szwajkowska et al, 2011). Milk proteins subjected to hydrolysis can be also a source of biologically active peptides with diff erent and pro-health properties (Meisel, 1997;Meisel, 1998;Szwajkowska et al, 2011).…”

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The changes of proteins fractions shares in milk and fermented milk drinks

Bonczar

Walczycka

Duda

2016

Acta Sci Pol Technol Aliment

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Background. The aim of this research was to observe the changes which take place in the electrophoretic picture of milk proteins after pasteurisation and inoculation with diff erent starter cultures (both traditional and probiotic). After incubation, the yoghurt, kefi r, acidifi ed milk, fermented Bifi dobacterium bifi dum drink and Lactobacillus acidophillus drink were chilled for 14 days to observe the changes which occurred. Materials and methods. The research materials were raw and pasteurised milk, as well as fermented milkbased drinks. The raw milk used for research came from Polish Holstein-Fresian black and white cows. The milk was sampled 3 times and divided into 5 parts, each of which was pasteurised at 95°C for 10 min and then cooled for inoculation: yoghurt to 45°C, kefi r and acidifi ed milk to 22°C and drinks with Bifi dobacterium bifi dum and Lactobacillus acidophillus to 38°C. Milk was inoculated with lyophilised, direct vat starter cultures, in an amount equal to 2% of the working starter. For the production of fermented drinks, the subsequent starters were applied: "YC-180" Christian Hansen for yoghurt, "D" Biolacta-Texel-Rhodia for kefi r, CH-N--11 Christian Hansen for acidifi ed milk, starter by Christian Hansen for the probiotic Bifi dobacterium bifi dum milk, starter by Biolacta-Texel-Rhodia for the probiotic Lactobacillus acidophillus milk. The analyses were conducted in raw, pasteurised and freshly fermented milk as well as in milk drinks stored for 14 days. The total solid content was estimated by the drying method; the fat content by the Gerber method; the lactose content by the Bertrand method; the protein content by the Kjeldahl method with Buchi apparatus; the density of milk was measured with lactodensimeter; acidity with a pH-meter; and potential acidity by Soxhlet-Henkl method (AOAC, 1990). The electrophoretic separation of proteins in raw and pasteurised milk, as well as in freshly produced milk drinks and those stored for 14 days, was performed with SDS-PAGE (on polyacrylamid gel) basing on procedure described by Laemmli (1970). Results. It was shown that, in comparison with raw milk, the pasteurised milk had smaller amounts of αs-, β-and κ-casein, whereas the shares of γ-casein and peptides were greater, and there were no changes in immunoglobulin, α-lactalbumin or β-lactoglobulin levels, which indicated that hydrolysis of caseins had occurred. In all freshly fermented milk drinks, a drop in αs-and β-casein was observed relative to raw milk. An increase in peptides and γ-casein was also noticed (with the exception of acidifi ed milk). There were diff erences in α-lactalbumin and β-lactoglobulin levels between the diff erent drinks: raw, pasteurised or freshly fermented milk. It was shown that kefi r, compared to the other drinks, had the lowest levels of αs-and β-casein, α-lactalbumin and of peptides, as well as the highest level of γ-casein, which is evidence of an increased rate of hydrolysis in that drink. It was stated that, during the storage of fermented milk drin...

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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The changes of proteins fractions shares in milk and fermented milk drinks

Bonczar

Walczycka

Duda

2016

Acta Sci Pol Technol Aliment

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“…After 92 days of storage, the zeta potential of casein micelles was −16.6 and −14.0 mV, and their hydration was 2.0 and 1.55 g of water per gramme of dried pellet for the UHT control milk and UHT milk manufactured from raw milk contaminated with P. fluorescens, respectively (Fig.3). A reduction in the zeta potential related to the release of peptides containing negatively charged groups such as glutamyl, aspartyl, phosphoseryl and glycosidic residues (N-terminal fragments of κ-casein) was also described by Gastaldi et al (2003) and Crudden et al (2005). The decrease of both these factors which are considered as stability factors of casein micelles can be related to changes in the structure of casein micelles induced by proteolysis.…”

Section: Discussionmentioning

confidence: 95%

Proteolysis of casein micelles by Pseudomonas fluorescens CNRZ 798 contributes to the destabilisation of UHT milk during its storage

Gaucher

Tanguy

Fauquant

et al. 2011

Dairy Science & Technol.

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“…The specificity of plasmin on the caseins is well established, but most studies in this area have been in model systems (e.g., in buffers); whether the action on caseins in the micellar state is similar has been less well studied, and the effects of plasmin on the properties of the casein micelle itself (e.g., size, charge, structure) are poorly understood, but may be significant in terms of effects on, for example, the rennet coagulation and heat stability of milk (Crudden et al, 2005a;Crudden, Afoufa-Bastien, Fox, Brisson, & Kelly, 2005b).…”

Section: Article In Pressmentioning

confidence: 99%