Microbiological and Chemical Changes in High-Pressure-Treated Milk during Refrigerated Storage

García-Risco, Mónica Rodríguez; Cortés, Enrique Claver; Carrascosa, Alfonso V.; López‐Fandiño, Rosina

doi:10.4315/0362-028x-61.6.735

Cited by 60 publications

(28 citation statements)

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“…The low level of proteolysis is probably due to the low activity of plasmin at refrigeration temperatures. Garcia-Risco et al [7] observed little difference between the level of proteolysis in untreated milk and milk treated at 400 MPa for 30 min, during storage at 7°C for 15 d; however, in the present study (Tab. II) milk treated under such conditions had slightly faster proteolysis than untreated milk on storage at 5 °C.…”

Section: Discussioncontrasting

confidence: 82%

Plasmin activity and proteolysis in high pressure-treated bovine milk

Huppertz

Fox

Kelly

2004

Lait

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-In this study, proteolysis resulting from the action of the indigenous milk proteinase, plasmin, in high pressure (HP)-treated raw skim bovine milk during storage was examined. Plasmin activity was reduced by treatment at pressures ≥400 MPa and decreased further throughout 28 d of storage at 5°C. In untreated milk or milk treated at 100 MPa plasmin activity increased during the first 3 d of storage at 37°C, indicating activation of plasminogen; considerably less activation occurred in milk treated at 200-600 MPa. However, considerable decreases in plasmin activity, probably due to autolysis, were apparent in all samples on storage at 37°C for >3 d. Proteolysis, as measured by increases in the level of pH 4.6-soluble N and decreases in the level of β-casein, was very limited on storage of milk at 5°C, with little difference between untreated and HP-treated samples. Proteolysis on storage of milk at 37°C was influenced only slightly by treatment of milk at a pressure ≤250 MPa and was reduced considerably in milk treated at 600 MPa for 30 min, but in milk treated at 300-400 MPa, proteolysis was more extensive than in untreated milk, possibly as a result of HP-induced disruption of casein micelles. Overall, HP can either induce or reduce proteolysis in milk, and may therefore have implications for products made from such milk.High pressure / milk / proteolysis / plasmin / casein micelle Résumé -Activité de la plasmine et protéolyse dans un lait de bovin traité par hautes pressions. Dans cette étude, nous nous sommes intéressés à la protéolyse résultant de l'activité d'une protéinase indigène du lait, la plasmine, au cours de l'incubation d'un lait de bovin frais écrémé et traité par hautes pressions. L'activité de la plasmine était réduite par un traitement à des pressions ≥400 MPa et diminuait progressivement au cours des 28 j de stockage à 5°C. Pour un lait non traité ou traité à 100 MPa, l'activité de la plasmine augmentait pendant les trois premiers jours d'incubation à 37°C, indiquant l'activation du plasminogène ; l'activation était bien moins importante pour un lait traité à des pressions comprises entre 200 et 600 MPa. Cependant, des diminutions considé-rables de l'activité de la plasmine, probablement due à une autolyse, étaient observées pour tous les échantillons incubés à 37 °C pour des durées de stockage >3 j. La protéolyse, mesurée par les augmentations du taux d'azote soluble à pH 4,6 et par les diminutions du taux de caséine β résiduelle, était très limitée pour un stockage du lait à 5°C, avec une petite différence entre les échantillons non traités et ceux traités aux hautes pressions. La protéolyse durant l'incubation du lait à 37°C était seulement légèrement influencée par le traitement du lait à des pressions ≤250 MPa et était considérablement réduite pour un lait traité à 600 MPa pour 30 min, mais pour un lait traité à 300-400 MPa, la protéolyse était plus importante que dans un lait non traité, cela étant probablement dû à la désintégration des micelles de caséine induite par les haut...

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Section: Discussioncontrasting

confidence: 82%

Plasmin activity and proteolysis in high pressure-treated bovine milk

Huppertz

Fox

Kelly

2004

Lait

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“…In milk, plasmin activity was reported to resist at least 400 MPa for 30 min at 25 1C (Garcı´a-Risco, Corte´s, Carrascosa, & Lo´pez-Fandin˜o, 1998). Huppertz et al (2004g) found that treatments at 400 and 600 MPa at 20 1C for 30 min reduced plasmin activity by 30% and 75%, respectively.…”

Section: Effects Of High Pressure On Native Milk Enzymesmentioning

confidence: 96%

High pressure-induced changes in milk proteins and possible applications in dairy technology

López‐Fandiño

2006

International Dairy Journal

133

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“…Quantification of the levels of denatured b-Lg present in the casein fraction showed that pressure-induced b-Lg denaturation was not reversible during two months at 77C [46]. The same CZE method was used to follow the distribution of proteins, after the separation of the micellar and serum phases of pressurized milks by ultracentrifugation, which was related with mineral changes and technological properties of pressurized milks [47].…”

Section: Assessment Of Technological Processesmentioning

confidence: 99%

Capillary electrophoresis for the analysis of food proteins of animal origin

2001

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In recent years, capillary electrophoresis (CE) has become an analytical technique with many applications in the study of food proteins and peptides. This review describes the existing CE methods of analysis of milk, egg, meat and fish proteins and peptides. The major developments in the application of CE to solve different problems in food technology, such as the assessment of technological processes, quality, and authenticity control of animal foods, are considered. A section dealing with future directions on the analysis of food proteins by CE is also included.

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Microbiological and Chemical Changes in High-Pressure-Treated Milk during Refrigerated Storage

Cited by 60 publications

References 0 publications

Plasmin activity and proteolysis in high pressure-treated bovine milk

Plasmin activity and proteolysis in high pressure-treated bovine milk

High pressure-induced changes in milk proteins and possible applications in dairy technology

Capillary electrophoresis for the analysis of food proteins of animal origin

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