Changes of the Proteins in Cheddar Cheese Made from Milk Heated at Different Temperatures

Melachouris, Nicholas; Tuckey, S.L.

doi:10.3168/jds.s0022-0302(66)87949-3

Cited by 23 publications

(8 citation statements)

References 8 publications

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“…Electrophoresis in starch gels, which was first applied to cheese by Melachouris and Tuckey (1966), has been used by sorne workers to separate caseins or their degradation products in cheese or other products (eg, Vreeman and van Reil, 1990;van den Berg and de Koning, 1990;de Koning et al, 1992) and is quite effective. Although starch gel electrophoresis gives far better results than earlier zonal techniques and MOIT(1971) c1aimed that it gave superior resolution of lower-mobility and cationic peptides than polyacrylamide gels, starch gels are brittle and opaque after staining (Creamer, 1991) and have been largely replaced by polyacrylamide gels.…”

Section: Electrophoresismentioning

confidence: 99%

Chemical methods for the characterization of proteolysis in cheese during ripening

McSweeney

Fox

1997

Lait

147

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Summary -Proteolysis is the principal and most complex biochemical event which occurs during the maturation of most cheese varieties. Proteolysis has been the subject of much study and a range of analytieal techniques has been developed to assess its extent and nature. Methods for assessing proteolysis can he c1assified under two broad headings: non-specifie and specifie techniques, both of which are reviewed. Non-specifie techniques include the quantitation of nitrogen soluble in various extractants or precipitants and the Iiberation of reactive groups. Specifie techniques include those which resolve individual peptides or free amino acids, principally chromatography or electrophoresis. Techniques are often combined into a fractionation scheme for cheese nitrogen to facilitate the isolation of individual peptides. Methods for the identification of individual peptides are also reviewed. Strategies for assessing proteolysis in various cheese varieties are discussed.proteolysis / cheese ripening / methodology Résumé -Méthodes chimiques pour la caractérisation de la protéolyse des fromages durant l'affinage. La protéolyse, qui est le phénomène principal et le plus complexe intervenant dans la maturation de la plupart des fromages, a été le sujet de nombreuses études. Toute une gamme de techniques analytiques a été développée afin de permettre une meilleure compréhension de ce phénomène. Les méthodes de suivi de la protéolyse peuvent être classées en deux grands chapitres, traités dans cette revue: les techniques non spécifiques, et les techniques spécifiques. Les techniques non spécifiques incluent la quantification de l'azote soluble dans les divers extraits, et s'intéressent aussi à la libération des groupements réactifs. Les techniques spécifiques, principalement la chromatographie ou l'élec-trophorèse, sont celles permettant de séparer les peptides ou les acides aminés libres. Ces diverses techniques sont souvent combinées dans la stratégie de purification de la fraction azotée du fro-

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Section: Electrophoresismentioning

confidence: 99%

Chemical methods for the characterization of proteolysis in cheese during ripening

McSweeney

Fox

1997

Lait

147

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“…The use of aseptic cheese vats and defined strains of starter bacteria has demonstrated that the starter alone could be responsible for the development of distinct Cheddar cheese flavour (Visser, 1977;Visser & de Groot-Mostert, 1977), although such cheeses lacked the full flavour of a mature typical Cheddar (Perry & McGillivray, 1964;Reiter et al, 1969). The quantitative and qualitative differences of proteolysis in cheeses manufactured from pasteurized instead of raw milk were attributed to deactivation of native milk enzymes (or destruction of microorganisms) and alteration of the milk component structure via thermally induced interactions of proteins that constrain the proteolytic action of rennet in the cheese curd (Sherwood, 1936;Melachouris & Tuckey, 1966;O'Keefe et al, 1976). Lau et al (1991) compared cheeses manufactured from raw and pasteurized milk using sophisticated analytical techniques and concluded that both the extent and characteristics of proteolysis were altered by pasteurization.…”

Section: Pasteurizationmentioning

confidence: 99%

Influence of pasteurization of milk and addition of starter cultures on protein breakdown in ovine cheeses manufactured with extracts from flowers of Cynara cardunculus

Sousa

Malcata

1996

Food Chemistry

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Ovine cheeses were manufactured from raw milk (R), pasteurized milk without starter addition (P), and pasteurized milk with starter addition (PS), using in all cases extracts of Cynara cardunculus as rennet and mimicking as far as possible the traditional manufacture process. The microbial counts were higher in R cheeses than in P cheeses, and the lowest microbial counts were found for PS cheeses. Such physicochemical characteristics as moisture, fat, protein, NaCl content, and pH of the three types of cheeses were similar to one another at each sampling time. In particular, pasteurization had no significant effect on protein breakdown as evaluated by either the water-soluble nitrogen, the trichloroaceticacid (TCA)-soluble nitrogen, or the phosphotungstic acid (PTA)-soluble nitrogen fractions. However, the TCA-soluble and the PTA-soluble fractions for the PS cheeses ripened for more than 28 days were higher than those for the R or P cheeses at similar ripening times. The cheeses and their water-soluble extracts could not be distinguished by urea-polyacrylamide gel electrophoresis for up to 7 days, but clear differences were apparent at 68 days of ripening for the PS cheeses with respect to the R and P cheeses.

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“…K-Casein is totally hydrolyzed during milk coagulation (Melachouris and Tuckey 1966), whereas para-K-casein is not hydrolyzed during cheese ripening (Green andFoster 1974, Ledford et al 1966). This latter result, together with the relatively low concentration and amino acid composition ofK-casein, would suggest that it is not an important source of bitter peptides in cheese.…”

Section: Introductionmentioning

confidence: 99%

Hydrolysis of κ-casein in solution by chymosin, plasmin, trypsin and Lactobacillus -proteinases

Pihlanto-Leppälä

Pahkala

Antila

1993

AFSci

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The aim of this study was to examine the enzymatic hydrolysis of K-casein by isolating and identifying the released peptides. The enzymes employed in the study were chymosin, plasmin and trypsin, as well as a cell-free extract from three Lactobacillus helveticus and nine Lactobacillus casei strains.The findings showed that the bond most sensitive to the proteolytic activity of chymosin was the Phe 105-Met 106. After 24 hours of hydrolysis a few other bonds in the casein macropeptide were also cleaved. Plasmin was found to have weak proteolytic activity under the conditions of this study. When the enzyme-substrate ratio was raised from 1:200 to 1:50, a few peptides were released from the N-terminal region. Trypsin was found to hydrolyze several K-casein bonds, and peptides were released from almost all regions of the protein.The proteases ofLactobacillus had less effect than chymosin, plasmin or trypsin. The strains could be divided into three categories. L. helveticus strains had activity on bonds in the mid-section and C-terminal region, L casei strains EB, P 3, P 8 and A 1 had activity on bonds in the N-and C-terminal regions, while L. casei A 5 and M 9 had activity only on bonds in the C-terminal region.

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Changes of the Proteins in Cheddar Cheese Made from Milk Heated at Different Temperatures

Cited by 23 publications

References 8 publications

Chemical methods for the characterization of proteolysis in cheese during ripening

Chemical methods for the characterization of proteolysis in cheese during ripening

Influence of pasteurization of milk and addition of starter cultures on protein breakdown in ovine cheeses manufactured with extracts from flowers of Cynara cardunculus

Hydrolysis of κ-casein in solution by chymosin, plasmin, trypsin and Lactobacillus -proteinases

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