Effect of Different Electrolytes on Heat-Stability Curves of Milk from Cows Free from Udder Infections

Feagan, J. T.; Griffin, Ashley; Lloyd, G.T.

doi:10.3168/jds.s0022-0302(66)88002-5

Cited by 6 publications

(2 citation statements)

References 5 publications

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“…At pH values above about 7-3, an increase in serum concentration introduced a second CT minimum (Fig. 11a), an effect which Feagan, Griffin & Lloyd (1966) observed with some milks adjusted to this pH level by the addition of phosphate (Na 2 HPO 4 ). The cause of a second CT minimum at high pH values where milk would be expected to maintain a high stability to heat, possibly through the non-formation or disruption of the /c-casein//?-lactoglobulin complex (Sweetsur & White, 1974) in addition to an increased net negative charge on the micelles, may again be a consequence of increasing calcium phosphate formation, or of a special effect of phosphate ions, as suggested by Feagan et al (1966).…”

Section: Discussionmentioning

confidence: 80%

Studies on the heat stability of milk protein: III. Effect of heat-induced acidity in milk

Sweetsur

White

1975

Journal of Dairy Research

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SUMMABY. An examination was made of the effect of varying the protein, lactose and total serum ion content of milk on the rate of production of heat-induced acidity (as measured by pH decrease), on heat stability (as measured by coagulation time), on the relationship between coagulation time and initial pH of milk (as measured by coagulation time-pH curves) and on the interrelationship of these parameters. In addition, the effect on these parameters and their interrelationship of varying the composition and volume of the headspace atmosphere in contact with the milk was investigated. Explanations are proposed for the observed effects on heat stability of varying the composition of milk and the heating conditions, with special reference to the influence of heat-induced acidity.Although the recent investigations of Sweetsur & White (1974, 1975) and many others have confirmed the important relation between the pH and heat stability of milk (as measured by coagulation time) first clarified by Rose (1961aRose ( , b, 1963 and Tessier & Rose (1964), little work appears to have been done on the influence of heat-induced acidity on coagulation time (CT). Pyne & McHenry (1955) found that the decrease in the pH of milk heated at 130 °C was roughly proportional to CT at 130 °C. Nearly one-half of total heat-induced acidity was derived from the decomposition of lactose, and the remainder from the formation of tricalcium phosphate from phosphate liberated from casein and from soluble phosphate initially present. They concluded that heat-induced acidity is normally a factor in the heat coagulation of milk. The purpose of the present investigation was to make a more extensive examination of factors that contribute to heat-induced acidity and of the influence this acidity may have on CT and hence on the relationship between CT and the initial pH of milk. EXPERIMENTAL

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Section: Discussionmentioning

confidence: 80%

Studies on the heat stability of milk protein: III. Effect of heat-induced acidity in milk

Sweetsur

White

1975

Journal of Dairy Research

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“…Phosphate salts have been extensively used as stabilizers in the dairy industry for the stabilization of concentrated milk. Rose (1961b, c) attributed the stabilizing effect to the changes in the pH brought about by the addition of stabilizers, but later Feagan (1966) and Sweetsur & Muir (1980b), proposed that factors other than the pH are also responsible for the stabilization. , attributed the stabilizing action of orthophosphate salts in evaporated milk to the decrease in the amount of diffusable calcium prior to concentration.…”

Section: Effect Of Addition Of Cross-linked Waxy Maize Phosphatementioning

confidence: 99%

Milk protein-carbohudrate interactions in sterilised milk products

Τζιμπουλά¹

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The present work deals with the nature of milk-protein carbohydrate interactions during the heat treatment of milk. Starches of different botanical origin were added (0.5-1.5% w/w) to milk (9% TS or 22% TS) and the mixtures were preheated at 70°C to ensure gelatinization of the starch granules. The heat stability of the milk-starch mixtures was defined as the time required for the coagulation of the milk proteins to occur on heating at 140°C (skim milk of 9% TS) or at 120°C (concentrated milk 22% TS), over the pH range, 6.5-7.1. On addition of native starches there was a reduction in the coagulation time of milk. The various starches hadsimilar effects on the coagulation time of milk, the destabilisation being proportional to the amount of starch added. The destabilisation of milk was not associated either with the amylose to amylopectin ratio of the starches sor to the granular structure of the starch. Further experiments probed the effects on heat stability of changing the molecular structure of starch in two ways: a) by the addition of acid modified starches and b) by the addition of cross-linked starches. Both types of treatment promoted a reduction in the water-binding capacity of the starch and both resulted in an improvement of the coagulation time of the milk-carbohydrate mixture. However,complete recovery of the heat stability was achieved only in the case of unconcentrated milk. Most of the research to date on milk proteincarbohydrate interactions has involved acidic polysaccharides, whereas there is limited information for non-ionic gums. Due to the importance of the heat stability of milk in the dairy industry it was useful to initiate this study by investigating the effect of various forms of carbohydrates on the stability of the milk proteins upon heating.

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Milk Proteins in Prospect

McKenzie¹

1971

Milk Proteins

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Effect of Different Electrolytes on Heat-Stability Curves of Milk from Cows Free from Udder Infections

Cited by 6 publications

References 5 publications

Studies on the heat stability of milk protein: III. Effect of heat-induced acidity in milk

Studies on the heat stability of milk protein: III. Effect of heat-induced acidity in milk

Milk protein-carbohudrate interactions in sterilised milk products

Milk Proteins in Prospect

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