The effect of concentration on the heat stability of skim-milk

1978 ◽  
Vol 45 (1) ◽  
pp. 37-45 ◽  
Author(s):  
D. D. Muir ◽  
A. W. M. Sweetsur
Keyword(s):  
Opposite Effect ◽  
Skim Milk ◽  
Heat Stability ◽  
Progressive Change ◽  
Ph Profile ◽  
Total N ◽  
Heated Milk ◽  
Depletion Curve ◽  
Concentrated Milk ◽  
Β Lactoglobulin

SummaryA progressive change takes place in the heat stability of skim-milk during concentration. At the maximum in the coagulation time (CT)–pH profile of milk concentrated to over 20% of total solids (TS) the total N depletion curve changed from single- to 2-stage and CT became insensitive to the addition of urea. Furthermore, addition of β-lactoglobulin to skim-milk concentrates destabilized the heated milk whilst the opposite effect was observed in the presence of sulphydryl-group blocking agents. As a result of these observations, it has been suggested that the mechanism of coagulation in concentrated milk is similar to that which occurs within the minimum of the CT–pH profile of skim-milk at normal levels of TS.

Effects of added salts on the heat stability of recombined concentrated milk

1990 ◽  
Vol 57 (2) ◽  
pp. 213-226 ◽  
Author(s):  
Mary-Ann Augustin ◽  
Phillip T. Clarke
Keyword(s):  
Skim Milk ◽  
Heat Stability ◽  
Ph Control ◽  
Ph Profile ◽  
Heat Stable ◽  
Low Levels ◽  
Concentrated Milk ◽  
Milk Solids ◽  
Ph Curve

SummaryChanges in heat stability and Ca2+ activity of recombined concentrated milk (18% solids non-fat:8% fat) induced by the additions of 0·011–0·217 mol phosphate/kg skim milk solids (SMS), 0·022–0·217 mol citrate/kg SMS, 0·011–0·022 mol Ca/kg SMS and 0·016–0·067 mol EDTA/kg SMS were evaluated. Heat stability was assessed using an objective method which involved determination of viscosity after heating under controlled conditions. Low levels of added phosphate and citrate generally effected an acid shift of the viscosity–pH profile, while higher levels caused a broadening of the profile. Addition of CaCl2 at a level of 0·011 mol/kg SMS resulted in a narrowing of the viscosity–pH curve; additions of higher levels resulted in a non-heat stable recombined milk concentrate. EDTA also caused a narrowing of the viscosity–pH curve. The results highlight the importance of pH control for effective stabilization of recombined milk concentrates by additions of phosphate and citrate.

Effects of phenolic compounds on the heat stability of milk and concentrated milk

1999 ◽  
Vol 66 (3) ◽  
pp. 399-407 ◽  
Author(s):  
JOHN E. O'CONNELL ◽  
PATRICK F. FOX
Keyword(s):  
Phenolic Compounds ◽  
Green Tea ◽  
Skim Milk ◽  
Epigallocatechin Gallate ◽  
Quinic Acid ◽  
Heat Stability ◽  
Green Tea Polyphenols ◽  
Epicatechin Gallate ◽  
Ph Profile ◽  
Concentrated Milk

A methanol extract of green tea was fractionated on Sephadex LH-20. The compounds eluted were identified by thin layer chromatography as catechin–epicatechin, gallocatechin, epigallocatechin, epicatechin gallate and epigallocatechin gallate. When added to milk at 2·0 g/l, these polyphenols, apart from the catechin–epicatechin mixture, increased the heat stability of skim milk, particularly in the region of the minimum (pH 6·8–7·1). When added at 0·4 g/l, green tea polyphenols also increased the heat stability of concentrated milk. The effects of other phenolic compounds on the heat stability of milk were also examined. Chlorogenic acid, guaiacol, thymol, vanillin, butylene hydroxyanisole, propyl gallate and butylene hydroxytoluene did not affect the heat stability of milk or concentrated milk. Quinic acid markedly reduced the heat stability of skim milk. Pyrogallol, catechol, tannic acid, ellagic acid, phloroglucinol and gallate converted a type A heat coagulation time–pH profile to a type B profile. Ferulic acid and vanillic acid increased heat stability in the region of the maximum, with little effect on the minimum, and stability did not recover at pH values on the alkaline side of the minimum. Caffeic acid increased the heat stability of milk while the related non-phenolic compounds 2,5-dimethoxycinnamic acid and 3,4-dimethoxycinnamic acid had no effect.

Heat stability of milk: pH-dependent dissociation of micellar κ-casein on heating milk at ultra high temperatures

1985 ◽  
Vol 52 (4) ◽  
pp. 529-538 ◽  
Author(s):  
Harjinder Singh ◽  
Partick F. Fox
Keyword(s):  
Whey Protein ◽  
Whey Proteins ◽  
Heat Stability ◽  
Casein Micelle ◽  
Casein Micelles ◽  
Ph Profile ◽  
Ph Values ◽  
Maximum Stability ◽  
Β Lactoglobulin ◽  
Maximum Minimum

SUMMARYPreheating milk at 140 °C for 1 min at pH 6·6, 6·8, 7·0 or 7·2 shifted the heat coagulation time (HCT)/pH profile to acidic values without significantly affecting the maximum stability. Whey proteins (both β-lactoglobulin and α-lactalbumin) co-sedimented with the casein micelles after heating milk at pH < 6·9 and the whey protein-coated micelles, dispersed in milk ultrafiltrate, showed characteristic maxima–minima in their HCT/pH profile. Heating milk at higher pH values (> 6·9) resulted in the dissociation of whey proteins and κ-casein-rich protein from the micelles and the residual micelles were unstable, without a maximum–minimum in the HCT/pH profile. Preformed whey protein–casein micelle complexes formed by preheating (140 °C for 1 min) milk at pH 6·7 dissociated from the micelles on reheating (140 °C for 1 min) at pH > 6·9. The dissociation of micellar-κ-casein, perhaps complexed with whey proteins, may reduce the micellar zeta potential at pH ≃ 6·9 sufficiently to cause a minimum in the HCT/pH profile of milk.

Heat stability of milk

1980 ◽  
Vol 47 (2) ◽  
pp. 199-210 ◽  
Author(s):  
Donald F. Darling
Keyword(s):  
Temperature Dependence ◽  
Elevated Temperatures ◽  
Skim Milk ◽  
Heat Stability ◽  
Coagulation Time ◽  
Ph Values ◽  
Protein Polymerization ◽  
Casein Protein ◽  
Apparent Activation Energies ◽  
Β Lactoglobulin

SummaryThe heat stability of a standard reconstituted skim-milk preparation has been investigated as a function of pH, temperature of coagulation, and forewarming treatment. Apparent activation energies have been calculated from the temperature dependence of coagulation time, and a constant value of 144 kJ/mole has been found for milks between pH 6·6 and 6·9. The effect of forewarming resulted in a decrease in stability at the most acid pH values, a slight increase at higher pH but below the pH maximum, and a decrease in the region of the pH minimum. A working hypothesis is proposed for the mechanisms leading to the coagulation of milk at elevated temperatures, based upon Ca induced precipitation of casein, protein polymerization, β-lactoglobulin: κ-casein interaction, and precipitation of insoluble Ca phosphates.

Heat stability of milk: further studies on the pH-dependent dissociation of micellar κ-casein

1986 ◽  
Vol 53 (2) ◽  
pp. 237-248 ◽  
Author(s):  
Harjinder Singh ◽  
Patrick F. Fox
Keyword(s):  
Whey Protein ◽  
Cetyltrimethylammonium Bromide ◽  
Opposite Effect ◽  
Whey Proteins ◽  
Sodium Dodecyl ◽  
Skim Milk ◽  
Heat Stability ◽  
Casein Micelles ◽  
Acetylneuraminic Acid ◽  
Ph Dependent

SUMMARYWhey protein complexed and became co-sedimentable with casein micelles after heating milk at ≥ 90°C for 10 min at pH ≤ 6·9 while at higher pH values (7·3) whey proteins and κ-casein-rich protein dissociated from the micelles on heating. κ-Casein-deficient micelles were more sensitive to heat, Ca2+ or ethanol than whey protein-coated or native micelles and were readily coagulable by rennet. Isolated κ-casein added to skim milk before preheating (90°C for 10 min) did not associate with the micelles at pH ≥ 6·9. Sodium dodecyl sulphate increased the level of both non-sedimentable N (NSN) and N-acetylneuraminic acid (NANA) and shifted the NSN-pH and NANA-pH curves to more acidic values while cetyltrimethylammonium bromide had the opposite effect. It is suggested that the pH-dependent dissociation in micellar κ-casein, which appears to be reversible, depends on the surface charge on the micelles; at a certain negative charge, disruption of hydrophobic and electrostatic forces could result in the dissociation of κ-casein from the casein micelles.

Whey protein denaturation in heated milk and cheese whey

1979 ◽  
Vol 46 (1) ◽  
pp. 95-102 ◽  
Author(s):  
Robyn M. Hillier ◽  
Richard L. J. Lyster
Keyword(s):  
Cheese Whey ◽  
Protein Denaturation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Whey Proteins ◽  
Skim Milk ◽  
Heat Stability ◽  
Second Order ◽  
First Order ◽  
Heated Milk ◽  
Native Whey

SUMMARYQuantitative polyacrylamide gel electrophoresis has been used to measure residual native whey proteins remaining after heat treatment of skim-milk and cheese whey in a kinetic study. The denaturation of α-lactalbumin (α-la) appeared to be first order, but was probably a second-order reaction displaying pseudo first-order kinetics. The denaturation of both β-lactoglobulin A and B (β-lgA and β-lgB) followed second-order kinetics while that of serum albumin was more complex, and could equally well be described as first or second order. Equations are given relating logk1(in s-1) to temperature for α-la denaturation in skim-milk between 70 and 95 °C and between 100 and 150 °C. Similarly, equations relating logk2(in lg-1s-1) to temperature are given for ²-lgA in skim-milk between 100 and 150 °C, and for ²-lgB between 95 and 150 °C. The relative heat stability of ²-lgA and ²-lgB was found to vary.Below 95 °C ²-lgA appeared slightly more thermostable than ²-lgB in skim-milk, and the same was observed in cheese whey below 100 °C. Above these temperatures ²-lgB appeared more stable than ²-lgA.Denaturation of ²-lgB was only slightly more rapid in skim-milk than in whey at temperatures below 95 °C, but was significantly slower at higher temperatures.

Heat stability of recombined milk: influence of lecithins on the heat coagulation time-pH profile

1992 ◽  
Vol 59 (2) ◽  
pp. 177-185 ◽  
Author(s):  
Catharina H. McCrae ◽  
D. Donald Muir
Keyword(s):  
Milk Powder ◽  
Skim Milk ◽  
Heat Stability ◽  
Skim Milk Powder ◽  
Coagulation Time ◽  
Ph Profile ◽  
Mineral Equilibria ◽  
Soya Lecithin ◽  
Before And After ◽  
Wide Ph Range

SummaryTwo types of lecithin, namely egg and soya lecithin, were investigated as potential stabilizers of recombined milk. They were incorporated into recombined milk both before and after homogenization (20·7 MPa; 60 °C). Their presence at homogenization changed neither mineral equilibria nor homogenization efficiency. However, heat stability varied significantly irrespective of batch of low-heat skim milk powder used in recombined milk. The variation in heat stability depended on type of lecithin. Soya lecithin proved to be a very effective stabilizer. It improved heat stability over a wide pH range (6·3–7·1) and the effect occurred even when the lecithin was added after homogenization. In contrast, egg lecithin destabilized the system to heat at pH < 6·7 by converting a Type A into a Type B heat coagulation time-pH profile if it was incorporated before homogenization; after homogenization it had no effect. The effects of both egg and soya lecithin on the heat stability of recombined milk strongly suggest that interactions occur between phospholipids and milk protein.

Factors affecting the action of rennin in heated milk

1972 ◽  
Vol 39 (3) ◽  
pp. 413-419 ◽  
Author(s):  
G. A. Wilson ◽  
J. V. Wheelock
Keyword(s):  
Complex Formation ◽  
Heat Stability ◽  
Primary Phase ◽  
Effect Of Temperature ◽  
Heat Denaturation ◽  
Clotting Time ◽  
Factors Affecting ◽  
Heated Milk ◽  
Whole Milk ◽  
Β Lactoglobulin

SummaryThe effect of temperature and time of heating whole milk on the renninclotting time, the primary phase of rennin action and the protein (mainly β-lactoglobulin) soluble in 2% trichloroacetic acid (TCA), have been studied. Considerable changes in these parameters occurred above 60°C. The primary phase was inhibited (the degree of inhibition being both temperature and time-dependent), the clotting time was increased, and the protein soluble in 2% TCA decreased considerably.It is suggested that the inhibition of the primary phase was due to complex formation between κ-casein and β-lactoglobulin, the increase in clotting time to a combination of complex formation and a change in the distribution of Ca, and the decrease in β-lactoglobulin to both its interaction with κ-casein and its heat denaturation. The relevance of such changes to the heat stability of milk is discussed.

The Role of β-lactoglobulin in the primary phase of rennin action on heated casein micelles and heated milk

1974 ◽  
Vol 41 (3) ◽  
pp. 367-372 ◽  
Author(s):  
J. V. Wheelock ◽  
A. Kirk
Keyword(s):  
Heat Treatment ◽  
Complex Formation ◽  
Skim Milk ◽  
Primary Phase ◽  
Casein Micelles ◽  
Heated Milk ◽  
Β Lactoglobulin

SummaryIt has been shown that the inhibition caused by heat treatment, of the primary phase of rennin action on casein micelles, is dependent on the presence of β-lactoglobulin. The degree of inhibition increased with increasing amounts of added β-lactoglobulin for both heated casein micelles and heated skim-milk to a constant value. The results are fully consistent with the hypothesis that the inhibition is caused by complex formation between β-lactoglobulin and κ-casein when milk is heated.

Influence of sulphydryl group interactions on the heat stability of homogenized concentrated milk

1983 ◽  
Vol 50 (3) ◽  
pp. 301-308 ◽  
Author(s):  
A. W. Maurice Sweetsur ◽  
D. Donald Muir
Keyword(s):  
Complex Formation ◽  
Heat Stability ◽  
Group Interactions ◽  
Sulphydryl Group ◽  
Oxidizing Agents ◽  
Concentrated Milk ◽  
Β Lactoglobulin

SUMMABYThe heat stability of homogenized concentrated milk was found to be more susceptible than that of unhomogenized concentrated milk to changes in the ratio of β-lactoglobulin to κ-casein which were deliberately designed to alter the extent of disulphide-linked complex formation during heating. When sulphydryl group interactions were prevented by the addition to the milk before homogenization of blocking or oxidizing agents, homogenization did not change the heat stability of subsequently concentrated milk.

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