Heat stability of milk: interrelationship between assay temperature, pH and agitation

1981 ◽  
Vol 48 (1) ◽  
pp. 123-129 ◽  
Author(s):  
Douglas B. Hyslop ◽  
Patrick F. Fox
Keyword(s):  
Heat Stability ◽  
Kcal Mole ◽  
Temperature Dependent ◽  
Total Solids ◽  
Ph Values ◽  
Assay Procedure ◽  
Concentrated Milk ◽  
The Stability ◽  
Ph Curve ◽  
Maximum Minimum

SummaryAs determined by the standard subjective assay procedure, the minimum in the heat stability–pH curve of milk persisted down to at least 116 °C. However when samples were not agitated during heating the minimum became progressively less pronounced as the assay temperature was lowered and it disappeared at approximately 116 °C. Activation energies (Ea) for unagitated samples were approximately 30 Kcal/mole at pH 6·87 (maximum) and at pH 7·18, throughout the temperature range 116–145 °C and for the pH 6·95 (minimum) sample at 116–125 °C; however Eα for the pH 6.95 sample increased to approximately 100 Kcal/mole in the range 127–135 °C suggesting that some highly temperature-dependent reaction had occurred and caused premature coagulation at certain pH values, i.e. to a heat stability minimum. The stability of concentrated milk (20% total solids) was very low at pH values above 6·9, regardless of whether the samples were agitated or not during heating and the maximum/minimum in the heat stability–pH curve persisted down to at least 90 °C in both agitated and quiescent samples.

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: influence of colloidal calcium phosphate and β-lactoglobulin

1975 ◽  
Vol 42 (3) ◽  
pp. 427-435 ◽  
Author(s):  
P. F. Fox ◽  
M. C. T. Hoynes
Keyword(s):  
Calcium Phosphate ◽  
Fold Increase ◽  
Heat Stability ◽  
Protein Charge ◽  
Ph Values ◽  
Colloidal Calcium Phosphate ◽  
Maximum Stability ◽  
Ph Range ◽  
Ph Curve ◽  
Β Lactoglobulin

SummaryReduction of the level of colloidal calcium phosphate (CCP) progressively increased the heat stability of milk at pH values <~7·0 and increased the pH of maximum stability. Removal of 40% CCP also stabilized the system at the pH of minimum stability, but removal of ≥60% CCP rendered milk very unstable at pH values >7·2, an effect not offset by a 4-fold increase in κ-casein concentration. Doubling CCP had a slight destabilizing effect in the pH range 6·5–7·5.Addition of β-lactoglobulin to serum protein-free casein micelles had a marked destabilizing effect at pH values > ~6·8, but increased stability in the pH range 6·4–6·8. β-Lactoglobulin had a similar and more apparent effect on the heat stability of Na caseinate dissolved in milk diffusate.It is suggested that rather than being a stabilizing factor responsible for the maximum in the heat stability-pH curve, the true effect of β-lactoglobulin is to shift the curve to more acid pH values (reason unknown) and to sensitize the caseinate system to heat-induced Ca phosphate precipitation at pH values > ~7·0. Low stability at ~pH 7·0 introduces an apparent maximum in the heat stability-pH curve at ~pH 6·8, but this has no independent existence. At pH values >7·2, increased protein charge more than off-sets the influence of heat-precipitated CCP and stability again increases in micellar but not in soluble casein systems.

Heat stability of milk: the mechanism of stabilization by formaldehyde

1985 ◽  
Vol 52 (1) ◽  
pp. 65-76 ◽  
Author(s):  
Harjinder Singh ◽  
Patrick F. Fox
Keyword(s):  
High Temperatures ◽  
Crosslinking Agent ◽  
Heat Stability ◽  
Cross Linking ◽  
Amino Groups ◽  
Coagulation Time ◽  
Ph Profile ◽  
Ph Values ◽  
Dimethyl Suberimidate ◽  
Ph Curve

SUMMARYThe increase produced by formaldehyde (HCHO) in the heat stability of milk did not occur when milk was treated with HCHO at temperatures up to 60°C followed by dialysis at 5°C. However, the minimum in the heat coagulation time (HCT)–pH curve was irreversibly removed if the milk was preheated at 80–C for 10 min in the presence of 5 mM-HCHO. Although this treatment blocked the ε-amino groups of lysyl residues, the stabilizing mechanism is considered to be due to the cross linking action of HCHO which reduced the level of non-sedimentable, κ-casein-rich protein dissociated from the micelles on heating. The specific crosslinking agent, dimethyl suberimidate, modified the HCT-pH profile of milk in a manner similar to preheating at 80°C for 10 min with 5 mM-HCHO, supporting the crosslinking hypothesis. The results of this study appear to lend some support to the proposal of Kudo (1980) that the minimum in the HCT-pH curve of milk is due to the dissociation of κ-casein from the micelles on heating at high temperatures at pH values greater than 6η7.

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.

scholarly journals Evaluation of physico-chemical characteristics of fresh, refrigerated and frozen Lacaune ewes' milk

2014 ◽  
Vol 66 (6) ◽  
pp. 1924-1930 ◽  
Author(s):  
L.W. Fava ◽  
I.C. Külkamp-Guerreiro ◽  
A.T. Pinto
Keyword(s):  
Chemical Composition ◽  
Titratable Acidity ◽  
Heat Stability ◽  
Chemical Characteristics ◽  
Total Solids ◽  
Average Percentage ◽  
Sheep Milk ◽  
Consequent Reduction ◽  
The Stability ◽  
Physical And Chemical

The production of ewe milk is seasonal and milk yield per animal is low, even in specialized animals. This study aimed to verify the possibility of preserving bulk tank milk for seven days under cooling (5°C) and freezing (-5°C), verify the influence of cooling treatments and of the months of the year on the physical and chemical characteristics of the product. The chemical composition of milk, including the fat, protein, lactose and total solids contents, was not altered by cooling and freezing. Protein and lactose contents varied according to the months of the year. The average percentage and standard deviation of fat, protein, lactose and total solids was 8.10±1.30, 5.22±0.37, 4.43±0.23 and 19.34±1.54, respectively. The density, pH, titratable acidity, as well as alcohol and heat stability tests were significantly influenced by the treatments used (P < 0.05), but no differences were found between fresh and frozen milk. Prolonged refrigeration caused an increase in acidity and decrease in pH, with a consequent reduction in the stability of milk. These results demonstrated that freezing does not affect the chemical composition and physical characteristics of milk in nature and it could be a solution for the producer and the sheep milk industry.

Heat stability characteristics of ovine, caprine and equine milks

1976 ◽  
Vol 43 (3) ◽  
pp. 433-442 ◽  
Author(s):  
P. F. Fox ◽  
M. C. T. Hoynes
Keyword(s):  
Heat Stability ◽  
Soluble Salts ◽  
Low Level ◽  
Ph Values ◽  
Colloidal Calcium Phosphate ◽  
Maximum Stability ◽  
Equine Milk ◽  
Ph Curve ◽  
Β Lactoglobulin ◽  
Marked Stability

SummaryOvine and caprine milks showed a marked stability maximum at ~ pH7 in their heat-stability/pH curves, but became very unstable at higher pH values. A low level of κ-casein appears to be responsible for this low stability of ovine milk; β-lactoglobulin offsets the stabilizing influence of κ-casein at lower pH values. Removal of colloidal calcium phosphate from ovine or caprine milks had very little influence on their heat stabilities and it was necessary to reduce the concentration of soluble salts to a very low level before an effect was observed. At the pH of maximum stability ovine and caprine milks, although quite variable, had stabilities in the same range as bovine milks. Equine milk was very unstable to heat and the shape of the heat-stability/pH curve of most individual samples was similar to ovine and caprine milks.

Heat stability of recombined concentrated milk: changes in calcium activity and pH on sterilization

1991 ◽  
Vol 58 (1) ◽  
pp. 67-74 ◽  
Author(s):  
Mary-Ann Augustin ◽  
Phillip T. Clarke
Keyword(s):  
Heat Stability ◽  
High Heat ◽  
Calcium Activity ◽  
Ph Values ◽  
Preheat Treatment ◽  
Powder Manufacture ◽  
Concentrated Milk ◽  
C 30

SummaryRecombined concentrated milks (18% SNF, 8% fat) at their natural pH and at pH values in the range 6·28–6·68, made with powders subjected to different preheat conditions (high heat (85°C, 30 min), indirect UHT (120°C, 2 min) and direct UHT (120°C, 2 min)), were sterilized at 120°C for 13 min. The heat stabilities of recombined concentrated milks were dependent on preheat treatment. Ca2+ activity and pH of sterilized recombined concentrated milks, measured l h after sterilization, were lower than those of corresponding unsterilized recombined concentrated milks. The magnitude of the decreases in Ca2+ activity and pH induced on sterilization were dependent on the pH of the unsterilized recombined concentrated milk but were not markedly influenced by the type of preheat treatment applied during powder manufacture. The results suggest that differences in heat stability of high heat, indirect UHT and direct UHT powders are unlikely to be due to Ca2+ activity.

scholarly journals Measurement of the Intestinal pH in Mice under Various Conditions Reveals Alkalization Induced by Antibiotics

Antibiotics ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 180
Author(s):  
Kouki Shimizu ◽  
Issei Seiki ◽  
Yoshiyuki Goto ◽  
Takeshi Murata
Keyword(s):  
Antibiotic Treatment ◽  
High Protein Diet ◽  
Intestinal Bacteria ◽  
High Protein ◽  
Protein Diet ◽  
Germ Free ◽  
Treatment Regimens ◽  
Ph Values ◽  
Specific Pathogen ◽  
The Stability

The intestinal pH can greatly influence the stability and absorption of oral drugs. Therefore, knowledge of intestinal pH is necessary to understand the conditions for drug delivery. This has previously been measured in humans and rats. However, information on intestinal pH in mice is insufficient despite these animals being used often in preclinical testing. In this study, 72 female ICR mice housed in SPF (specific pathogen-free) conditions were separated into nine groups to determine the intestinal pH under conditions that might cause pH fluctuations, including high-protein diet, ageing, proton pump inhibitor (PPI) treatment, several antibiotic treatment regimens and germ-free mice. pH was measured in samples collected from the ileum, cecum and colon, and compared to control animals. An electrode, 3 mm in diameter, enabled accurate pH measurements with a small amount of gastrointestinal content. Consequently, the pH values in the cecum and colon were increased by high-protein diet, and the pH in the ileum was decreased by PPI. Drastic alkalization was induced by antibiotics, especially in the cecum and colon. The alkalized pH values in germ-free mice suggested that the reduction in the intestinal bacteria caused by antibiotics led to alkalization. Alkalization of the intestinal pH caused by antibiotic treatment was verified in mice. We need further investigations in clinical settings to check whether the same phenomena occur in patients.

Effect of concentration by ultrafiltration on the heat stability of skim-milk

1980 ◽  
Vol 47 (3) ◽  
pp. 327-335 ◽  
Author(s):  
A. W. Maurice Sweetsur ◽  
D. Donald Muir
Keyword(s):  
Skim Milk ◽  
Heat Stability ◽  
High Protein ◽  
Milk Products ◽  
Total Solids

SUMMARYAn examination has been made of the heat stability characteristics of skim-milk concentrate prepared by ultrafiltration (UF). Concentrate prepared by UF was found to be more stable than that prepared by conventional evaporation. In contrast to conventional concentrate, the heat stability of UF concentrate was not appreciably affected by forewarming or addition of permitted stabilizers, but the effect of addition of urea was generally the same for both UF and conventional concentrates; an increase in heat stability was obtained if the milk total solids level was less than 14%. As with conventional concentrate, addition of simple aldehydes induced large increases in the heat stability of UF concentrate. It is suggested that a novel range of sterile milk products could be prepared from UF concentrates. Because of the high protein and low lactose contents of these concentrates, the products might be nutritionally more attractive than those prepared from conventional concentrates.

scholarly journals DNA Genome Size Affects the Stability of the Adenovirus Virion

2008 ◽  
Vol 83 (4) ◽  
pp. 2025-2028 ◽  
Author(s):  
Adam C. Smith ◽  
Kathy L. Poulin ◽  
Robin J. Parks
Keyword(s):  
Genome Size ◽  
Critical Role ◽  
Heat Stability ◽  
Helper Virus ◽  
Heat Inactivation ◽  
Similar Relationship ◽  
Viral Dna ◽  
A Genome ◽  
The Stability ◽  
Replication Defective Adenovirus

ABSTRACT Replication-defective adenovirus (Ad) vectors can vary considerably in genome length, but whether this affects virion stability has not been investigated. Helper-dependent Ad vectors with a genome size of ∼30 kb were 100-fold more sensitive to heat inactivation than their parental helper virus (>36 kb), and increasing the genome size of the vector significantly improved heat stability. A similar relationship between genome size and stability existed for Ad with early region 1 deleted. Loss of infectivity was due to release of vertex proteins, followed by disintegration of the capsid. Thus, not only does the viral DNA encode all of the heritable information essential for virus replication, it also plays a critical role in maintaining capsid strength and integrity.

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