Seasonal variation in the composition and processing characteristics of herd milk with varying proportions of milk from spring-calving and autumn-calving cows

2017 ◽  
Vol 84 (4) ◽  
pp. 444-452 ◽  
Author(s):  
Yingchen Lin ◽  
James A. O'Mahony ◽  
Alan L. Kelly ◽  
Timothy P. Guinee
Keyword(s):  
Milk Powder ◽  
Heat Stability ◽  
Casein Micelle ◽  
Total Calcium ◽  
Volume Proportion ◽  
Micelle Size ◽  
Total Milk ◽  
Herd Milk ◽  
Ethanol Stability ◽  
Total P

The study investigated the seasonal changes in the compositional, physicochemical and processing characteristics of milk from a mixed-herd of spring- and autumn-calving cows during the year 2014–2015. The volume proportion of autumn-calving milk (% of total milk) varied with season, from ~10–20 in Spring (March–May), 5–13 in Summer (June–August), 20–40 in Autumn (September–November) and 50–100 in Winter (December–February). While all characteristics varied somewhat from month to month, variation was inconsistent, showing no significant trend with progression of time (year). Consequently, season did not significantly affect many parameters including concentrations of total protein, casein, whey protein, NPN, total calcium, pH, rennet gelation properties or heat stability characteristics. However, season had a significant effect on the concentrations of total P and serum P, levels of αs1- and β-caseins as proportions of total casein, casein micelle size, zeta potential and ethanol stability. The absence of a significant effect of season for most compositional parameters, rennet gelation and heat-stability characteristics suggest that milk from a mixed-herd of spring- and autumn-calving cows is suitable for the manufacture of cheese and milk powder on a year-round basis, when the volume proportion of autumn milk, as a % of total, is similar to that of the current study.

Denaturation, aggregation and heat stability of milk protein during the manufacture of skim milk powder

1991 ◽  
Vol 58 (3) ◽  
pp. 269-283 ◽  
Author(s):  
Harjinder Singh ◽  
Lawrence K. Creamer
Keyword(s):  
Spray Drying ◽  
Milk Powder ◽  
Skim Milk ◽  
Heat Stability ◽  
Skim Milk Powder ◽  
Casein Micelle ◽  
Commercial Plant ◽  
Preheat Treatment ◽  
Solids Content ◽  
Time Required

SummaryThe effect of preheat treatment, evaporation and drying in a commercial plant on the denaturation of βlactoglobulin and α-lactalbumin, their incorporation into the casein micelle and the heat stability characteristics of the milks and powders were determined. Preheat treatments between 110 °C for 2 min and 120 °C for 3 min denatured between 80 and 91% of β-lactoglobulin and between 33 and 45% of α-lactalbumin. Evaporation increased the extent of denaturation but spray drying did not increase it further. The incorporation of α-lactalbumin and βlactoglobulin into the micelles was markedly less than the amount that denatured and was not a constant ratio to it. Heat coagulation times at 140 °C of milks, concentrates and powders diluted to the original milk concentration were measured as a function of pH. In general, the greater the collective heat treatment, the shorter the time required to achieve coagulation. Spray drying shifted the peak positions in the pH-heat coagulation time profiles. In contrast, heat coagulation times (measured at 120 °C) of concentrates and powders diluted to 20% total solids content increased with the severity of the preheat treatment. Surprisingly, spray drying markedly increased the heat coagulation times of the diluted concentrates.

Physico-chemical properties of casein micelles reformed from urea-treated milk

1974 ◽  
Vol 41 (1) ◽  
pp. 45-53 ◽  
Author(s):  
T. C. A. McGann ◽  
P. F. Fox
Keyword(s):  
Binding Capacity ◽  
Chemical Properties ◽  
Heat Stability ◽  
Casein Micelles ◽  
Second Stage ◽  
Bulk Milk ◽  
Rennet Coagulation ◽  
Physico Chemical ◽  
Micelle Size ◽  
Ethanol Stability

SummaryMicelles reconstituted from urea-treated milk by exhaustive dialysis against bulk milk were similar to native micelles with respect to colloidal phosphate: casein ratio, ethanol stability, heat stability and susceptibility to first-stage rennin action. Reconstituted micelles were considerably smaller than native micelles as indicated by turbidity, sedimentation and viscosity, had shorter second-stage rennet coagulation times, were unstable to [Ca2+] > 20 mM and had reduced base-binding capacity. It is suggested that the induced Ca sensitivity is due to unfavourable alterations in the micellar κ-casein coat arising from the decrease in average micelle size and can be offset by increasing the κ-casein complement of the system or by increasing the degree of aggregation by slowly raising the [Ca2+] level.

Improved heat stability of recombined evaporated milk emulsions by wet heat pretreatment of skim milk powder dispersions

2021 ◽  
pp. 106757
Author(s):  
Jianfeng Wu ◽  
Simin Chen ◽  
Teng Wang ◽  
Hao Li ◽  
Ali Sedaghat Doost ◽  
...  
Keyword(s):  
Milk Powder ◽  
Skim Milk ◽  
Heat Stability ◽  
Skim Milk Powder ◽  
Heat Pretreatment ◽  
Wet Heat

Contribution of casein micelle size and proteolysis on protein distribution and sediment formation in UHT milk during storage

2021 ◽  
Vol 117 ◽  
pp. 104980
Author(s):  
Marije Akkerman ◽  
Lene Buhelt Johansen ◽  
Valentin Rauh ◽  
Nina Aagaard Poulsen ◽  
Lotte Bach Larsen
Keyword(s):  
Casein Micelle ◽  
Protein Distribution ◽  
Uht Milk ◽  
Micelle Size ◽  
Sediment Formation

Hydrophobic interactions in human casein micelle formation: β-casein aggregation

1989 ◽  
Vol 56 (3) ◽  
pp. 427-433 ◽  
Author(s):  
Charles W. Slattery ◽  
Satish M. Sood ◽  
Pat Chang
Keyword(s):  
Light Scattering ◽  
Conformational Transition ◽  
Hydrophobic Interactions ◽  
Micelle Formation ◽  
Tryptophan Fluorescence ◽  
Phosphate Esters ◽  
Casein Micelle ◽  
Protein Association ◽  
P Protein ◽  
Micelle Size

SummaryThe association of non-phosphorylated (0-P) and fully phosphorylated (5-P) human β-caseins was studied by fluorescence spectroscopy and laser light scattering. The tryptophan fluorescence intensity (FI) level increased between 20 and 35 °C, indicating a change in the environment of that residue. A similar transition occurred when ANS was used as a probe. Transition temperatures were slightly lower in 10 mM-CaCl2 but were not affected by an equivalent increase in ionic strength caused by NaCl. The magnitude of the FI change was less for the 5-P than the 0-P protein but was increased for both by CaCl2 addition. These FI data were characteristic of a conformational change and this was supported by fluorescence polarization which indicated that with CaCl2, tryptophan and ANS mobility increased at the transition temperature even though the extent of protein association also increased. Light scattering suggested that protein association proeeeded with the primary formation of submicellar aggregates containing 20–30 monomers which then associated further to form particles of minimum micelle size (12–15 submicelles), and eventually larger. The temperature of precipitation of the 5-P form in the presence of CaCl2 was lower than the conformational transition and suggested that both hydrophobic interactions and Ca bridges between phosphate esters on adjacent molecules are important in micelle formation.

scholarly journals Association of casein micelle size and enzymatic curd strength and dry matter curd yield

2019 ◽  
Vol 49 (3) ◽  
Author(s):  
Denise Ribeiro de Freitas ◽  
Fernando Nogueira de Souza ◽  
Jamil Silvano de Oliveira ◽  
Diêgo dos Santos Ferreira ◽  
Cristiane Viana Guimarães Ladeira ◽  
...  
Keyword(s):  
Fixed Effects ◽  
Dry Matter ◽  
Linear Models ◽  
Favorable Effect ◽  
Casein Micelle ◽  
Casein Micelles ◽  
Micelle Size ◽  
Milk Protein Content ◽  
Bulk Tank ◽  
Cheese Production

ABSTRACT: The aim of the present study was to explore the association between milk protein content and casein micelle size and to examine the effects of casein micelle size on enzymatic curd strength and dry matter curd yield using reduced laboratory-scale cheese production. In this research, 140 bulk tank milk samples were collected at dairy farms. The traits were analyzed using two linear models, including only fixed effects. Smaller micelles were associated with higher κ-casein and lower αs-casein contents. The casein micellar size (in the absence of the αs-casein and κ-casein effects) did not affect the enzymatic curd strength; however, smaller casein micelles combined with higher fat, lactose, casein and κ-casein contents exhibited a favorable effect on the dry matter curd yield. Overall, results of the present study provide new insights into the importance of casein micelle size for optimizing cheese production.

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.

Effect of the A and B variants of both αs1- and κ-casein on bovine casein micelle solvation and κ-casein content

1993 ◽  
Vol 60 (4) ◽  
pp. 505-516 ◽  
Author(s):  
Skelte G. Anema ◽  
Lawrence K. Creamer
Keyword(s):  
Genetic Variants ◽  
The Other ◽  
Casein Micelle ◽  
Lactation Period ◽  
Chromosomal Dna ◽  
Electrophoretic Method ◽  
Milk Samples ◽  
Micelle Size ◽  
Centrifugation Technique ◽  
Β Lactoglobulin

SummaryCasein micelle solvation, a micelle characteristic that is sensitive to many factors, has been measured by a centrifugation technique at 30 °C for a series of uncooled fresh skim milks at pH 6·3, 6·6, 6·9 and 7·1. The relative αs-(αs1- plus αs2-), β– and κ-casein contents of all centrifuge pellets and supernatants were determined by a standardized electrophoretic method. The calcium and phosphate contents of a number of the pellets and milk samples were also determined. Solvation of micelles from milks with various genetic variants of β-lactoglobulin (A and B), αs1-casein (A and B) and κ-casein (A and B) was often found to be lower for milks containing either the B variant of αs1-casein or the A variant of κ-casein. It was also found that these two variant caseins were associated with a lower κ-casein content of the milks and the micelles, which is consistent with the lower solvation as κ-casein is associated with smaller micelle size and greater solvation. The solvations also seemed to increase during the lactation period. It is possible that some of the other features of milk and its products that have been ascribed to the differences in functional character between the A and B variants of αs1-casein may be partly caused by the increased level of κ-casein. The reason for the association of the A variant of αs1-casein with higher concentrations of κ-casein (and micelle solvation) is not obvious but possibly the haplotype αs1-casein A, β-casein A1, κ-casein A contains a controlling sequence in the chromosomal DNA that enhances expression of the κ-casein gene.

scholarly journals Role of protein aggregation in heat-induced heat stability during milk powder manufacture

2008 ◽  
Vol 88 (1) ◽  
pp. 121-147 ◽  
Author(s):  
Roderick P.W. Williams ◽  
Lynette D'Ath ◽  
Bogdan Zisu
Keyword(s):  
Protein Aggregation ◽  
Milk Powder ◽  
Heat Stability ◽  
Powder Manufacture

Influence of homogenization of concentrated milks on the structure and properties of rennet curds

1983 ◽  
Vol 50 (3) ◽  
pp. 341-348 ◽  
Author(s):  
Margaret L. Green ◽  
Richard J. Marshall ◽  
Frank A. Glover
Keyword(s):  
Fatty Acid ◽  
Free Fatty Acid ◽  
Size Distribution ◽  
Casein Micelle ◽  
Structure And Properties ◽  
Moisture Retention ◽  
Casein Micelles ◽  
Micelle Size ◽  
Whole Milk ◽  
Milk Casein

SummaryWhole milk was concentrated by ultrafiltration in a plant causing some homogenization of the fat. Comparisons were made with milk concentrated in a plant causing little homogenization and with milk homogenized conventionally. None of the processes appreciably affected the casein micelle size distribution. On rennet treatment of homogenized milk, casein micelle aggregation occurred more slowly, the protein network in the curd was less coarse and the rate of whey loss was reduced, compared with non-homogenized milk at the same concentration. In using concentrated milks for cheesemaking homogenization improved the composition of Cheddar cheese, because of increased fat and moisture retention, but curd fusion was poorer. Some aspects of the texture of the mature cheeses were improved, but the free fatty acid levels were higher. Values for the firmness of curds, formed from milks processed in different ways, did not relate to the extent of aggregation of the casein micelles. It is suggested that the complete cheesemaking process is driven by the tendency of the casein to aggregate.

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