Interactive effects of casein micelle size and calcium and citrate content on rennet‐induced coagulation in bovine milk

2019 ◽  
Vol 50 (6) ◽  
pp. 508-519 ◽  
Author(s):  
Hasitha Priyashantha ◽  
Åse Lundh ◽  
Annika Höjer ◽  
Mårten Hetta ◽  
Monika Johansson ◽  
...  
Keyword(s):  
Bovine Milk ◽  
Interactive Effects ◽  
Casein Micelle ◽  
Micelle Size

High pressure treatment of bovine milk: effects on casein micelles and whey proteins

2004 ◽  
Vol 71 (1) ◽  
pp. 97-106 ◽  
Author(s):  
Thom Huppertz ◽  
Patrick F Fox ◽  
Alan L Kelly
Keyword(s):  
High Pressure ◽  
Treatment Time ◽  
Whey Proteins ◽  
Bovine Milk ◽  
Casein Micelle ◽  
Pressure Treatment ◽  
Casein Micelles ◽  
High Pressure Treatment ◽  
Micelle Size ◽  
Β Lactoglobulin

Effects of high pressure (HP) on average casein micelle size and denaturation of α-lactalbumin (α-la) and β-lactoglobulin (β-lg) in raw skim bovine milk were studied over a range of conditions. Micelle size was not influenced by treatment at pressures <200 MPa, but treatment at 250 MPa increased micelle size by ∼25%, while treatment at [ges ]300 MPa irreversibly reduced it to ∼50% of that in untreated milk. The increase in micelle size after treatment at 250 MPa was greater with increasing treatment time and temperature and milk pH. Treatment times [ges ]2 min at 400 MPa resulted in similar levels of micelle disruption, but increasing milk pH to 7·0 partially stabilised micelles against HP-induced disruption. Denaturation of α-la did not occur [les ]400 MPa, whereas β-lg was denatured at pressures >100 MPa. Denaturation of α-la and β-lg increased with increasing pressure, treatment time and temperature and milk pH. The majority of denatured β-lg was apparently associated with casein micelles. These effects of HP on casein micelles and whey proteins in milk may have significant implications for properties of products made from HP-treated milk.

Composition of poorly and non-coagulating bovine milk and effect of calcium addition

2010 ◽  
Vol 77 (4) ◽  
pp. 398-403 ◽  
Author(s):  
Elin Hallén ◽  
Anne Lundén ◽  
Anna-Maria Tyrisevä ◽  
Maria Westerlind ◽  
Anders Andrén
Keyword(s):  
Bovine Milk ◽  
Protein Composition ◽  
Calcium Content ◽  
Casein Micelle ◽  
Independent Data ◽  
Coagulation Time ◽  
Data Set ◽  
Milk Samples ◽  
Micelle Size ◽  
Similar Association

Ninety-nine individual milk samples from 37 cows in lactation week 10–35, selected for producing well or poorly/non-coagulating milk, were compared regarding protein composition, total calcium content, casein micelle size, pH, and coagulating properties after addition of 0·05% CaCl2. The results showed that a low κ-casein concentration in milk was a risk factor for non-coagulation. CaCl2 addition improved coagulating properties (coagulation time, curd firmness) of nearly all samples and eliminated differences between poorly/non-coagulating and well-coagulating milk, particularly regarding curd firmness. A second, independent data set with 18 non-coagulating or well-coagulating milk samples were analysed for protein composition, where indications of a similar association with κ-casein was observed.

Interactive Effects of Milk Fat Globule and Casein Micelle Size on the Renneting Properties of Milk

2014 ◽  
Vol 7 (11) ◽  
pp. 3175-3185 ◽  
Author(s):  
Amy Logan ◽  
Li Day ◽  
Audrey Pin ◽  
Martin Auldist ◽  
Andrew Leis ◽  
...  
Keyword(s):  
Milk Fat ◽  
Interactive Effects ◽  
Casein Micelle ◽  
Micelle Size ◽  
Milk Fat Globule ◽  
Fat Globule

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 Aggregation of casein micelle from bovine milk by wheat germ lectin.

1978 ◽  
Vol 42 (10) ◽  
pp. 1923-1926 ◽  
Author(s):  
Masaaki YOSHIKAWA ◽  
Kyoya TAKAHATA ◽  
Ryuzo SASAKI ◽  
Hideo CHIBA
Keyword(s):  
Wheat Germ ◽  
Bovine Milk ◽  
Casein Micelle ◽  
Wheat Germ Lectin

scholarly journals Sedimentation Analysis of Bovine Milk Casein Micelle at pH 6.8 and pH 5.8

1973 ◽  
Vol 20 (10) ◽  
pp. 473-477 ◽  
Author(s):  
I LIANG ◽  
ZENICHIRO HAMAUZU ◽  
SACHIO MATSUMOTO ◽  
DAIZO YONEZAWA
Keyword(s):  
Bovine Milk ◽  
Casein Micelle ◽  
Sedimentation Analysis ◽  
Milk Casein

High pressure homogenisation of raw whole bovine milk (a) effects on fat globule size and other properties

2003 ◽  
Vol 70 (3) ◽  
pp. 297-305 ◽  
Author(s):  
Maurice G Hayes ◽  
Alan L Kelly
Keyword(s):  
High Pressure ◽  
Bovine Milk ◽  
Published Data ◽  
Inlet Temperature ◽  
Casein Micelle ◽  
Two Stage ◽  
Milk Samples ◽  
Globule Size ◽  
Pharmaceutical Industries ◽  
Fat Globule

Although widely adopted by the chemical and pharmaceutical industries in recent years, little published data is available regarding possible applications of high pressure homogenisation for dairy products. The objective of this work was to compare the effects of conventional (18 MPa, two-stage) and single or two-stage high pressure homogenisation (HPH) at 50–200 MPa on some properties of raw whole bovine milk (∼4% fat). Fat globule size decreased as HPH pressure increased and, under certain conditions of temperature and pressure, HPH yielded significantly smaller fat globules than conventional homogenisation. Fat globule size was also affected by milk inlet temperature. The pH of all homogenised milk samples decreased during 24 h refrigerated storage. Total bacterial counts of milk were decreased significantly (P<0·05) for milk samples HPH-treated at 150 or 200 MPa. Whiteness and rennet coagulation properties of milk were unaffected or enhanced, respectively, as homogenisation pressure was increased. Average casein micelle size decreased slightly when skim milk was homogenised at 200 MPa. Thus, HPH treatment has several, potentially significant, effects on milk properties.

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