scholarly journals Effect of microfluidization on casein micelle size of bovine milk

Author(s):  
H Sinaga ◽  
H Deeth ◽  
B Bhandari
2004 ◽  
Vol 71 (1) ◽  
pp. 97-106 ◽  
Author(s):  
Thom Huppertz ◽  
Patrick F Fox ◽  
Alan L Kelly

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.


2010 ◽  
Vol 77 (4) ◽  
pp. 398-403 ◽  
Author(s):  
Elin Hallén ◽  
Anne Lundén ◽  
Anna-Maria Tyrisevä ◽  
Maria Westerlind ◽  
Anders Andrén

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.


2019 ◽  
Vol 50 (6) ◽  
pp. 508-519 ◽  
Author(s):  
Hasitha Priyashantha ◽  
Åse Lundh ◽  
Annika Höjer ◽  
Mårten Hetta ◽  
Monika Johansson ◽  
...  

2021 ◽  
Vol 117 ◽  
pp. 104980
Author(s):  
Marije Akkerman ◽  
Lene Buhelt Johansen ◽  
Valentin Rauh ◽  
Nina Aagaard Poulsen ◽  
Lotte Bach Larsen

1989 ◽  
Vol 56 (3) ◽  
pp. 427-433 ◽  
Author(s):  
Charles W. Slattery ◽  
Satish M. Sood ◽  
Pat Chang

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.


1978 ◽  
Vol 42 (10) ◽  
pp. 1923-1926 ◽  
Author(s):  
Masaaki YOSHIKAWA ◽  
Kyoya TAKAHATA ◽  
Ryuzo SASAKI ◽  
Hideo CHIBA

1973 ◽  
Vol 20 (10) ◽  
pp. 473-477 ◽  
Author(s):  
I LIANG ◽  
ZENICHIRO HAMAUZU ◽  
SACHIO MATSUMOTO ◽  
DAIZO YONEZAWA

2003 ◽  
Vol 70 (3) ◽  
pp. 297-305 ◽  
Author(s):  
Maurice G Hayes ◽  
Alan L Kelly

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.


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 ◽  
...  

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.


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