scholarly journals Investigating changes of proteome in the bovine milk serum after retort processing using proteomics techniques

2021 ◽  
Author(s):  
Zikai Wei ◽  
Jiaxin Kang ◽  
Minhe Liao ◽  
Huanhuan Ju ◽  
Rong Fan ◽  
...  
Keyword(s):  
Bovine Milk ◽  
Milk Serum ◽  
Retort Processing

Observations on the influence of high cell count on lipolysis in bovine milk

1979 ◽  
Vol 46 (3) ◽  
pp. 453-462 ◽  
Author(s):  
Amer M. A. Salih ◽  
Malcolm Anderson
Keyword(s):  
Cell Count ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Bovine Milk ◽  
Skim Milk ◽  
High Cell ◽  
Lipoprotein Lipase Activity ◽  
Milk Serum ◽  
Cell Counts ◽  
And Control

SummaryThe effect that changes in composition which occur in milks possessing high cell counts have on milk lipolysis has been investigated. High cell counts were produced either by intramammary infusion of Escherichia coli endotoxin or Streptococcus agalactiae or by addition of washed cells which were isolated from milk obtained from quarters infused with endotoxin. Free fatty acid levels in milk were measured in terms of acid degree value (ADV) either as initial ADV measured immediately after milking or ADV developed after a prescribed incubation period.There was an increase in initial ADV after the infusion either of endotoxin or of Str. agalactiae relative to a control quarter. This increase appeared to be associated with changes in cell count, but in absolute terms the influence of cells on ADV became less as cell count increased. Neither type of infusion had any effect on lipoprotein lipase activity. The addition of washed cells to normal milk resulted in an increase in developed ADV, but the increment was not as large as that produced by the addition of 1% blood serum. When cream and skim-milk from endotoxin-treated quarters and control quarters were mixed in different combinations with and without additional cells, developed ADV was higher in those samples containing endotoxin cream and those with added cells. Milk from a quarter treated with endotoxin was diluted with its own skim-milk to produce different cell counts and ADV was determined after various time intervals at 4 and 37 °C. Lipolysis increased with increasing cell count, but a depression in lipolytic rate was noted after incubation for 6 h at 4 °C and 20 min at 37 °C.The proportion of skim-milk lipoprotein lipase activity in milk serum was larger both in milks possessing high cell counts and in normal milk adjusted to between 5 and 20 mM-NaCl by addition of solid NaCl. These levels of NaCl inhibited lipolysis.The possible direct and indirect effects of high cell count on milk lipolysis are discussed.

Factors affecting the distribution of lipoprotein lipase activity between serum and casein micelles in bovine milk

1982 ◽  
Vol 49 (1) ◽  
pp. 51-59 ◽  
Author(s):  
Malcolm Anderson
Keyword(s):  
Blood Serum ◽  
Lipoprotein Lipase ◽  
Post Partum ◽  
Bovine Milk ◽  
Casein Micelles ◽  
Factors Affecting ◽  
Milk Serum ◽  
Heparin Treatment ◽  
Micellar Casein ◽  
Consistent Increase

SUMMARYThe influence of mastitis and early lactation, and the effect of treating milk with heparin, blood serum and trypsin, on the proportion of lipoprotein lipase (LPL) activity in milk serum was investigated. The relative importance of milk serum LPL and LPL bound to micellar casein in promoting lipolysis was also examined. Colostrum contained LPL activity, 45% of which was found in the serum phase in samples obtained from the first milking post partum, but this value fell to 34% in samples taken 24 h later. The proportion of serum LPL was also increased in milks from quarters infected with Staphylococcus aureus, but not after overnight treatment of normal milk at 4 °C with 5% (w/v) blood serum or 2 µg/ml trypsin. The addition of 5 µg/ml heparin resulted in a consistent increase in serum LPL which varied between 14 and 50% of total milk LPL. Heparin did not release all the enzyme bound to casein micelles even after a second heparin treatment of resuspended micelles. Serum LPL was more effective in promoting lipolysis and was more responsive to blood serum activation than LPL bound to casein micelles. Lipolysis increased after heparin treatment but the increase was not related to serum LPL activity.

scholarly journals Effect of Processing Intensity on Immunologically Active Bovine Milk Serum Proteins

Nutrients ◽  
2017 ◽  
Vol 9 (9) ◽  
pp. 963 ◽  
Author(s):  
Tabea Brick ◽  
Markus Ege ◽  
Sjef Boeren ◽  
Andreas Böck ◽  
Erika von Mutius ◽  
...  
Keyword(s):  
Serum Proteins ◽  
Bovine Milk ◽  
Milk Serum

Identification of lipid synthesis and secretion proteins in bovine milk

2014 ◽  
Vol 81 (1) ◽  
pp. 65-72 ◽  
Author(s):  
Jing Lu ◽  
Toon van Hooijdonk ◽  
Sjef Boeren ◽  
Jacques Vervoort ◽  
Kasper Hettinga
Keyword(s):  
Dairy Cows ◽  
Milk Fat ◽  
Bovine Milk ◽  
Lipid Synthesis ◽  
Milk Proteins ◽  
Milk Fat Globule Membrane ◽  
Milk Serum ◽  
Milk Fat Globule ◽  
Fat Globule ◽  
Secretion Pathways

Lactation physiology is a process that is only partly understood. Proteomics techniques have shown to be useful to help advance the knowledge on lactation physiology in human and rodent species but have not been used as major tools for dairy cows, except for mastitis. In this paper, advanced non-targeted proteomics techniques (Filter aided sample preparation and NanoLC-Orbitrap-MS/MS) were applied to study the milk fat globule membrane and milk serum fraction, resulting in the identification of 246 proteins. Of these, 23 transporters and enzymes were related to lipid synthesis and secretion in mammary gland and their functions are discussed in detail. The identification of these intracellular transporters and enzymes in milk provides a possibility of using milk itself to study lipid synthesis and secretion pathways. This full-scale scan of milk proteins by using non-targeted proteomic analysis helps to reveal the important proteins involved in lipid synthesis and secretion for further examination in targeted studies.

Effect of high-pressure treatment at various temperatures on indigenous proteolytic enzymes and whey protein denaturation in bovine milk

2008 ◽  
Vol 75 (3) ◽  
pp. 262-269 ◽  
Author(s):  
Golfo Moatsou ◽  
Constantinos Bakopanos ◽  
Dimitis Katharios ◽  
George Katsaros ◽  
Ioannis Kandarakis ◽  
...  
Keyword(s):  
High Pressure ◽  
Whey Protein ◽  
Cathepsin D ◽  
Room Temperature ◽  
Protein Denaturation ◽  
Proteolytic Enzymes ◽  
Bovine Milk ◽  
Negative Effects ◽  
Milk Serum ◽  
Β Lactoglobulin

The objective of the present study was to determine the effect of high pressure (HP) processing (200, 450 and 650 MPa) at various temperatures (20, 40 and 55°C) on the total plasmin plus plasminogen-derived activity (PL), plasminogen activator(s) (PA) and cathepsin D activities and on denaturation of major whey proteins in bovine milk. Data indicated that transfer of both PL and PA from the casein micelles to milk serum occurred at all pressures utilized at room temperature (20°C). In addition to the transfer of PL and PA from micelles, there were reductions in activities of PL (16–18%) and PA (38–62%) for the pressures 450 and 650 MPa, at room temperature. There were synergistic negative effects between pressure and temperature on residual PL activity at 450 and 650 MPa and on residual PA activity only at 450 MPa. Cathepsin D activity in the acid whey from HP-treated milk was in general baroresistant at room temperature. The residual activity of cathepsin D decreased significantly at 650 MPa and 40°C and at the pressures 450 and 650 MPa at 55°C. Synergistic negative effects on the amount of native β-lactoglobulin were observed at 450 and 650 MPa and on the amount of native α-lactalbumin at 650 MPa. There were significant correlations between enzymatic activities (PL, PA and cathepsin D) and the residual native β-lactoglobulin and α-lactalbumin in bovine milk. In conclusion, HP significantly affected the activity of indigenous proteolytic enzymes and whey protein denaturation in bovine milk. Reduction in activity of indigenous enzymes (PL, PA and cathepsin D) and transfer of PL and PA from the casein to milk serum induced by HP is expected to have a profound effect on cheese yield, proteolysis during cheese ripening and quality of UHT milk during storage.

Factors affecting the ethanol stability of bovine milk: II. The origin of the pH transition

1981 ◽  
Vol 48 (2) ◽  
pp. 285-291 ◽  
Author(s):  
David S. Horne ◽  
Thomas G. Parker
Keyword(s):  
Bovine Milk ◽  
Skim Milk ◽  
Soluble Phosphate ◽  
Ph Profile ◽  
Factors Affecting ◽  
Milk Serum ◽  
Ethanol Stability ◽  
Artificial Mixtures

SummaryDialysing milk against phosphate-free sera showed that the transition in the ethanol (EtOH) stability/pH profile was associated with the soluble phosphate component of the milk serum. Sigmoidal behaviour similar to that of milk was reproduced when the EtOH stability of artificial mixtures of casein, Ca and phosphate was measured as a function of pH. A mechanism for the s coagulation of skim-milk is discussed.

Superoxide Dismutase Activity in Bovine Milk Serum

1979 ◽  
Vol 42 (11) ◽  
pp. 867-871 ◽  
Author(s):  
M. KORYCKA-DAHL ◽  
T. RICHARDSON ◽  
C. L. HICKS
Keyword(s):  
Superoxide Dismutase ◽  
Cytochrome C ◽  
Polyacrylamide Gel Electrophoresis ◽  
Bovine Milk ◽  
Enzymic Activity ◽  
Superoxide Dismutase Activity ◽  
Bovine Erythrocyte ◽  
Milk Serum ◽  
Erythrocyte Superoxide Dismutase ◽  
Acid Whey

Superoxide dismutase activity was shown to be present in bovine milk serum and was quantified by measuring the capacity of retentate from dialyzed milk serum to inhibit reduction of cytochrome c by xanthine-xanthine oxidase-generated superoxide anion. One unit of enzyme was defined as the quantity of superoxide dismutase which inhibits cytochrome c reduction by 20%. By this definition 19,500 units of enzyme were present per liter of retentate from dialyzed milk serum. This amount is equivalent to about 2.4 mg of purified bovine erythrocyte superoxide dismutase per liter. Polyacrylamide gel electrophoresis of a partially-purified superoxide dismutase from acid whey, followed by staining for enzymic activity, confirmed the presence of the enzyme in milk serum which was identical in electrophoretic properties to those of bovine erythrocyte copper-zinc superoxide dismutase. Pasteurization at 63 C for 30 min did not decrease superoxide dismutase activity in milk serum. Heating of purified bovine erythrocyte-superoxide dismutase at 100 C for 1 min resulted in almost complete loss of enzymic activity, whereas the partially-purified superoxide dismutase from acid whey still retained 40% of the original activity under these conditions. Bovine milk superoxide dismutase may be an important naturally-occurring antioxidant for increasing oxidative stability of milk and other dairy products.

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