Interactions in Heated Skim Milk between Genetic Variants of β-Lactoglobulin and κ-Casein

1998 ◽  
Vol 46 (8) ◽  
pp. 3004-3008 ◽  
Author(s):  
Toomas Allmere ◽  
Anders Andrén ◽  
Anne Lundén ◽  
Lennart Björck
1995 ◽  
Vol 62 (4) ◽  
pp. 593-600 ◽  
Author(s):  
Gilles Robitaille

SUMMARYHeat coagulation time-pH curves at 140°C were obtained for 43 blended skim milk samples from Holstein cows to determine the effects of genetic variants of κ-casein and β-lactoglobulin on milk heat stability. The blended milk samples were similar in terms of protein content and milk salts, but were genotypically different for κ-casein (AA, AB) and β-lactoglobulin (AA, AB, BB). Type A curves were obtained for all milks. Maximum heat stability was affected by the κ-casein genotype (AB > AA, P < 0·01) but the influence of the β-lactoglobulin genotype was only significant when the κ-casein AA genotype was present (β-lactoglobulin AA > BB, P < 0·0001). Minimum heat stability was significantly higher (P < 0·0001) for milk genotyped κ-casein AB:β-lactoglobulin BB. The effects of milk genotyped κ-casein BB on maximum and minimum heat stability were determined by analysing individual milks: κ-casein BB:β-lactoglobulin AB (n=8) and reconstituted milks: κ-casein BB:β-lactoglobulin AA, AB and BB (n = 17). Type B curves were obtained on three occasions for individual κ-casein BB:β-lactoglobulin AB milk and on five occasions in the case of reconstituted milks with κ-casein BB:β-lactoglobulin AA, AB and BB. This suggests a relationship between the type B curve and the κ-casein B genetic variant. Comparison of the mean values of heat stability at the pH of maximum heat stability of each individual and reconstituted milk genotype suggested that the best genotype for κ-casein in terms of heat stability was BB.


1987 ◽  
Vol 54 (2) ◽  
pp. 219-235 ◽  
Author(s):  
Douglas M. McLean ◽  
E. R. Bruce Graham ◽  
Raul W. Ponzoni ◽  
Hugh A. Mckenzie

SummarySkim milk samples from 126 Friesian and 147 Jersey cows in eight commercial herds were preheated at 85 °C for 30 min and concentrated to 200 g l−1 total solids. A heat coagulation time–pH curve was determined at 120 °C for each treated sample. Heat coagulation times ranged from 1 to 50 min at the non-adjusted pH and 1 to 60 min at the pH of maximum stability. The following statistically significant effects were found. Maximum heat stability was affected by genetic variants of κ-casein (B > AB > A; P < 0·001) and β-lactoglobulin (B, AB>A; P < 0·05) whereas natural heat stability was affected only by κ-casein genetic variants (B > AB > A; P < 0·001). Maximum and natural heat stability were corre-lated positively with β-casein and κ-casein concentrations and were negatively correlated with αs1-casein and β-lactoglobulin concentrations. Milk from Jersey cows had greater maximum and natural heat stability than milk from Friesian cows. Differences were found between herds within breed for natural heat stability, but not for maximum heat stability. Maximum heat stability declined with age of the cow. The heat stability of skim milk samples taken from 40 Jersey cows in one of the herds was determined at 140 °C. A considerable variation was found in the coagulation time–pH curves. There was a difference in natural heat stability between κ-casein variants (B > AB; P < 0°05). Natural and maximum heat stability were correlated positively with urea concentration. No relationship was found between the heat stability of preheated concentrated skim milk and the heat stability of the original skim milk. The pH of skim milk samples was associated with αs1-casein genetic variant, age of cow, stage of lactation and concentration of γ-casein.


Beverages ◽  
2018 ◽  
Vol 4 (4) ◽  
pp. 95 ◽  
Author(s):  
Jared Raynes ◽  
Delphine Vincent ◽  
Jody Zawadzki ◽  
Keith Savin ◽  
Dominik Mertens ◽  
...  

Milk samples with twelve combinations of κ- and β-casein (CN) and β-lactoglobulin (β-Lg) variants were obtained to investigate the effect of protein variant on the mechanism/s of age gelation in ultra-high temperature (UHT) skim milk. Only milk groups with κ-CN/β-CN/β-Lg combinations AB/A1A2/AB and AB/A2A2/AB suffered from the expected age gelation over nine months storage, although this could not be attributed to the milk protein genetic variants. Top-down proteomics revealed three general trends across the twelve milk groups: (1) the abundance of intact native proteins decreases over storage time; (2) lactosylated proteoforms appear immediately post-UHT treatment; and (3) protein degradation products accumulate over storage time. Of the 151 identified degradation products, 106 (70.2%) arose from β-CN, 33 (21.9%) from αs1-CN, 4 (2.7%) from β-Lg, 4 (2.7%) from α-La, 3 (2%) from κ-CN and 1 (0.7%) from αs2-CN. There was a positive correlation between milk viscosity and 47 short peptides and four intact proteoforms, while 20 longer polypeptides and 21 intact proteoforms were negatively correlated. Age gelation was associated with specific patterns of proteolytic degradation and also with the absence of the families Bacillaceae, Aerococcaceae, Planococcaceae, Staphylococcaceae and Enterobacteriaceae, present in all the non-gelling milk groups pre-UHT.


Foods ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 888
Author(s):  
Zhibin Li ◽  
Dasong Liu ◽  
Shu Xu ◽  
Wenjin Zhang ◽  
Peng Zhou

Effects of pore diameters (100, 50, and 20 nm), concentration factors (1–8) and processing stages (1–5) on the transmission of major serum proteins (β-lactoglobulin and α-lactalbumin) and minor serum proteins (immunoglobulin (Ig) G, IgA, IgM, lactoferrin (LF), lactoperoxidase (LPO), xanthine oxidase (XO)) during ceramic microfiltration (MF) of skim milk were studied. Holstein skim milk was microfiltered at a temperature of 50 °C, a transmembrane pressure of 110 kPa and a crossflow velocity of 6.7 m/s, using a tubular single stainless steel module that consisted of three ceramic tubes, each with 19 channels (3.5 mm inner diameter) and a length of 0.5 m. For MF with 100 nm and 50 nm pore diameters, the recovery yield of major serum proteins in permeate was 44.3% and 44.1%, while the recovery yield of minor serum proteins was slightly less by 0%–8% than 50 nm MF. MF with 20 nm pore diameters showed a markedly lower (by 12%–45%) recovery yield for both major and minor serum proteins, corresponding with its lower membrane flux. Flux sharply decreased with an increasing concentration factor (CF) up to four, and thereafter remained almost unchanged. Compared to the decrease (88%) of flux, the transmission of major and minor serum proteins was decreased by 4%–15% from CF = one to CF = eight. With increasing processing stages, the flux gradually increased, and the recovery yield of both major and minor proteins in the permeate gradually decreased and reached a considerably low value at stage five. After four stages of MF with 100 nm pore diameter and a CF of four for each stage, the cumulative recovery yield of major serum proteins, IgG, IgA, IgM, LF, LPO, and XO reached 95.7%, 90.8%, 68.5%, 34.1%, 15.3%, 39.1% and 81.2% respectively.


2022 ◽  
Vol 124 ◽  
pp. 107186
Author(s):  
Davor Daniloski ◽  
Noel A. McCarthy ◽  
Tatijana Markoska ◽  
Martin J. Auldist ◽  
Todor Vasiljevic

2011 ◽  
Vol 94 (4) ◽  
pp. 1043-1059 ◽  
Author(s):  
Petra Lutter ◽  
Véronique Parisod ◽  
Hans Weymuth

Abstract The protection of allergic consumers is crucial to the food industry. Therefore, accurate methods for the detection of food allergens are required. Targeted detection of selected molecules by MS combines high selectivity with accurate quantifcation. A confrmatory method based on LC/selected reaction monitoring (SRM)-MS/MS was established and validated for the quantifcation of milk traces in food. Tryptic peptides of the major milk proteins β-lactoglobulin, β-casein, αS2-casein, and κ-casein were selected as quantitative markers. Precise quantifcation was achieved using internal standard peptides containing isotopically labeled amino acids. For each peptide, qualifer and quantifer fragments were selected according to Commission Decision 2002/657/EC. A simple sample preparation method was established without immunoaffnity or SPE enrichment steps for food matrixes containing different amounts of protein, such as baby food, breakfast cereals, infant formula, and cereals. Intermediate reproducibility, repeatability, accuracy, and measurement uncertainty were determined for each matrix. LOD values of 0.2–0.5 mg/kg, e.g., for β-lactoglobulin, were comparable to those obtained with ELISA kits. An LOQ of approximately 5 mg/kg, expressed as mass fraction skim milk powder, was validated in protein-rich infant cereals. The obtained validation data show that the described LC/SRM-MS/MS approach can serve as a confrmatory method for the determination of milk traces in selected food matrixes.


Foods ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 1721
Author(s):  
Ritika Puri ◽  
Upendra Singh ◽  
James A. O’Mahony

The effects of processing temperature on filtration performance and characteristics of retentates and permeates produced during ultrafiltration (UF) of skim milk at 5, 20, and 50 °C were investigated. The results indicate that despite higher flux at 50 °C, UF under these conditions resulted in greater fouling and rapid flux decline in comparison with 5 and 20 °C. The average casein micelle diameter was higher in retentate produced at 5 and 20 °C. The retentate analysed at 5 °C displayed higher viscosity and shear thinning behaviour as compared to retentate analysed at 20 and 50 °C. Greater permeation of calcium and phosphorus was observed at 5 and 20 °C in comparison with 50 °C, which was attributed to the inverse relationship between temperature and solubility of colloidal calcium phosphate. Permeation of α-lactalbumin was observed at all processing temperatures, with permeation of β-lactoglobulin also evident during UF at 50 °C. All UF retentates were shown to have plasmin activity, while lower activity was measured in retentate produced at 5 °C. The findings revealed that UF processing temperature influences the physicochemical, rheological, and biochemical properties of, and thereby govern the resulting quality and functionality of, retentate- and permeate-based dairy ingredients.


Author(s):  
Henk Bovenhuis

Several studies have shown milk protein genetic variants to be associated with manufacturing properties of milk. The main findings were that κ-casein genetic variants affect renneting time of milk and βlactoglobulin genetic variants are associated with casein number (reviewed by Grosclaude, 1988). There are reports also of associations between milk protein genetic variants and milk production traits. Results from these studies indicate that κ-casein genotypes are associated with protein content and βlactoglobulin genotypes are related to fat content (reviewed by Bovenhuis et al., 1992). Therefore, κ-casein and βlactoglobulin genotypes might be of value as selection criteria. The aim of the present study was to quantify the potential effects of selection for κ-casein and β-lactoglobulin genotypes by using stochastic simulation of a closed adult MOET nucleus breeding scheme.


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