Improving the sensory quality, shelf-life and functionality of milk

Kelly, Philip M.; Woonton, Brad W.; Smithers, Geoffrey W.

doi:10.1533/9781845695569.2.170

Cited by 16 publications

(11 citation statements)

References 196 publications

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“…overall accuracy was between 0.86 and 1.18 g/100 g powder. This is perhaps due to the higher content of tryptophan-rich alpha-lactalbumin in the formula which may have skewed the instrument response (Kelly, Woonton, & Smithers, 2009). Therefore, users must be careful when drawing comparisons between products which exhibit significant differences in tryptophan rich or deficient proteins.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Fluorescence-based analyser as a rapid tool for determining soluble protein content in dairy ingredients and infant milk formula

Henihan

O'Donnell

Esquerre

et al. 2019

Innovative Food Science & Emerging Technologies

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Section: Accepted Manuscriptmentioning

confidence: 99%

Fluorescence-based analyser as a rapid tool for determining soluble protein content in dairy ingredients and infant milk formula

Henihan

O'Donnell

Esquerre

et al. 2019

Innovative Food Science & Emerging Technologies

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“…Caseins (Bos d8) and β-lactoglobulin (β-lg; Bos d5) are the strongest allergens, but the list also includes bovine serum albumin (BSA; Bos d 6). Caseins comprise nearly 80% of total milk proteins, and β-lg and BSA nearly 3% each [12,13,14]. Cross-reactivity between BSA and other bovine proteins has been observed in milk and meat, suggesting that BSA is a potential allergen for CMA patients [15].…”

Section: Introductionmentioning

confidence: 99%

Milk and Meat Allergens from Bos taurus β-Lactoglobulin, α-Casein, and Bovine Serum Albumin: An In-Vivo Study of the Immune Response in Mice

Fuc¹,

Złotkowska²,

Wróblewska³

2019

Nutrients

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The mechanism of food allergy may vary. This study aimed to compare the effects of milk, yogurt, or beef meat supplementation on humoral and cellular immune responses in a mice model. Mice were divided into four groups: The “Milk group” was sensitized with a β-lactoglobulin (β-lg)/α-casein (α-CN) mixture and supplemented cow milk; the “Yogurt group” was sensitized with β-lg/α-CN and supplemented yogurt; the “Beef group” was immunized with bovine serum albumin (BSA) and supplemented beef meat; and the “PBS group” received PBS in all procedures. ELISA was used to measure humoral response, including: Total IgE, specific IgG, and IgA. Cellular response was determined by phenotyping lymphocyte from lymphoid tissue and measuring the Th1/Th2 cytokine concentration with flow cytometry. The qPCR method was used for quantification of the fecal microbiota. The results obtained revealed a lower IgE level for the Yogurt group than for the Milk one. In the Yogurt group, the contribution of regulatory T cells to MLN and PP was higher compared to the other groups. We confirmed that diet supplementation with yogurt modulates the immune response to the prime allergen, and changes the activity of serum antibodies to milk proteins and BSA. Based on a specific antibodies level, we cannot exclude the possibility of CMA mice reaction against BSA.

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“…For example, at pH values between 5.2 and 7.0, it is a dimer, and its molecular weight (MW) is around 37 kDa. However, at pH values over 8.0, it exists as a monomer, and its MW is approximately 18 kDa [19]. This protein has a great potential as milk allergen because it is remarkably stable and it is not present in human milk [20], and, apart from that, it is regularly used as an additive in lots of food products [21].The development of analytical approaches used to detect and quantify food allergens has become increasingly significant [22] because labeling in food is crucial for the consumers, in order to prevent major health problems.…”

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confidence: 99%

mentioning

confidence: 99%

Folding-Based Electrochemical Aptasensor for the Determination of β-Lactoglobulin on Poly-L-Lysine Modified Graphite Electrodes

Amor-Gutiérrez

Selvolini

Fernández‐Abedul

et al. 2020

Sensors

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Nowadays, food allergy is a very important health issue, causing adverse reactions of the immune system when exposed to different allergens present in food. Because of this, the development of point-of-use devices using miniaturized, user-friendly, and low-cost instrumentation has become of outstanding importance. According to this, electrochemical aptasensors have been demonstrated as useful tools to quantify a broad variety of targets. In this work, we develop a simple methodology for the determination of β-lactoglobulin (β-LG) in food samples using a folding-based electrochemical aptasensor built on poly-L-lysine modified graphite screen-printed electrodes (GSPEs) and an anti-β-lactoglobulin aptamer tagged with methylene blue (MB). This aptamer changes its conformation when the sample contains β-LG, and due to this, the spacing between MB and the electrode surface (and therefore the electron transfer efficiency) also changes. The response of this biosensor was linear for concentrations of β-LG within the range 0.1-10 ng·mL −1 , with a limit of detection of 0.09 ng·mL −1 . The biosensor was satisfactorily employed for the determination of spiked β-LG in real food samples.incidence of the most popular food allergies throughout Europe [13] revealed that allergy to cow's milk is, nowadays, the most frequent food allergy, especially in early-age children, implying a percentage of around 6% in the youngest population [14,15]. Immunoglobulin E (IgE) normally mediates cow's milk allergy, and the symptoms usually occur within 2 h after milk intake [16]. In whey from cow's milk, one of the most important proteins considered to be an allergen is β-lactoglobulin (β-LG), which is classified within the lipocalins, a group of binding proteins with small ligands [17]. Its quaternary structure, identified in 1997 using X-Ray diffraction [18], is dependent on the pH. For example, at pH values between 5.2 and 7.0, it is a dimer, and its molecular weight (MW) is around 37 kDa. However, at pH values over 8.0, it exists as a monomer, and its MW is approximately 18 kDa [19]. This protein has a great potential as milk allergen because it is remarkably stable and it is not present in human milk [20], and, apart from that, it is regularly used as an additive in lots of food products [21].The development of analytical approaches used to detect and quantify food allergens has become increasingly significant [22] because labeling in food is crucial for the consumers, in order to prevent major health problems. The analysis of allergens in food samples [23] is usually carried out by immunoassay-based approaches, such as enzyme-linked immunosorbent assays (ELISAs) [11,14,24] or lateral-flow immunoassays (LFIAs) [25,26], as well as DNA-based methods, which detect the genes encoding for the proteins using amplifying methods, for instance, the polymerase chain reaction (PCR) [27,28]. Proteomic tests have been also used for the determination of allergens [29]. Although these methods are very sensitive, they are time-consuming and the instrumenta...

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Improving the sensory quality, shelf-life and functionality of milk

Cited by 16 publications

References 196 publications

Fluorescence-based analyser as a rapid tool for determining soluble protein content in dairy ingredients and infant milk formula

Fluorescence-based analyser as a rapid tool for determining soluble protein content in dairy ingredients and infant milk formula

Milk and Meat Allergens from Bos taurus β-Lactoglobulin, α-Casein, and Bovine Serum Albumin: An In-Vivo Study of the Immune Response in Mice

Folding-Based Electrochemical Aptasensor for the Determination of β-Lactoglobulin on Poly-L-Lysine Modified Graphite Electrodes

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