Milk allergens, their characteristics and their detection in food: A review

Monaci, Linda; Tregoat, Virginie; Hengel, Arjon J. van; Anklam, Elke

doi:10.1007/s00217-005-0178-8

Cited by 228 publications

(220 citation statements)

References 268 publications

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“…In previous studies, the content of α-lactalbumin and β-lactoglobulin in cow's milk was the following: 1-1.5 g·l -1 and 3-4 g·l -1 (Monaci et al 2006), 0.6-1.7 g·l -1 and 2-4 g·l -1 (Farrell et al 2004), respectively. Sztankóová (2006) The contents and genetic variants of fractions of different types of milk are different.…”

Section: Discussionmentioning

confidence: 90%

“…gelling, filmforming, foaming and emulsifying) (Moatsou et al 2005). However, lactoglubulins can also cause development of allergy to cow's milk, mainly affecting children (Monaci et al 2006). The most allergenic whey protein is β-lactoglobulin, which constitutes 50% of whey proteins.…”

mentioning

confidence: 99%

“…Nevertheless, some studies (Skripak et al 2008;Passalacqua et al 2012) indicate that administration of gradually increasing doses of the allergen leads in children to induction of tolerance to the substance that originally caused the allergic reaction. It is therefore important, especially for people suffering from allergy to milk protein, to know the content of particular proteins in food (Monaci et al 2006;Passalacqua et al 2012). The content of whey proteins and identification of individual fractions are also important because of milk adulteration, especially in case of replacement of goat's or sheep's milk by cow's milk.…”

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confidence: 99%

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Determination of whey proteins in different types of milk

et al. 2014

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Protein analysis is very important both in terms of milk protein allergy, and of milk and dairy product adulteration (β-lactoglobulin may be an important marker in the detection of milk adulteration). The aim of this study was to detect major whey proteins α-lactalbumin and β-lactoglobulin and their genetic variants by reversed-phase high-performance liquid chromatography. Milk samples from cows (n = 40), goats (n = 40) and sheep (n = 40) were collected at two farms and milk bars in the Czech Republic from April to June 2010. The concentration of α-lactalbumin was higher in goat's milk (1.27 ± 0.05 g·l -1 , P < 0.001) and cow's milk (1.16 ± 0.02 g·l -1, P = 0.0037) compared to sheep's milk (0.95 ± 0.06 g·l -1 ); however, concentration of α-lactalbumin in goat's milk and cow's milk did not differ significantly (P < 0.05). Goat's milk contained less β-lactoglobulin (3.07 ± 0.08 g·l -1 ) compared to cow's milk (4.10 ± 0.04 g·l -1 , P < 0.001) or sheep's milk (5.97 ± 0.24 g·l -1 , P < 0.001). A highly significant positive correlation (r = 0.8686; P < 0.001) was found between fraction A and B of β-lactoglobulin in sheep's milk, whereas in cow's milk there was a negative correlation (r = -0.3010; P = 0.0296). This study summarizes actual information of the whey protein content in different types of milk which may be relevant in assessing their allergenic potential. -lactalbumin, β-lactoglobulin, cow, goat, sheep, RP-HPLC α

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Section: Discussionmentioning

confidence: 90%

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confidence: 99%

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confidence: 99%

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Determination of whey proteins in different types of milk

et al. 2014

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“…With its increasing incidence over the last years, it represents an important health problem, especially in industrialized countries, where it has been estimated to affect about 2% 20 of the adult population and up to 8% of children (Monaci et al 2006). Together with hen's egg, cow's milk, fish, crustacea, peanut, tree nuts and wheat, soybeans belong to the 'big 22 Due to its diverse functional properties, such as water and fat absorption, emulsification, foaming and gelation, soybean proteins are often included during food processing steps.…”

Section: Introductionmentioning

confidence: 99%

Effect of protein glycation in the presence or absence of wheat proteins on detection of soybean proteins by commercial ELISA

Platteau¹,

Cucu²,

Meulenaer³

et al. 2011

Food Additives & Contaminants: Part A

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“…population and up to 8% of children (Monaci et al, 2006). Together with the hen's egg, cow's milk, fish, crustacean, peanut, soybean and wheat, tree nuts are typically associated with 24 severe allergic reactions.…”

mentioning

confidence: 99%

ELISA detection of hazelnut proteins: effect of protein glycation in the presence or absence of wheat proteins

Cucu

Platteau

Taverniers

et al. 2010

Food Additives & Contaminants: Part A

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Hazelnuts are widely used in the food industry, especially confectionary foods. Nevertheless, these nuts contain several allergenic proteins that may be unexpectedly present as contaminants in various foods and may pose a serious threat to allergic consumers. The enzyme-linked immunosorbent assay ( ELISA) is the preferred method to assess the level of hazelnut protein contamination. It is commonly used by both the food industry and enforcement agencies. Several ELISA kits are commercially available. However, protein detectability by ELISA may be affected by severe changes that proteins undergo during processing. The aim of this study is therefore to investigate the impact of processing on the ability to detect hazelnut protein by four commercial ELISA kits. Hazelnut proteins in the presence or absence of soluble wheat proteins were modified with glucose via the Maillard reaction. Changes in hazelnut proteins, such as the formation of protein-bound carbonyls, losses of reactive lysine residues and free amino groups, and severe aggregation dramatically affected the hazelnut protein detection by the commercial kits. The observed impact was highly dependent on the type of ELISA kit used

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Milk allergens, their characteristics and their detection in food: A review

Cited by 228 publications

References 268 publications

Determination of whey proteins in different types of milk

Determination of whey proteins in different types of milk

Effect of protein glycation in the presence or absence of wheat proteins on detection of soybean proteins by commercial ELISA

ELISA detection of hazelnut proteins: effect of protein glycation in the presence or absence of wheat proteins

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