I. L. Bhoomika ¹, H. M. Jayaprakasha ¹, G. S. Bhat ¹

Affiliations
1 Dairy Science College, KVAFSU, Hebbal, Bangalore - 560 024, IN

Abstract

Caseinophosphopeptides (CPPs) have been shown to possess the unique property of binding macro elements such as Ca, Mg and Fe along with trace elements such as Zn, Ba, Cr, Ni, Co and Se. Milk and dairy products are excellent sources of Ca²⁺. CPPs produced during the digestion of caseins are known to enhance the bio-availability of Ca²⁺ in the diet, specifically by increasing the solubility of Ca²⁺ in the alkaline environment of the small intestine where maximal passive absorption of dietary Ca²⁺ is thought to take place. Casein derived phosphorylated peptides are reported to enhance vitamin D independent bone calcification in rachitic infants.

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T. Suchitra ¹, D. Vijayalaxmi ¹, H. M. Jayaprakasha ¹

Affiliations
1 Departments of Rural Home Science and Dairy Technology, University of Agricultural Sciences, Hebbal, Bangalore-560 024, IN

Abstract

Diets consumed by majority of the population in India are cereal based. Cereals provide 80 per cent of the total calories and a small per cent of protein, but the cereals fail to provide some of the important nutrients like essential amino acids, as they are noted neither for the quality nor for the quantity of protein which they contain. Thus, protein fortification of foods is of current interest because of nutritional awareness, government guidelines and changing demographics.

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B. P. Pushpa ¹, B. Shobha ¹, G. S. Bhat ¹, H. M. Jayaprakasha ¹

Affiliations
1 Department of Dairy Chemistry, University of Agricultural Sciences, Hebbal, Bangalore - 24, IN

Abstract

Cow's milk proteins induce w4de spectrum of allergic disorders in infants and young children causing undesirable effects such as irritation in the respiratory and gastro intestinal track, dermatitis, diarrhoea and nausea. The incidence of sensitivity to cow's milk is approximately 1-2 per cent during the first 2 years of infancy'. A number of studies have shown that the major risk factors of cow's milk allergy are a positive family history of allergy and atopic diseases and early exposure to cow's milk. Among milk proteins, p-lactoglobulin, a major component of cow's milk whey protein, has attracted the attention of many researchers as being the main allergenic substance because of its absence in human milk.

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B. P. Pushpa ¹, G. S. Bhat ¹, H. M. Jayaprakasha ²

Affiliations
1 Department of Dairy Chemistry, Dairy Science College, KVAFSU, Hebbal, Bengaluru-560024, IN
2 Department of Dairy Technology, Dairy Science College, KVAFSU, Hebbal, Bengaluru-560024, IN

Abstract

The allergy due to different fractions of milk protein was estimated by the level of milk specific Ig E blood sera of children suspected for milk allergy with a history of symptoms such as wheezing, diarrhoea or dermatitis. It was observed that among the milk proteins β-lactoglobulin of whey protein is the most potent allergen. Effect of heat treatment and enzymatic hydrolysis on reduction in β-lactoglobulin allergenicity was investigated by inhibition ELISA while heat treatment could reduce the allergenicity only to the extent of 12.5%, enzymatic hydrolysis could reduce the allergenicity significantly. The extent of hydrolysis as well as the enzyme used had significant role in reduction of milk protein allergenicity. The degree of hydrolysis corresponded well with the reduction of milk protein allergenicity. Though chymotrypsin was effective in hydrolyzing β-lactoglobulin, neutrase was more effective in reducing the allergenicity by 52% even at lower degree of hydrolysis. The combination of chymotrypsin and neutrase was found to be more useful in hydrolysis as well as reduction in allergenicity of the protein.

Keywords

β-Lactoglobulin, Allergenicity, Ig E, ELISA, Enzyme Hydrolysis, Heat Treatment.

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