Effect of heat treatment on the antigenicity of bovine α-lactalbumin and β-lactoglobulin in whey protein isolate

Bu, Guanhao; Luo, Yongkang; Zheng, Zhe; Hai, Zheng

doi:10.1080/09540100903026116

Cited by 115 publications

(71 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Covalent bonds were suggested corresponding to the degree of saccharide polymerization [28]. With the formation of numerous polymers, the antigenicity of glycated products might be altered since these generated adducts may mask IgE binding epitopes [29,30].…”

Section: Resultsmentioning

confidence: 98%

“…Lagemaat et al [16] reported that the antigenicity of wet-heated SPI in the absence of fructooligosaccharides or fructose reduced up to 20 %, and the electrophoretic behavior of allergenic β-conglycinin and glycinin was modified. High temperature for longtime may make protein denature and expose the buried sulfhydryl groups, exchange sulfhydryl-disulfide in molecular, and then the antigenic epitopes hidden inside exposed owing to the protein unfolding of conformational structure [29,34].…”

Section: Antigenicity Of the Glycated Productsmentioning

confidence: 99%

See 1 more Smart Citation

Effects of saccharide on the structure and antigenicity of β-conglycinin in soybean protein isolate by glycation

Zhu

Chen

et al. 2014

Eur Food Res Technol

Self Cite

View full text Add to dashboard Cite

Section: Resultsmentioning

confidence: 98%

Section: Antigenicity Of the Glycated Productsmentioning

confidence: 99%

Effects of saccharide on the structure and antigenicity of β-conglycinin in soybean protein isolate by glycation

Zhu

Chen

et al. 2014

Eur Food Res Technol

Self Cite

View full text Add to dashboard Cite

“…The effect of heat in moderating the antigenicity of α-lactalbumin and β-lactoglobulin in whey protein isolate was investigated through indirect competitive enzyme-linked immunosorbent assay (ELISA). Above 90°C, the antigenicity of both proteins showed significant drop (Bu et al 2009). Yet it is a predominant risk factor for infants.…”

Section: Quality Improvement/combination With Other Supplementmentioning

confidence: 99%

Emerging trends in nutraceutical applications of whey protein and its derivatives

Patel

2015

J Food Sci Technol

125

View full text Add to dashboard Cite

The looming food insecurity demands the utilization of nutrient-rich residues from food industries as valueadded products. Whey, a dairy industry waste has been characterized to be excellent nourishment with an array of bioactive components. Whey protein comprises 20 % of total milk protein and it is rich in branched and essential amino acids, functional peptides, antioxidants and immunoglobulins. It confers benefits against a wide range of metabolic diseases such as cardiovascular complications, hypertension, obesity, diabetes, cancer and phenylketonuria. The protein has been validated to boost recovery from resistance exercise-injuries, stimulate gut physiology and protect skin against detrimental radiations. Apart from health invigoration, whey protein has proved its suitability as fat replacer and emulsifier. Further, its edible and antimicrobial packaging potential renders its highly desirable in food as well as pharmaceutical sectors. Considering the enormous nutraceutical worth of whey protein, this review emphasizes on its established and emerging biological roles. Present and future scopes in food processing and dietary supplement formulation are discussed. Associated hurdles are identified and how technical advancement might augment its applications are explored. This review is expected to provide valuable insight on whey protein-fortified functional foods, associated technical hurdles and scopes of improvement.

show abstract

“…Whey proteins present in dairy products (α-la and β-lg) were denatured and modified so that they did not react with human sera. At the moment there is no sufficient data in the literature on the protein detected in electrophoresis and characterised as BSA without confirming the data by immunoblot (Sletten et al 2008), and BSA or LF as potential allergens (Bu et al 2009). …”

Section: Allergnicity Of Food Extract Proteinsmentioning

confidence: 94%

Cow's milk proteins immunoreactivity and allergenicity in processed food

Wróblewska¹,

Kaliszewska²

2012

Czech J. Food Sci.

View full text Add to dashboard Cite

Wróblewska B., Kaliszewska A. (2012): Cow's milk proteins immunoreactivity and allergenicity in processed food. Czech J. Food Sci., 30: 211-219.The immunoreactivity and allergenicity of proteins present in processed food (UHT milk, yoghurt, hard cheese, cottage cheese, biscuit, and sausage intended for children) were determined in this study. Proteins were characterised by SDS-PAGE electrophoresis. The changes in immunoreactivity were compared by enzyme-linked immunosorbent assay (ELISA) using polyclonal rabbit antibodies specific to α-lactalbumin (α-la), β-lactoglobulin (β-lg), α-, β-, and κ-casein. The allergenicity was determined with human pooled sera from CMA allergic patients by ELISA and immunoblot. The results have shown that the allergenicity of the food products is mainly correlated with bovine serum albumin (BSA), lactofferin (LF), and α-casein or the products of non-specific reactions between carbohydrate and proteins (e.g. lactosylation).

show abstract

Effect of heat treatment on the antigenicity of bovine α-lactalbumin and β-lactoglobulin in whey protein isolate

Cited by 115 publications

References 22 publications

Effects of saccharide on the structure and antigenicity of β-conglycinin in soybean protein isolate by glycation

Effects of saccharide on the structure and antigenicity of β-conglycinin in soybean protein isolate by glycation

Emerging trends in nutraceutical applications of whey protein and its derivatives

Cow's milk proteins immunoreactivity and allergenicity in processed food

Contact Info

Product

Resources

About