Effect of processing on conformational changes of food proteins related to allergenicity

T Rahaman, T Vasiljevic, L Ramchandran - Trends in Food Science & …, 2016 - Elsevier
Background Food allergy is one of the major health concerns worldwide that has been
increasing at an alarming rate in recent times. Foods undergo various processing steps …

Transforming insect biomass into consumer wellness foods: A review

D Sun-Waterhouse, GIN Waterhouse, L You… - Food Research …, 2016 - Elsevier
Potential food shortages, human health challenges and environmental concerns, all
thematically linked to growing and aging global populations, drive the search for alternative …

Food allergy

SK Sathe, C Liu, VD Zaffran - Annual review of food science and …, 2016 - annualreviews.org
Food allergy is receiving increased attention in recent years. Because there is currently no
known cure for food allergy, avoiding the offending food is the best defense for sensitive …

Conjugation of polyphenols prevents lactoferrin from thermal aggregation at neutral pH

F Liu, D Wang, C Ma, Y Gao - Food Hydrocolloids, 2016 - Elsevier
Because of the aggregation and/or gelation of lactoferrin (LF) occurred during thermal
treatment, its application is limited in food products. The present study was focused on the …

Proteomic study on the stability of proteins in bovine, camel, and caprine milk sera after processing

L Zhang, S Boeren, M Smits, T van Hooijdonk… - Food Research …, 2016 - Elsevier
Milk proteins have been shown to be very sensitive to processing. This study aims to
investigate the changes of the bovine, camel, and caprine milk proteins after freezing …

Impact of α-lactalbumin: β-lactoglobulin ratio on the heat stability of model infant milk formula protein systems

SV Crowley, AP Dowling, V Caldeo, AL Kelly… - Food chemistry, 2016 - Elsevier
Abstract Model infant milk formula systems (5.5% protein) were formulated to contain α-
lactalbumin: β-lactoglobulin ratios of 0.1, 0.5, 1.3, 2.1 or 4.6 and assessed for heat stability …

Glycation of β-lactoglobulin under dynamic high pressure microfluidization treatment: Effects on IgE-binding capacity and conformation

Y Chen, Z Tu, H Wang, L Zhang, X Sha, J Pang… - Food research …, 2016 - Elsevier
The effects of dynamic high-pressure microfluidization (DHPM)(80, 120, and 160 MPa)
treatment and glycation with galactose on the IgE-binding capacity and conformation of β …

[HTML][HTML] The decrease in the IgG-binding capacity of intensively dry heated whey proteins is associated with intense Maillard reaction, structural changes of the …

F Liu, M Teodorowicz, MAJS van Boekel, HJ Wichers… - Food & function, 2016 - pubs.rsc.org
Heat treatment is the most common way of milk processing, inducing structural changes as
well as chemical modifications in milk proteins. These modifications influence the immune …

Effects of heat treatment on the antigenicity of four milk proteins in milk protein concentrates

Q Xu, J Shi, M Yao, M Jiang, Y Luo - Food and agricultural …, 2016 - Taylor & Francis
The effects of heat treatment on the antigenicity and potential allergenicity of α-Lactalbumin
(α-LA), β-Lactoglobulin (β-LG), α-casein (α-CN), and β-casein (β-CN) in milk protein …

Effect of pulsed light on structure and immunoreactivity of gluten

A Panozzo, L Manzocco, G Lippe, MC Nicoli - Food Chemistry, 2016 - Elsevier
The effect of pulsed light (from 1.75 to 26.25 J cm− 2) on selected properties of wheat gluten
powder and aqueous suspension (absorbance, particle size and microstructure, free …