Milk protein–gum tragacanth mixed gels: Effect of heat-treatment sequence

2014 ◽  
Vol 101 ◽  
pp. 1068-1073 ◽  
Author(s):  
Masoud Hatami ◽  
Mohammad Nejatian ◽  
Mohammad Amin Mohammadifar ◽  
Hanieh Pourmand
2018 ◽  
Vol 85 ◽  
pp. 299-310 ◽  
Author(s):  
An Thi-Binh Nguyen ◽  
Michaël Nigen ◽  
Luciana Jimenez ◽  
Hassina Ait-Abderahim ◽  
Charles Cunault ◽  
...  

2001 ◽  
Vol 68 (3) ◽  
pp. 471-481 ◽  
Author(s):  
CATHERINE SCHORSCH ◽  
DEBORAH K. WILKINS ◽  
MALCOLM G. JONES ◽  
IAN T. NORTON

The aim of the present work was to investigate the role of whey protein denaturation on the acid induced gelation of casein. This was studied by determining the effect of whey protein denaturation both in the presence and absence of casein micelles. The study showed that milk gelation kinetics and gel properties are greatly influenced by the heat treatment sequence. When the whey proteins are denatured separately and subsequently added to casein micelles, acid-induced gelation occurs more rapidly and leads to gels with a more particulated microstructure than gels made from co-heated systems. The gels resulting from heat-treatment of a mixture of pre-denatured whey protein with casein micelles are heterogeneous in nature due to particulates formed from casein micelles which are complexed with denatured whey proteins and also from separate whey protein aggregates. Whey proteins thus offer an opportunity not only to control casein gelation but also to control the level of syneresis, which can occur.


Foods ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 1836
Author(s):  
Hannah E. Zenker ◽  
Malgorzata Teodorowicz ◽  
Harry J. Wichers ◽  
Kasper A. Hettinga

For the determination of the binding of heated cow’s milk whey proteins such as β-lactoglobulin to the receptors expressed on immune cells, inhibition ELISA with the soluble form of the receptor for advanced glycation end products (sRAGE) and scavenger receptor class B (CD36) has been successfully used in the past. However, binding to heated and glycated caseins in this read-out system has not been tested. In this study, inhibition ELISA was applied to measure the binding of cow’s milk casein alone, as well as all milk proteins together, which underwent differential heat treatment, to sRAGE and CD36, and we compared those results to a dot blot read out. Moreover, binding to sRAGE and CD36 of differentially heated milk protein was measured before and after in vitro digestion. Casein showed binding to sRAGE and CD36, independent from the heat treatment, in ELISA, while the dot blot showed only binding to high-temperature-heated milk protein, indicating that the binding is not related to processing but to the physicochemical characteristics of the casein. This binding decreased after passage of casein through the intestinal phase.


2019 ◽  
Vol 56 (3) ◽  
pp. 1462-1472 ◽  
Author(s):  
Ashwajit Tejram Patil ◽  
Ganga Sahay Meena ◽  
Neelam Upadhyay ◽  
Yogesh Khetra ◽  
Sanket Girdharbhai Borad ◽  
...  

1970 ◽  
Vol 33 (9) ◽  
pp. 377-379 ◽  
Author(s):  
W. L. Wendorff ◽  
C. H. Amundson ◽  
N. F. Olson

Heat treated, condensed skimmilk and nonfat dry milk (NDM) were treated with lactase enzyme obtained from Saccharomyces fragilis. The effect of heat treatment on lactose hydrolysis was determined. Forewarming treatments of 62.8, 68.3, 73.9, 79.5, and 85.0 C resulted in 17, 17, 100, 59, and 156 g, respectively, of lactose hydrolyzed. Concentrates with forewarming treatments of 62.8, 73.9, and 85.0 C for 30 min were given additional heat treatments of 62.8, 73.9, or 85.0 C for 20 min. Activity was lower in all concentrates given the double heat treatment, except those heated at 85.0 C for 20 min after forewarming at 62.8 and 73.9 C. These showed a substantial increase in lactose hydrolysis. Portions of each concentrate, spray dried and reconstituted to 30% total solids, exhibited the same effect on lactose hydrolysis as the original concentrates. Additional studies were conducted with whey and a 5% lactose plus milk salt solution. Results indicated that heating lactose in the presence of milk protein had a great effect on lactose hydrolysis.


1987 ◽  
Vol 54 (2) ◽  
pp. 207-218 ◽  
Author(s):  
Geoffrey R. Andrews ◽  
S. Krishna Prasad

SummaryMilk ultrafiltrate and milks of varying protein, citrate and phosphate concentrations were heated in sealed containers. Protein was found not to be involved in the mechanism of formation of lactulose, but increasing the protein content of milk reduced the concentration of lactulose after heating. This was considered to be due to increased condensation of lactose and lactulose with amino groups of the protein, Less lactulose was formed in milk ultrafiltrate than in skimmed milk accorded the same heat treatment, which was attributed to the buffering capacity of the milk protein in skimmed milk. Activation energies for lactulose formation in skimmed milk and in ultrafiltrate were 128 and 131 kJ/mol respectively. Citrate and phosphate catalysed the formation of lactulose. It is proposed that the formation of free lactulose in heated milk and ultrafiltrate proceeds exclusively by the Lobry de Bruyn-Alberda van Ekenstein transformation with the naturally occurring phosphate and citrate acting as base catalysts.


2017 ◽  
Vol 37 (1) ◽  
pp. 44-51 ◽  
Author(s):  
Fang Qian ◽  
Jiayue Sun ◽  
Di Cao ◽  
Yanfeng Tuo ◽  
Shujuan Jiang ◽  
...  

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