Boundary layer phenomena during ultrafiltration of dextran and whey protein solutions

Desalination ◽  
1984 ◽  
Vol 51 (1) ◽  
pp. 61-77 ◽  
Author(s):  
G. Jonsson
2014 ◽  
Vol 32 (No. 1) ◽  
pp. 82-89 ◽  
Author(s):  
M. Tomczyńska-Mleko ◽  
E. Kamysz ◽  
E. Sikorska ◽  
C. Puchalski ◽  
S. Mleko ◽  
...  

The secondary structure of proteins in unheated and heated whey protein isolate dispersions and the surface tension of the solutions were investigated at different pH. Heating protein solutions at 80°C results in an increase of unordered structure. Nevertheless, the difference between the contents of unordered structure in the unheated and heated samples increases with increasing pH of the solution. At low protein concentrations the surface tension decreased with increasing protein concentration to about 5 mg/ml. For the heated solution, a similar trend was observed in the decrease in the surface tension with increasing concentrations of protein. In both cases, the curves depicting the surface tension as a function of protein concentration could be fitted to the exponential function with a negative exponent, but with the heated solutions lower values of surface tension were observed. Studies on the surface tension of whey protein isolate solutions prove that the unfolding of whey proteins, revealed by changes in the secondary structure, causes a decrease in the surface tension.


2012 ◽  
Vol 51 (9) ◽  
pp. 2113-2119 ◽  
Author(s):  
Mahboubeh Sadeghi ◽  
Ashkan Madadlou ◽  
Asghar Khosrowshahi ◽  
Mohammadamin Mohammadifar

1996 ◽  
Vol 63 (2) ◽  
pp. 315-320 ◽  
Author(s):  
Mohammad R. Alizadehfard ◽  
Dianne E. Wiley

Foods ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 259
Author(s):  
Luisa A. Scudeller ◽  
Pascal Blanpain-Avet ◽  
Thierry Six ◽  
Séverine Bellayer ◽  
Maude Jimenez ◽  
...  

Fouling of plate heat exchangers (PHEs) is a recurring problem when pasteurizing whey protein solutions. As Ca2+ is involved in denaturation/aggregation mechanisms of whey proteins, the use of calcium chelators seems to be a way to reduce the fouling of PHEs. Unfortunately, in depth studies investigating the changes of the whey protein fouling mechanism in the presence of calcium chelators are scarce. To improve our knowledge, reconstituted whey protein isolate (WPI) solutions were prepared with increasing amounts of phosphate, expressed in phosphorus (P). The fouling experiments were performed on a pilot-scale PHE, while monitoring the evolution of the pressure drop and heat transfer coefficient. The final deposit mass distribution and structure of the fouling layers were investigated, as well as the whey protein denaturation kinetics. Results suggest the existence of two different fouling mechanisms taking place, depending on the added P concentration in WPI solutions. For added P concentrations lower or equal to 20 mg/L, a spongy fouling layer consists of unfolded protein strands bound by available Ca2+. When the added P concentration is higher than 20 mg/L, a heterogeneously distributed fouling layer formed of calcium phosphate clusters covered by proteins in an arborescence structure is observed.


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