High pressure thermal denaturation kinetics of whey proteins

2004 ◽  
Vol 71 (4) ◽  
pp. 480-488 ◽  
Author(s):  
Jörg Hinrichs ◽  
Britta Rademacher

Pressure processing of foodstuff has been applied to produce or modify proteinaceous gel structures. In real pressure processing the treatment is non-isothermal, due to the adiabatic nature of the process and the heat loss from the product to the vessel. In order to estimate the effect of pressurization on milk constituents pressure and temperature dependent kinetics were determined separately from each other. In a detailed kinetic study whey protein isolate was treated under isobaric (200 to 800 MPa) and isothermal conditions (−2 to 70 °C), and the resulting degree of denaturation of β-lactoglobulin A and B and α-lactalbumin was analysed. Kinetic parameters of denaturation were estimated using a one step non-linear regression method which allowed a global fit of the whole data set. The isobaric isothermal denaturation of β-lactoglobulin and α-lactalbumin was found to follow third and second order kinetics, respectively. Isothermal pressure denaturation of both β-lactoglobulin fractions do not differ significantly and were characterized by an activation volume decreasing with increasing temperature from −10 to about −30 ml mol−1, which demonstrates that the denaturation rate is accelerated with increasing temperature. The activation energy of about 70 to 100 kJ mol−1 obtained for β-lactoglobulin A and B is not dependent to a great extent on the pressure which indicates that above 200 MPa denaturation rate is limited by the aggregation rate while pressure forces unfolding of the molecule.

2001 ◽  
Vol 68 (1) ◽  
pp. 95-107 ◽  
Author(s):  
WENDIE L. CLAEYS ◽  
LINDA R. LUDIKHUYZE ◽  
ANN M. VAN LOEY ◽  
MARC E. HENDRICKX

A detailed kinetic study of alkaline phosphatase, lactoperoxidase and β-lactoglobulin was carried out in the context of identifying intrinsic time–temperature indicators for controlling the heat processing of milk. The heat inactivation or denaturation of alkaline phosphatase, lactoperoxidase and β-lactoglobulin under isothermal conditions was found to follow first order kinetics. Experimental results were analysed using both a two step linear regression and a one step non-linear regression method. Results obtained using the two statistical techniques were comparable, but the 95% confidence interval for the predicted values was smaller when the one step non-linear regression method was used, indicating its superiority for estimating kinetic parameters. Thermal inactivation of alkaline phosphatase and lactoperoxidase was characterized by z values of 5·3 deg C (D60 °C = 24·6 min) and 4·3 deg C (D71 °C = 38·6 min) respectively. For the denaturation of β-lactoglobulin we found z values of 7·9 deg C (D75 °C = 49·9 min) in the temperature range 70–80 °C and 24·2 deg C (D85 °C = 3·53 min) in the range 83-95 °C. Dref and z were evaluated under dynamic temperature conditions. To estimate the statistical accuracy of the parameters, 90% joint confidence regions were constructed.


2020 ◽  
Vol 21 (8) ◽  
pp. 2792
Author(s):  
Claudie Aspirault ◽  
Alain Doyen ◽  
Laurent Bazinet

Separation of α-lactalbumin and β-lactoglobulin improves their respective nutritional and functional properties. One strategy to improve their fractionation is to modify their pH and ionic strength to induce the selective aggregation and precipitation of one of the proteins of interest. Electrodialysis with bipolar membrane (EDBM) is a green process that simultaneously provides acidification and demineralization of a solution without adding any chemical compounds. This research presents the impact on whey proteins separation of different preheating temperatures (20, 50, 55 and 60 °C) combined with EDBM or chemical acidification of 10% whey protein isolate solutions. A β-lactoglobulin fraction at 81.8% purity was obtained in the precipitate after EDBM acidification and preheated at 60 °C, representing a recovery yield of 35.8%. In comparison, chemical acidification combined with a 60 °C preheating treatment provides a β-lactoglobulin fraction at 70.9% purity with a 11.6% recovery yield. The combination of EDBM acidification with a preheating treatment at 60 °C led to a better separation of the main whey proteins than chemical acidification.


2014 ◽  
Vol 898 ◽  
pp. 326-329
Author(s):  
Li Fu ◽  
Xi Qing Yue ◽  
Jian Xin Song

First of all, whey protein concentrat was added to milk adjusting the proportion of casein and whey proteins to 40:60. And then milk was hydrolyzed by trypsin and flavourzyme (TF) single respectively in one-step process or staged in two-step process. The Antigen contents of α-lactalbumin (α-LA) and β-lactoglobulin (β-LG) during the hydrolysis process were determined by indirect competitive enzyme-linked immunosorbent assay (ELISA) methods. The result showed that the most significant antigen reduction was observed in two-step hydrolysis process compared with one-step hydrolysis process


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.


2019 ◽  
Vol 86 (1) ◽  
pp. 114-119
Author(s):  
Katarina Lisak Jakopović ◽  
Seronei Chelulei Cheison ◽  
Ulrich Kulozik ◽  
Rajka Božanić

AbstractThe experiments reported in this research paper examine the potential of digestion using acidic enzymes Protease A and Protease M to selectively hydrolyse α-lactalbumin (α-La) whilst leaving β-lactoglobulin (β-Lg) relatively intact. Both enzymes were compared with pepsin hydrolysis since its selectivity to different whey proteins is known. Analysis of the hydrolysis environment showed that the pH and temperature play a significant role in determining the best conditions for achievement of hydrolysis, irrespective of which enzyme was used. Whey protein isolate (WPI) was hydrolysed using pepsin, Acid Protease A and Protease M by randomized hydrolysis conditions. Reversed-phase high performance liquid chromatography was used to analyse residual proteins. Regarding enzyme selectivity under various milieu conditions, all three enzymes showed similarities in the reaction progress and their potential for β-Lg isolation.


2005 ◽  
Vol 72 (3) ◽  
pp. 369-378 ◽  
Author(s):  
David J Oldfield ◽  
Harjinder Singh ◽  
Mike W Taylor

Microfiltration and ultrafiltration were used to manufacture skim milks with an increased or reduced concentration of whey proteins, while keeping the casein and milk salts concentrations constant. The skim milks were heated on a pilot-scale UHT plant at 80, 90 and 120 °C. The heat-induced denaturation and aggregation of β-lactoglobulin (β-lg), α-lactalbumin (α-la) and bovine serum albumin (BSA) were quantified by polyacrylamide gel electrophoresis. Apparent rate constants and reaction orders were calculated for β-lg, α-la and BSA denaturation. Rates of β-lg, α-la and BSA denaturation increased with increasing whey protein concentration. The rate of α-la and BSA denaturation was affected to a greater extent than β-lg by the change in whey protein concentration. After heating at 120 °C for 160 s, the concentration of β-lg and α-la associated with the casein micelles increased as the initial concentration of whey proteins increased.


2013 ◽  
Vol 31 (13-14) ◽  
pp. 1532-1544 ◽  
Author(s):  
M. Amdadul Haque ◽  
Aditya Putranto ◽  
Peter Aldred ◽  
Jie Chen ◽  
Benu Adhikari

Sign in / Sign up

Export Citation Format

Share Document