Method for the isolation of bovine β-lactoglobulin from a cheese whey protein fraction and physicochemical characterization of the purified product

1997 ◽  
Vol 7 (4) ◽  
pp. 229-235 ◽  
Author(s):  
Petra W.J.R. Caessens ◽  
Servaas Visser ◽  
Harry Gruppen
2009 ◽  
Vol 4 (5) ◽  
pp. 797-808 ◽  
Author(s):  
Abigail Santillán-Moreno ◽  
Fernando Martínez-Bustos ◽  
Eduardo Castaño-Tostado ◽  
Silvia L. Amaya-Llano

2017 ◽  
Vol 104 ◽  
pp. 133-143 ◽  
Author(s):  
Maria C. Capellini ◽  
Vanessa Giacomini ◽  
Maitê S. Cuevas ◽  
Christianne E.C. Rodrigues

2006 ◽  
Vol 05 (06) ◽  
pp. 959-966 ◽  
Author(s):  
LI-JUN YIN ◽  
MASAYOSHI SAITO ◽  
ISAO KOBAYASHI ◽  
MITSUTOSHI NAKAJIMA

We investigated the preparation and characterization of protein-stabilized emulsions by microchannel (MC) emulsification. BSA, β-lactoglobulin, γ-globulin, lysozyme, soybean flour, whey protein, and egg white protein were used as emulsifiers. Stable monodispersed emulsions were prepared using BSA, β-lactoglobulin, soybean flour, and whey protein, whose particle sizes ranged from 41.0 to 44.1 μm, and whose coefficients of variation were less than 6.5%. Monodispersed emulsions could not be prepared using γ-globulin, lysozyme, and egg white protein as emulsifiers. The particle became significantly bigger and its monodispersity decreased with the increase of the dispersed-phase flux, but monodispersed emulsion was successfully prepared even when the dispersed-phase flux was increased to 30 L/(m2h). Particle formation behaviors were closely related to protein solution properties, such as interfacial tension and contact angle on a silicon plate, pH and the ionic strength of protein solution.


2015 ◽  
Vol 24 (4) ◽  
pp. 1335-1340 ◽  
Author(s):  
Renda Kankanamge ◽  
Chaturika Jeewanthi ◽  
Na-Kyoung Lee ◽  
Si-Kyung Lee ◽  
Yoh Chang Yoon ◽  
...  

1980 ◽  
Vol 47 (3) ◽  
pp. 337-342 ◽  
Author(s):  
Thomas G. Parker ◽  
David S. Horne

SUMMARYThe turbidity increase on storage of milk dialysate was shown to be due to Ca phosphate precipitation. The rate of precipitation at 40 °C could be decreased by shortening the duration of dialysis or by the addition of small amounts of EDTA. The dialysate was stabilized against Ca phosphate precipitation by the addition of the whey protein fraction of milk. Individual whey proteins varied in their stabilizing ability: α-lactalbumin was found to be more effective than β-lactoglobulin which gave approximately the same effect as an immunoglobulin fraction. BSA and lysozyme had a destabilizing effect and ovalbumin possessed a slight stabilizing ability.


LWT ◽  
2016 ◽  
Vol 72 ◽  
pp. 285-291 ◽  
Author(s):  
M. Soazo ◽  
L.M. Pérez ◽  
G.N. Piccirilli ◽  
N.J. Delorenzi ◽  
R.A. Verdini

1999 ◽  
Vol 66 (2) ◽  
pp. 225-236 ◽  
Author(s):  
GENEVIEVE GÉSAN-GUIZIOU ◽  
GEORGES DAUFIN ◽  
MARTIN TIMMER ◽  
DURITA ALLERSMA ◽  
CAROLINE VAN DER HORST

Fractions enriched with α-lactalbumin (α-la) and β-lactoglobulin (β-lg) were produced by a process comprising the following successive steps: clarification–defatting of whey protein concentrate, precipitation of α-lactalbumin, separation of soluble β-lactoglobulin, washing the precipitate, solubilization of the precipitate, concentration and purification of α-la. The present study evaluated the performance of the process, firstly on a laboratory scale with acid whey and then on a pilot scale with Gouda cheese whey. In both cases soluble β-lg was separated from the precipitate using diafiltration or microfiltration and the purities of α-la and β-lg were in the range 52–83 and 85–94% respectively. The purity of the β-lg fraction was higher using acid whey, which does not contain caseinomacropeptide, than using sweet whey. With the pilot scale plant, the recoveries (6% for α-la; 51% for β-lg) were disappointing, but ways of improving each step in the process are discussed.


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