Interfacial Shear Rheology of Aged and Heat-Treated β-Lactoglobulin Films:  Displacement by Nonionic Surfactant

2000 ◽  
Vol 48 (5) ◽  
pp. 1491-1497 ◽  
Author(s):  
Stéphane Roth ◽  
Brent S. Murray ◽  
Eric Dickinson
Langmuir ◽  
2010 ◽  
Vol 26 (19) ◽  
pp. 15366-15375 ◽  
Author(s):  
Jin-Mi Jung ◽  
Deniz Zeynel Gunes ◽  
Raffaele Mezzenga

2018 ◽  
Vol 62 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Yu-Jiun Lin ◽  
Sourav Barman ◽  
Peng He ◽  
Zhuqing Zhang ◽  
Gordon F. Christopher ◽  
...  

1986 ◽  
Vol 53 (4) ◽  
pp. 601-613 ◽  
Author(s):  
Mary B. Grufferty ◽  
Patrick F. Fox

SummaryThe report that addition of KI03 (0·1 mm) to milk before ultra high temperature (UHT) treatment induces extensive proteolysis during subsequent storage at 37 °C was confirmed. None was produced by addition of H202 KMn04 or K2Cr207. The pH optimum for KI03-induced proteolysis was between 7·0 and 8·0 and the temperature optimum 37—45 °C. β-Casein was particularly susceptible and the proteolysis pattern was similar to that caused by indigenous alkaline milk proteinase (MPA, plasmin). Addition of plasmin to milk before UHT treatment (140 °C/10 s) caused slight proteolysis during subsequent storage but addition of 0·1 mm-KI03 and plasmin caused extensive proteolysis which was prevented by addition of soyabean trypsin inhibitor, indicating the probable involvement of plasmin in KI03-induced proteolysis in UHT-treated milk. Equally extensive proteolysis occurred in serum protein-free casein micelle systems (SPFCM), with or without KI03, during storage at 37 °C following UHT treatment, indicating a role for whey proteins in KI03-induced proteolysis. Addition of β-lactoglobulin (β-lg) to a SPFCM system inhibited proteolysis, but extensive proteolysis occurred in a SPFCM system containing both β-lg and KI03. MPA-free Na caseinate (prepared by heating at 140 °C for 7 min) underwent extensive proteolysis when treated with plasmin before UHT treatment; proteolysis was inhibited by addition of °-lg to this system and KI03 reversed the inhibitory effect of β-lg. Plasmin proteolysis of isolated αs1-casein was inhibited by denatured β-lg (90 °C/30 min) at a level of 4 mg/ml but not by native β-lg. When denatured in the presence of KI03, β-lg had a lower free SH content than the control and was less inhibitory for plasmin in proteolysis of isolated αsl-casein. The results show that denatured β-lg inhibits plasmin proteolysis of caseins in UHT milk and that inhibition is prevented by KI03. This inhibition may occur via thiol–disulphide interchange, which is prevented if the SH group of ²-lg is oxidized by KI03, thus permitting the stimulatory effect of KI03 on proteolysis in UHT-treated milk.


Soft Matter ◽  
2014 ◽  
Vol 10 (1) ◽  
pp. 175-186 ◽  
Author(s):  
Eline Hermans ◽  
Jan Vermant

1994 ◽  
Vol 3 (5) ◽  
pp. 473-479
Author(s):  
Tuomo Tupasela ◽  
Heikki Koskinen ◽  
Pirkko Antila

Whey is a by-product of cheesemaking. Whey dry matter contains mainly lactose, but also valuable whey proteins. The aim of this study was to develop improvements to whey protein membrane isolation processes. In our trials CaCl2 -added, pH-adjusted and heat-treated wheys were found to have MF (microfiltration) permeate fluxes about 30% higher than in untreated MF whey. The total solids and protein content of the MF permeates decreased compared to the original wheys. UF (ultrafiltration) trials were conducted using MF whey to compare it with centrifugally separated whey. The MF whey consistently maintained an UF flux about 1.5 to 2.5 times higher than that of the separated whey. Differently treated MF whey UF permeate fluxes also showed a difference. With CaCl2 addition, pH adjustment and heat treatment, the UF permeate fluxes were about 20 to 40% higher than when only MF was used. The total solids content decreased in each trial. The protein content of the UF concentrate also decreased compared to the MF permeate. The (β-lg (β-lactoglobulin) and α-la (α-lactalbumin) content was almost the same in UF concentrates as in MF permeates.


2010 ◽  
Vol 15 (4) ◽  
pp. 246-255 ◽  
Author(s):  
Jürgen Krägel ◽  
Svetlana R. Derkatch

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