Whey protein interactions in acidic cold-set gels at different pH values

2007 ◽  
Vol 87 (6) ◽  
pp. 535-554 ◽  
Author(s):  
Angelo Luiz Fazani Cavallieri ◽  
Antonio Paulino Costa-Netto ◽  
Marcelo Menossi ◽  
Rosiane Lopes Da Cunha
Keyword(s):  
Whey Protein ◽  
Protein Interactions ◽  
Ph Values

Oscillatory rheological study of the effects of pH and salts on gel development in heated whey protein concentrate solutions

1995 ◽  
Vol 62 (3) ◽  
pp. 469-477 ◽  
Author(s):  
Qingnong Tang ◽  
Owen J. McCarthy ◽  
Peter A. Munro
Keyword(s):  
Ionic Strength ◽  
Whey Protein ◽  
Protein Interactions ◽  
Salt Concentration ◽  
Food System ◽  
Whey Proteins ◽  
Whey Protein Concentrate ◽  
Protein Concentrate ◽  
Ph Values ◽  
Effects Of Ph

SummaryThe effects of pH and added NaCl or CaCl2 on gel development in heated whey protein concentrate (WPC) solutions were studied by oscillatory rheometry using a Bohlin rheometer, and by qualitative visual and tactile observations. The storage modulus (G′) exhibited maxima at pH values of about 4 and 7, while the phase angle (δ) exhibited minima at the same pH values. At pH 5·5, which lies within the range of the isoelectric points of the whey proteins, G′ was a minimum while δ was a maximum. At pH 7 and 8 G′ increased to a maximum and then decreased as added ionic strength was increased. At pH 4 G′ decreased steadily but slowly with increasing added ionic strength. The effects of CaCl2 were essentially the same as those of NaCl, but occurred at much lower added ionic strength. All the results are discussed in physicochemical terms. The main conclusions were, firstly, that changes in pH and salt concentration both affected gel development by altering the balance between attractive and repulsive protein-protein interactions, and secondly, that the effects of pH, salt concentration and salt type were interactive. Interaction both partly explains the wide variation in gel character and rheological properties among commercial WPC and potentially provides means of tailoring the gelling behaviour of a WPC so that it functions in a desired way in a given food system.

Quantification of heat-induced casein–whey protein interactions in milk and its relation to gelation kinetics

2003 ◽  
Vol 31 (1-4) ◽  
pp. 115-123 ◽  
Author(s):  
Astrid J Vasbinder ◽  
Arno C Alting ◽  
Kees G de Kruif
Keyword(s):  
Whey Protein ◽  
Protein Interactions ◽  
Gelation Kinetics

scholarly journals Effect of casein to whey protein ratios on the protein interactions and coagulation properties of low-fat yogurt

2016 ◽  
Vol 99 (10) ◽  
pp. 7768-7775 ◽  
Author(s):  
L.L. Zhao ◽  
X.L. Wang ◽  
Q. Tian ◽  
X.Y. Mao
Keyword(s):  
Whey Protein ◽  
Protein Interactions ◽  
Low Fat

Heat stability of milk: pH-dependent dissociation of micellar κ-casein on heating milk at ultra high temperatures

1985 ◽  
Vol 52 (4) ◽  
pp. 529-538 ◽  
Author(s):  
Harjinder Singh ◽  
Partick F. Fox
Keyword(s):  
Whey Protein ◽  
Whey Proteins ◽  
Heat Stability ◽  
Casein Micelle ◽  
Casein Micelles ◽  
Ph Profile ◽  
Ph Values ◽  
Maximum Stability ◽  
Β Lactoglobulin ◽  
Maximum Minimum

SUMMARYPreheating milk at 140 °C for 1 min at pH 6·6, 6·8, 7·0 or 7·2 shifted the heat coagulation time (HCT)/pH profile to acidic values without significantly affecting the maximum stability. Whey proteins (both β-lactoglobulin and α-lactalbumin) co-sedimented with the casein micelles after heating milk at pH < 6·9 and the whey protein-coated micelles, dispersed in milk ultrafiltrate, showed characteristic maxima–minima in their HCT/pH profile. Heating milk at higher pH values (> 6·9) resulted in the dissociation of whey proteins and κ-casein-rich protein from the micelles and the residual micelles were unstable, without a maximum–minimum in the HCT/pH profile. Preformed whey protein–casein micelle complexes formed by preheating (140 °C for 1 min) milk at pH 6·7 dissociated from the micelles on reheating (140 °C for 1 min) at pH > 6·9. The dissociation of micellar-κ-casein, perhaps complexed with whey proteins, may reduce the micellar zeta potential at pH ≃ 6·9 sufficiently to cause a minimum in the HCT/pH profile of milk.

The use of high hydrostatic pressure to modulate milk protein interactions for the production of an alpha-lactalbumin enriched-fraction

2018 ◽  
Vol 20 (2) ◽  
pp. 515-524 ◽  
Author(s):  
Alice Marciniak ◽  
Shyam Suwal ◽  
Michel Britten ◽  
Yves Pouliot ◽  
Alain Doyen
Keyword(s):  
Hydrostatic Pressure ◽  
Whey Protein ◽  
Protein Interactions ◽  
High Hydrostatic Pressure ◽  
Milk Protein ◽  
Protein Solution ◽  
Green Method ◽  
Alpha Lactalbumin

An innovative and green method for the fractionation of α-lactalbumin with 86% purity from whey protein solution was developed using high hydrostatic pressure as a pretreatment.

The cheesemaking potential of milk concentrated up to four-fold by ultrafiltration and heated in the range 90–97 °C

1990 ◽  
Vol 57 (4) ◽  
pp. 549-557 ◽  
Author(s):  
Margaret L. Green
Keyword(s):  
Electron Microscopy ◽  
Heat Treatment ◽  
Whey Protein ◽  
Protein Interactions ◽  
Heat Denaturation ◽  
The Difference

SummaryProperties of interest to cheesemaking were investigated with milks concentrated by ultrafiltration and heated at 90 °C or 95–97 °C for 15 s. The effects of light homogenization before concentration and of addition of CaCl2 after heating were assessed. No changes in casein–fat or casein–whey protein interactions were detected by electron microscopy. The heat denaturation of whey protein increased linearly as the milk became more concentrated. Coagulability by rennet after heat treatment increased with concentration to close to the unheated value in 3·5 to 4-fold concentrates. The decrease in curd firming rate by heat treatment was slightly affected by concentration and addition of CaCl2 restored some of the difference. Heat treatment reduced the rate of whey loss and slightly improved the curd structure but did not affect fat losses. Light homogenization slightly reduced heat denaturation of whey protein and whey loss.

scholarly journals Effects of pH Values on Physicochemical Properties and Antioxidant Potential of Whey Protein Isolate-safflower Yellow Complexes

2018 ◽  
Vol 24 (3) ◽  
pp. 475-484 ◽  
Author(s):  
Xueyan Li ◽  
Zengli Gao ◽  
Tong Li ◽  
Shuvan-Kumar Sarker ◽  
Sathi Chowdhury ◽  
...  
Keyword(s):  
Physicochemical Properties ◽  
Whey Protein ◽  
Whey Protein Isolate ◽  
Protein Isolate ◽  
Antioxidant Potential ◽  
Ph Values ◽  
Effects Of Ph

The Effects of Grass Carp Skin Gelatin and Whey Protein Interactions on Rheological and Textural Properties and Nanostructure

2017 ◽  
Vol 26 (7) ◽  
pp. 790-800
Author(s):  
Luyun Cai ◽  
Liping Leng ◽  
Jianrong Li ◽  
Xiaoqiang Chen ◽  
Joe M. Regenstein ◽  
...  
Keyword(s):  
Whey Protein ◽  
Protein Interactions ◽  
Grass Carp ◽  
Textural Properties

Effect of pH on heat-induced casein-whey protein interactions: A comparison between caprine milk and bovine milk

2014 ◽  
Vol 39 (1) ◽  
pp. 178-183 ◽  
Author(s):  
Mirjana B. Pesic ◽  
Miroljub B. Barac ◽  
Sladjana P. Stanojevic ◽  
Miroslav M. Vrvic
Keyword(s):  
Whey Protein ◽  
Protein Interactions ◽  
Bovine Milk ◽  
Effect Of Ph ◽  
Caprine Milk
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