Process steps for the preparation of purified fractions of α-lactalbumin and β-lactoglobulin from whey protein concentrates

1999 ◽  
Vol 66 (2) ◽  
pp. 225-236 ◽  
Author(s):  
GENEVIEVE GÉSAN-GUIZIOU ◽  
GEORGES DAUFIN ◽  
MARTIN TIMMER ◽  
DURITA ALLERSMA ◽  
CAROLINE VAN DER HORST
Keyword(s):  
Whey Protein ◽  
Cheese Whey ◽  
Pilot Scale ◽  
Whey Protein Concentrate ◽  
Protein Concentrate ◽  
Whey Protein Concentrates ◽  
Sweet Whey ◽  
Acid Whey ◽  
Gouda Cheese ◽  
Β Lactoglobulin

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.

Functional properties of native and cheese whey protein concentrate powders

2007 ◽  
Vol 60 (4) ◽  
pp. 277-285 ◽  
Author(s):  
ANTTI T HEINO ◽  
JANNE O UUSI-RAUVA ◽  
PIRJO R RANTAMÄKI ◽  
OLLI TOSSAVAINEN
Keyword(s):  
Whey Protein ◽  
Functional Properties ◽  
Cheese Whey ◽  
Whey Protein Concentrate ◽  
Protein Concentrate

Comparison of heat and pressure treatments of skim milk, fortified with whey protein concentrate, for set yogurt preparation: effects on milk proteins and gel structure

2000 ◽  
Vol 67 (3) ◽  
pp. 329-348 ◽  
Author(s):  
ERIC C. NEEDS ◽  
MARTA CAPELLAS ◽  
A. PATRICIA BLAND ◽  
PRETIMA MANOJ ◽  
DOUGLAS MACDOUGAL ◽  
...  
Keyword(s):  
Heat Treatment ◽  
Whey Protein ◽  
Skim Milk ◽  
Milk Proteins ◽  
Whey Protein Concentrate ◽  
Protein Concentrate ◽  
Casein Micelles ◽  
Micelle Structure ◽  
Dynamic Structures ◽  
Β Lactoglobulin

Heat (85 °C for 20 min) and pressure (600 MPa for 15 min) treatments were applied to skim milk fortified by addition of whey protein concentrate. Both treatments caused > 90% denaturation of β-lactoglobulin. During heat treatment this denaturation took place in the presence of intact casein micelles; during pressure treatment it occurred while the micelles were in a highly dissociated state. As a result micelle structure and the distribution of β-lactoglobulin were different in the two milks. Electron microscopy and immunolabelling techniques were used to examine the milks after processing and during their transition to yogurt gels. The disruption of micelles by high pressure caused a significant change in the appearance of the milk which was quantified by measurement of the colour values L*, a* and b*. Heat treatment also affected these characteristics. Casein micelles are dynamic structures, influenced by changes to their environment. This was clearly demonstrated by the transition from the clusters of small irregularly shaped micelle fragments present in cold pressure-treated milk to round, separate and compact micelles formed on warming the milk to 43 °C. The effect of this transition was observed as significant changes in the colour indicators. During yogurt gel formation, further changes in micelle structure, occurring in both pressure and heat-treated samples, resulted in a convergence of colour values. However, the microstructure of the gels and their rheological properties were very different. Pressure-treated milk yogurt had a much higher storage modulus but yielded more readily to large deformation than the heated milk yogurt. These changes in micelle structure during processing and yogurt preparation are discussed in terms of a recently published micelle model.

Antibotulinal Activity of Process Cheese Ingredients

2004 ◽  
Vol 67 (8) ◽  
pp. 1765-1769 ◽  
Author(s):  
KATHLEEN A. GLASS ◽  
ERIC A. JOHNSON
Keyword(s):  
Whey Protein ◽  
Clostridium Botulinum ◽  
Antimicrobial Effect ◽  
Toxin Production ◽  
Whey Protein Concentrate ◽  
Protein Concentrate ◽  
Fat Replacer ◽  
Blue Cheese ◽  
Sweet Whey ◽  
Process Cheese

Ingredients used in the manufacture of reduced-fat process cheese products were screened for their ability to inhibit growth of Clostridium botulinum serotypes A and B in media. Reinforced clostridial medium (RCM) supplemented with 0,0.5, 1, 2, 3, 5, or 10% (wt/vol) of various ingredients, including a carbohydrate-based fat replacer, an enzyme-modified cheese (EMC) derived from a Blue cheese, sweet whey, modified whey protein, or whey protein concentrate, did not inhibit botulinal growth and toxin production when stored at 30°C for 1 week. In contrast, RCM supplemented with 10% soy-based flavor enhancer, 10% Parmesan EMC, or 5 or 10% Cheddar EMC inhibited botulinal toxin production in media for at least 6 weeks of storage at 30°C. Subsequent trials revealed that the antibotulinal effect varied significantly among 13 lots of EMC and that the antimicrobial effect was not correlated with the pH or water activity of the EMC.

Whey Protein Use in Cottage Cheese Dressing

1980 ◽  
Vol 43 (10) ◽  
pp. 752-752
Author(s):  
B. J. DEMOTT ◽  
O. G. SANDERS
Keyword(s):  
Whey Protein ◽  
Xanthan Gum ◽  
Cheese Whey ◽  
Cottage Cheese ◽  
Whey Protein Concentrate ◽  
Protein Concentrate ◽  
Sensory Panel ◽  
Commercial Sample ◽  
Cheese Curd

Cottage cheese whey protein concentrate prepared by heat precipitation and centrifugation was mixed with skimmilk, NaCl and xanthan gum and used as a dressing for cottage cheese curd. The resultant experimental cottage cheese contained more protein than a sample of commercial cottage cheese. The dressed curd particles of the experimental cheese tended to cling together and the flavor was somewhat flat. When evaluated by an 18-member sensory panel, it was given preference scores slightly below the commercial sample.

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