Gelation of Calcium‐Reduced and Lipid‐Reduced Whey Protein Concentrates as Affected by Total and Ionic Mineral Concentrations

Mei, F.-I.; Laye, I.; Karleskind, D.; Morr, C.V.

doi:10.1111/j.1365-2621.1996.tb10898.x

Cited by 7 publications

(3 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This near‐neutral pH promotes intermolecular disulphide interchange giving gels with high rigidity and elasticity. Also, at this pH protein molecules have net negative charges and, thus, protein–protein interactions would be more susceptible to changes in cation concentrations ( Mei et al ., 1996 ).…”

Section: Resultsmentioning

confidence: 99%

Rheological properties of commercial whey protein samples from the MADGELAS survey

Puyol¹,

Pérez²,

Calvo³

1999

Int J of Food Sci Tech

View full text Add to dashboard Cite

Thermally induced gelation of commercial whey protein samples from the Molecular Basis of the Aggregation, Denaturation, Gelation and Surface Activity of Whey Proteins (MADGELAS) survey has been studied in order to develop a current status report on their rheological properties. Solutions of 10% protein (w/v) were prepared in distilled water, 200 mM NaCl or 10 mM CaCl 2 at neutral pH. Small-scale deformation of the samples was measured by dynamic oscillatory rheometry using a Bohlin CS Rheometer. Large-scale deformation at penetration mode was measured using a Texture Analyser (Stable Micro Systems, Surrey, UK). For solutions containing salts, there was a general trend for gel point to decrease and GЈ values to increase, the effect being more marked in the presence of NaCl. Similarly, force values at failure also tended to increase in the presence of salts. Results obtained with samples of similar protein composition dissolved in water were highly scattered, these differences being reduced in the presence of added salts.

show abstract

Section: Resultsmentioning

confidence: 99%

Rheological properties of commercial whey protein samples from the MADGELAS survey

Puyol¹,

Pérez²,

Calvo³

1999

Int J of Food Sci Tech

View full text Add to dashboard Cite

show abstract

“…The production of WPC in North America, Western Europe, and the Pacific Rim is currently 155,000 ton/yr with an approximate value AUD $1.01 billion. A particular function of WPC desired by many food manufacturers for bakery, confectionery, structured meat, and seafood applications is the production of a high-strength gel with good water-holding capacity (Mei, et al, 1996). High gel strength WPC currently on the market are limited and are usually produced from acid wheys obtained after casein precipitation.…”

Section: Introductionmentioning

confidence: 99%

Production of a High Gel Strength Whey Protein Concentrate from Cheese Whey

Veith

Reynolds

2004

Journal of Dairy Science

View full text Add to dashboard Cite

In order to develop a process for the production of a whey protein concentrate (WPC) with high gel strength and water-holding capacity from cheese whey, we analyzed 10 commercially available WPC with different functional properties. Protein composition and modification were analyzed using electrophoresis, HPLC, and mass spectrometry. The analyses of the WPC revealed that the factors closely associated with gel strength and water-holding capacity were solubility and composition of the protein and the ionic environment. To maintain whey protein solubility, it is necessary to minimize heat exposure of the whey during pretreatment and processing. The presence of the caseinomacropeptide (CMP) in the WPC was found to be detrimental to gel strength and water-holding capacity. All of the commercial WPC that produced high-strength gels exhibited ionic compositions that were consistent with acidic processing to remove divalent cations with subsequent neutralization with sodium hydroxide. We have shown that ultrafiltration/diafiltration of cheese whey, adjusted to pH 2.5, through a membrane with a nominal molecular weight cut-off of 30,000 at 15 degrees C substantially reduced the level of CMP, lactose, and minerals in the whey with retention of the whey proteins. The resulting WPC formed from this process was suitable for the inclusion of sodium polyphosphate to produce superior functional properties in terms of gelation and water-holding capacity.

show abstract

“…Calcium affects gelation properties of WPC (Mei et al, 1996;Varunsatian et al, 1983) and ␤-Lg (Mulvihill & Kinsella, 1988). Exact nature/role of calcium/␤-lactoglobulin interaction is not clear though significant interaction between calcium and free sulfhydryl groups have been reported in whey proteins (Schmidt et al, 1984).…”

mentioning

confidence: 99%

Influence of Cation Sequestering and pH on Quiescent Thermal Association of .BETA.-Lacto-globulin NB from Fresh Cheddar Whey: An Insight into Gelation Mechanism.

Haque

Sharma

2002

FSTR

View full text Add to dashboard Cite

Freshly fractionated ␤-lactoglobulin AB (␤-Lg) from Cheddar whey was dispersed at pH 3.5, 7, and 9 buffers containing 20 mM EDTA, and circulated at 25˚C through a closed loop containing a 200 nm pore size membrane, to remove traces of dust and large aggregates, and an water jacketed cuvette placed within a Dynamic Light Scattering (DLS) device for real-time data acquisition. Filtered samples were step-wise heated from 25˚C to 90˚C with continuous data acquisition to study dynamic changes in mean aggregate diameter (MAD). Data were analyzed by cumulant method for apparent MAD and CONTIN for size distribution. Initial MAD (IMAD) of about 200 nm, reflecting the pore size of the filter used, was observed for all experiments prior to heating. Mid-range aggregate, Agg3 (100-599 nm), was ubiquitous in all distributions and Agg1 (monomer-dimer) was only seen at pH 7 and 25˚C. Increased temperatures gave rise to larger aggregates (>micron) (Agg4 and 5) with concomitant disappearance of Agg3. The greatest increase in MAD was at pH 3.5 and the lowest was at pH 9. Pre-gelation (<70˚C) kinetic rates were 4.29, 1.53, and -0.11¥ ¥ ¥ ¥10 -4 s -1 for pH 3.5, 7.0, and 9.0, respectively, giving MADs that were 3.5, 2.2 and 0.8 fold compared to IMAD. Above 70˚C (apparent gelation range), relative aggregate enlargement was greatest at pH 3.5 being 55, 21, and 4.2 fold of IMAD, respectively, for pH 3.5, 7, and 9 at 90˚C. An apparent gel formed at pH 3.5 and a turbid gel/coagulum formed at pH 7 and none at pH 9. It is conceivable that increased association at pre-gelation temperatures is required for gelation. A mechanism has been postulated.

show abstract

Gelation of Calcium‐Reduced and Lipid‐Reduced Whey Protein Concentrates as Affected by Total and Ionic Mineral Concentrations

Cited by 7 publications

References 32 publications

Rheological properties of commercial whey protein samples from the MADGELAS survey

Rheological properties of commercial whey protein samples from the MADGELAS survey

Production of a High Gel Strength Whey Protein Concentrate from Cheese Whey

Influence of Cation Sequestering and pH on Quiescent Thermal Association of .BETA.-Lacto-globulin NB from Fresh Cheddar Whey: An Insight into Gelation Mechanism.

Contact Info

Product

Resources

About