Comparison of Calcium-Induced Associations of Bovine and Caprine Caseins and the Relationship of αs1-Casein Content to Colloidal Stabilization: A Thermodynamic Linkage Analysis

Mora-Gutierrez, Adela; Farrell, Harold M.; Kumosinski, Thomas F.

doi:10.3168/jds.s0022-0302(93)77711-5

Cited by 13 publications

(20 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In contrast to this, κ-casein content decreased with increasing holding time to a much lesser extent and there was no marked difference between holding times. These observations are in agreement with the results of Mora-Gutierrez et al (1993) concerning the calcium sensitivity and tendency of self-association of individual caseins when we consider heat-induced coagulation as a heat-induced re-arrangement…”

Section: Heat-induced Aggregation Of Caseins In Concentrated Skim Milksupporting

confidence: 92%

Dissociation and coagulation of caseins and whey proteins in concentrated skim milk heated by direct steam injection

Dumpler

Wohlschläger

Kulozik

2016

Dairy Sci. & Technol.

View full text Add to dashboard Cite

Heat treatment of concentrated milk systems for preservation and long shelf life or at least a sufficient removal of food pathogens prior to spray drying is a crucial step due to the decreasing stability of these systems toward heat compared to unconcentrated milk. Heat-induced coagulation is observed when temperature-time combinations for the achievement of certain microbial inactivation effects are higher than the heat and colloidal stability of the concentrated milk system allows. In this work, the effects of direct steam injection on the stability of casein micelles in concentrated skim milk (CSM) of 18, 23, and 27% total non-fat solids, heat-treated by direct steam injection (DSI), were investigated. Quantitative differential centrifugation for the separation of aggregates, casein micelles, dissociated submicellar particles, and soluble proteins and subsequent analysis of caseins and whey proteins within these fractions by RP-HPLC were applied. Quantitative separation was monitored by particle size measurements. The dissociation of κ-casein as well as an increase in casein micelle hydrodynamic radius were observed to increase with increasing total solid content of CSM, heat treatment time, and temperature. Heat-induced dissociation of β-Lg-κcasein complexes at a critical level of 30-35% was found to induce severe coagulation of κ-casein-depleted calcium-sensitive casein micelles in CSM heated by DSI. Dissociated and aggregated proteins were found to be present as distinct colloidal particle classes differing in size from casein micelles.

show abstract

Section: Heat-induced Aggregation Of Caseins In Concentrated Skim Milksupporting

confidence: 92%

Dissociation and coagulation of caseins and whey proteins in concentrated skim milk heated by direct steam injection

Dumpler

Wohlschläger

Kulozik

2016

Dairy Sci. & Technol.

View full text Add to dashboard Cite

show abstract

“…Moreover, it has also been shown that genetically variable caprine caseins also differ from those of bovine milk in terms of their interactions with calcium, and their resultant solubilities and colloidal stabilities (Mora-Gutierrez, Farrell, & Kumosinski, 1993. It was therefore of interest to determine if these in vitro effects would carryover to the cheese matrix and the digestive process.…”

Section: Discussionmentioning

confidence: 98%

“…Accordingly based on phosphorylation, the mineral binding activity of caseins follows the order: a s2 -casein4a s1 -casein4b-casein4k-casein (Kitts, 1994). In addition, it has been suggested that coordinate complexes may be formed between a s -and b-casein molecules with calcium and other divalent cations, which lead to increased solubility (Farrell, 1999;Mora-Gutierrez et al, 1993). CPP released from casein hydrolysis in vivo have the ability to bind and keep soluble cations (Brule´& Fauquant, 1982); they improve calcium and zinc absorption (Hansen, Sandstro¨m, & Lo¨nnerdal, 1996).…”

Section: Controlmentioning

confidence: 98%

Effects of bovine and caprine Monterey Jack cheeses fortified with milk calcium on bone mineralization in rats

Mora-Gutierrez¹,

Farrell²,

Attaie³

et al. 2007

International Dairy Journal

View full text Add to dashboard Cite

“…They have been studied using various techniques including FT‐IR spectroscopy,1 thermodynamic linkage analysis,2 scattering and turbidimetric techniques,3 and transmission electron microscopy and scanning electron microscopy 4. Spherical micelles (up to 300 nm) form at low ionic strength 2, 4. Caseins are heterogeneous proteins containing mainly α S1, α S2, β , and κ polypeptides consisting of both hydrophobic and hydrophilic amino acids.…”

Section: Introductionmentioning

confidence: 99%

Morphology and Phase Separation of Hydrophobic Clusters of Soy Globular Protein Polymers

Sun

Wang

Zhang

et al. 2008

Macromolecular Bioscience

View full text Add to dashboard Cite

Protein hydrophobic interaction has been considered the most important factor dominating protein folding, aggregation, gelling, self-assembly, adhesion, and cohesion properties. In this paper, morphology and phase separation of hydrophobic clusters, networks, and aggregates of soy globular protein polymers, induced by using a reducing agent (NaHSO3), are studied using microscopic instruments. The morphology and phase separation of these hydrophobic clusters are sensitive to protein structure and composition, pH, and ionic-strength (I(m)). Most of the clusters are in spherical-shape architecture and mainly consist of hydrophobic polypeptides. Rod-shape clusters were also observed at higher ionic strength, and mainly consist of hydrophilic polypeptides. The ratio of hydrophobic/hydrophilic (HB/HL) polypeptides is important to facilitate the formation of clusters in an environment with a certain pH value and ionic strength. At HB/HL 0.8, uniform spherical clusters were observed and diameters ranged from 30 to 70 nm. At HB/HL <0.8, large spherical clusters were formed with diameters ranging from 100 to 1,000 nm, and at HB/HL >or=1.8, large hydrophobic aggregates formed, and size of aggregates can be up to 2 500 nm. When solid content increased from 3% to 38%, at I(m) or= 0.115 mol x L(-1), HB/HL ratio >or=1.8, the large aggregates became very cohesive and viscoelastic. Clear phase separation was observed during curing between hydrophobic and hydrophilic protein polymers. Phase-separation degree increased as HB/HL ratio increased.

show abstract

Comparison of Calcium-Induced Associations of Bovine and Caprine Caseins and the Relationship of αs1-Casein Content to Colloidal Stabilization: A Thermodynamic Linkage Analysis

Cited by 13 publications

References 17 publications

Dissociation and coagulation of caseins and whey proteins in concentrated skim milk heated by direct steam injection

Dissociation and coagulation of caseins and whey proteins in concentrated skim milk heated by direct steam injection

Effects of bovine and caprine Monterey Jack cheeses fortified with milk calcium on bone mineralization in rats

Morphology and Phase Separation of Hydrophobic Clusters of Soy Globular Protein Polymers

Contact Info

Product

Resources

About