Influence of enzymatic cross-linking on the apparent viscosity and molecular characteristics of casein micelles at neutral and acidic pH

[1]  A. Castro,et al.  Revisiting the dynamics of proteins during milk powder hydration using asymmetric flow field-flow fractionation (AF4) , 2021, Current research in food science.

[2]  A. Castro,et al.  Investigating the effect of powder manufacturing and reconstitution on casein micelles using asymmetric flow field-flow fractionation (AF4) and transmission electron microscopy. , 2021, Food research international.

[3]  Q. Zhong,et al.  Gluconic acid as a chelator to improve clarity of skim milk powder dispersions at pH 3.0. , 2020, Food chemistry.

[4]  M. Fenelon,et al.  Influence of sodium hexametaphosphate addition on the functional properties of milk protein concentrate solutions containing transglutaminase cross-linked proteins , 2020, International Dairy Journal.

[5]  Q. Zhong,et al.  Physicochemical properties of skim milk powder dispersions after acidification to pH 2.4–3.0 and heating , 2020 .

[6]  D. Horne Casein micelle structure and stability , 2020, Milk Proteins.

[7]  Quanyang Li,et al.  Acid and rennet-induced coagulation behavior of casein micelles with modified structure. , 2019, Food chemistry.

[8]  D. Jaros,et al.  Asymmetric flow field flow fractionation for the investigation of caseins cross-linked by microbial transglutaminase , 2019, Food Hydrocolloids.

[9]  C. Ranadheera,et al.  Impact of shear and pH on properties of casein micelles in milk protein concentrate , 2019, LWT.

[10]  Guilherme M. Tavares,et al.  Physico-chemical stability of casein micelles cross-linked by transglutaminase as a function of acidic pH , 2019, Food Structure.

[11]  T. Henle,et al.  Reassembling of Alkali-Treated Casein Micelles by Microbial Transglutaminase. , 2018, Journal of agricultural and food chemistry.

[12]  I. Chronakis,et al.  Crosslinking of milk proteins by microbial transglutaminase: Utilization in functional yogurt products. , 2018, Food chemistry.

[13]  D. Jaros,et al.  Size Separation Techniques for the Characterisation of Cross-Linked Casein: A Review of Methods and Their Applications , 2018 .

[14]  A. Riaublanc,et al.  Determination of hydro-colloidal characteristics of milk protein aggregates using Asymmetrical Flow Field-Flow Fractionation coupled with Multiangle Laser Light Scattering and Differential Refractometer (AF4-MALLS-DRi) , 2018 .

[15]  D. Jaros,et al.  Enzymatic Cross-Linking of Casein Facilitates Gel Structure Weakening Induced by Overacidification , 2017, Food Biophysics.

[16]  D. Jaros,et al.  Cross-linking with microbial transglutaminase: Isopeptide bonds and polymer size as drivers for acid casein gel stiffness , 2017 .

[17]  F. Gaucheron,et al.  Stability of casein micelles cross-linked with genipin: A physicochemical study as a function of pH , 2017, 1701.06638.

[18]  A. Madadlou,et al.  Enzymatic Modification to Stabilize the Fermented Milk Drink, Doogh , 2015 .

[19]  D. Jaros,et al.  Cross-linking with microbial transglutaminase: Relationship between polymerisation degree and stiffness of acid casein gels , 2014 .

[20]  P. Fox,et al.  Milk: An Overview , 2014 .

[21]  E. Şenel,et al.  The effect of transglutaminase on some physicochemical and sensory properties of the Turkish drinking yoghurt Ayran , 2013 .

[22]  M. Richter,et al.  Enzyme-catalyzed protein crosslinking , 2012, Applied Microbiology and Biotechnology.

[23]  V. Urban,et al.  Casein micelles and their internal structure. , 2012, Advances in colloid and interface science.

[24]  Ulrich Kulozik,et al.  Effect of transglutaminase-treated milk powders on the properties of skim milk yoghurt , 2011 .

[25]  P. Brown,et al.  On the distribution of protein refractive index increments. , 2011, Biophysical journal.

[26]  H. Singh Milk Protein Products | Functional Properties of Milk Proteins , 2011 .

[27]  A. Håkansson,et al.  Revealing the size, conformation, and shape of casein micelles and aggregates with asymmetrical flow field-flow fractionation and multiangle light scattering. , 2010, Langmuir : the ACS journal of surfaces and colloids.

[28]  Doris Jaros,et al.  Excessive cross-linking of caseins by microbial transglutaminase and its impact on physical properties of acidified milk gels , 2010 .

[29]  V. Trappe,et al.  Rheology and structural arrest of casein suspensions. , 2010, Journal of colloid and interface science.

[30]  B. Cabane,et al.  Rheology and phase behavior of dense casein micelle dispersions. , 2009, The Journal of chemical physics.

[31]  R. Guo,et al.  pH-dependent structures and properties of casein micelles. , 2008, Biophysical chemistry.

[32]  C. G. D. Kruif,et al.  Structure and stability of nanogel particles prepared by internal cross-linking of casein micelles , 2008 .

[33]  Ulrich Kulozik,et al.  Transglutaminase cross-linking of milk proteins and impact on yoghurt gel properties , 2007 .

[34]  U. Kulozik,et al.  Yoghurt gel formation by means of enzymatic protein cross-linking during microbial fermentation , 2007 .

[35]  Thom Huppertz,et al.  Ethanol stability of casein micelles cross-linked with transglutaminase , 2007 .

[36]  D. Jaros,et al.  ENZYMATIC MODIFICATION THROUGH MICROBIAL TRANSGLUTAMINASE ENHANCES THE VISCOSITY OF STIRRED YOGURT , 2007 .

[37]  T. Huppertz,et al.  Biocompatible micro-gel particles from cross-linked casein micelles. , 2007, Biomacromolecules.

[38]  A. Kelly,et al.  Stability of casein micelles cross-linked by transglutaminase. , 2006, Journal of dairy science.

[39]  Doris Jaros,et al.  TRANSGLUTAMINASE IN DAIRY PRODUCTS: CHEMISTRY, PHYSICS, APPLICATIONS , 2006 .

[40]  Philip M. Kelly,et al.  Influence of transglutaminase treatment on properties of micellar casein and products made therefrom , 2005 .

[41]  U. Kulozik,et al.  Effect of Ultra-high Temperature Treatment on the Enzymatic Cross-linking of Micellar Casein and Sodium Caseinate by Transglutaminase , 2004 .

[42]  E. M. Brown,et al.  Nomenclature of the proteins of cows' milk--sixth revision. , 1965, Journal of dairy science.

[43]  J. Lucey,et al.  Use of multi-angle laser light scattering and size-exclusion chromatography to characterize the molecular weight and types of aggregates present in commercial whey protein products. , 2003, Journal of dairy science.

[44]  A. Bot,et al.  Gelation mechanism of milk as influenced by temperature and pH; studied by the use of transglutaminase cross-linked casein micelles. , 2003, Journal of dairy science.

[45]  Daniel M. Mulvihill,et al.  Functional Milk Proteins: Production and Utilization , 2003 .

[46]  C. Holt,et al.  Casein Micelle Structure, Functions and Interactions , 2003 .

[47]  Juliet A. Gerrard,et al.  Protein–protein crosslinking in food: methods, consequences, applications , 2002 .

[48]  H. Neve,et al.  Effect of enzymatic cross‐linking of milk proteins on functional properties of set‐style yoghurt , 2002 .

[49]  A. Clark,et al.  Cross-linking casein micelles by a microbial transglutaminase conditions for formation of transglutaminase-induced gels , 2000 .

[50]  I. Norton,et al.  Cross-linking casein micelles by a microbial transglutaminase: influence of cross-links in acid-induced gelation , 2000 .

[51]  E. Dickinson Enzymic crosslinking as a tool for food colloid rheology control and interfacial stabilization , 1997 .

[52]  D. Piotrowski,et al.  [Introduction to rheology]. , 1982, Acta haematologica Polonica.

[53]  C. V. Morr,et al.  Molecular weight and size distribution of bovine milk casein micelles. , 1974, Biochimica et biophysica acta.

[54]  V. Bloomfield,et al.  Molecular weight of bovine milk casein micelles from diffusion and viscosity measurements. , 1973, Journal of dairy science.

[55]  P. W. Cole,et al.  Mechanism of action of guinea pig liver transglutaminase. I. Purification and properties of the enzyme: identification of a functional cysteine essential for activity. , 1966, The Journal of biological chemistry.

[56]  G. Berry Thermodynamic and Conformational Properties of Polystyrene. I. Light‐Scattering Studies on Dilute Solutions of Linear Polystyrenes , 1966 .

[57]  G. P. Ellis,et al.  The Maillard reaction. , 1959, Advances in carbohydrate chemistry.