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Heat stability of micellar casein concentrates as affected by temperature and pH
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Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1006/fstl.2000.0665openalex-snapshot
Further Studies on the Heat-induced, pH-dependent Dissociation of Casein from the Micelles in Reconstituted Skim Milk
inferredcites →https://doi.org/10.1007/978-0-387-84865-5_9openalex-snapshot
Milk Salts: Technological Significance
inferredcites →https://doi.org/10.1007/978-1-4419-8602-3_1openalex-snapshot
Milk Proteins: General and Historical Aspects
inferredcites →https://doi.org/10.1007/978-1-4419-8602-3_25openalex-snapshot
Heat-Induced Coagulation of Milk
inferredcites →https://doi.org/10.1016/0308-8146(83)90108-5openalex-snapshot
Developments in dairy chemistry—1
inferredcites →https://doi.org/10.1016/j.memsci.2004.06.029openalex-snapshot
Membrane fractionation of milk: state of the art and challenges
inferredcites →https://doi.org/10.1017/s002202990001284xopenalex-snapshot
The heat stability of milk as affected by variations in pH and milk salts
inferredcites →https://doi.org/10.1021/jf960507mopenalex-snapshot
Heat-Induced, pH-Dependent Dissociation of Casein Micelles on Heating Reconstituted Skim Milk at Temperatures below 100 °C
inferredcites →https://doi.org/10.1074/jbc.m413504200openalex-snapshot
Physicochemical Characterization of Casein Phosphopeptide-Amorphous Calcium Phosphate Nanocomplexes
inferredcites →https://doi.org/10.3168/jds.2008-1467openalex-snapshot
Effect of solvent and temperature on the size distribution of casein micelles measured by dynamic light scattering
inferredcites →https://doi.org/10.3168/jds.2010-3121openalex-snapshot
Processing factors that influence casein and serum protein separation by microfiltration
inferredcites →https://doi.org/10.3168/jds.2010-3169openalex-snapshot
Micellar casein concentrate production with a 3X, 3-stage, uniform transmembrane pressure ceramic membrane process at 50°C
inferredcites →https://doi.org/10.3168/jds.2011-4875openalex-snapshot
The effect of commercial sterilization regimens on micellar casein concentrates
inferredcites →https://doi.org/10.3168/jds.s0022-0302(05)72865-4openalex-snapshot
A Microfiltration Process to Maximize Removal of Serum Proteins from Skim Milk Before Cheese Making
inferredcites →https://doi.org/10.3168/jds.s0022-0302(85)81005-5openalex-snapshot
Role of Phosphate Groups in the Calcium Sensitivity of αs2-Casein
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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inferred← citeshttps://doi.org/10.1016/j.foodhyd.2020.105778openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.idairyj.2018.01.002openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.idairyj.2018.02.009openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.idairyj.2020.104657openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.idairyj.2021.104980openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.idairyj.2021.105136openalex-snapshot
Heat-induced changes in caseins and casein micelles, including interactions with denatured whey proteins
inferred← citeshttps://doi.org/10.1016/j.idairyj.2022.105373openalex-snapshot
The heat stability of caprine and bovine micellar casein dispersions
inferred← citeshttps://doi.org/10.1016/j.idairyj.2022.105403openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.idairyj.2023.105583openalex-snapshot
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Investigation of Blended Milk-Pea Protein Beverage Fouling and Cleaning Using a Quartz Crystal Microbalance with Dissipation
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Effect of microfiltration concentration factor on serum protein removal from skim milk using spiral-wound polymeric membranes
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