2005
DOI: 10.1016/j.lwt.2004.03.013
|View full text |Cite
|
Sign up to set email alerts
|

Whey proteins solubility as function of temperature and pH

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

14
163
0
6

Year Published

2006
2006
2023
2023

Publication Types

Select...
8
2

Relationship

0
10

Authors

Journals

citations
Cited by 279 publications
(183 citation statements)
references
References 9 publications
14
163
0
6
Order By: Relevance
“…The increase in the solubility might be attributed to conformational and structural changes so that hydrophilic amino acids residues are reoriented towards the water. Generally, higher solubility implies better emulsion, gelation, and foaming properties [57]. It has been reported that sonication could favor the enlargement of soluble protein aggregates from insoluble precipitates [58].…”
Section: Effect Of Ultrasound Pretreatment On Solubility Of Rapeseed mentioning
confidence: 99%
“…The increase in the solubility might be attributed to conformational and structural changes so that hydrophilic amino acids residues are reoriented towards the water. Generally, higher solubility implies better emulsion, gelation, and foaming properties [57]. It has been reported that sonication could favor the enlargement of soluble protein aggregates from insoluble precipitates [58].…”
Section: Effect Of Ultrasound Pretreatment On Solubility Of Rapeseed mentioning
confidence: 99%
“…Proteins are denatured due to the effect of temperature on the non-covalent bonds involved in the stabilization of secondary and tertiary structure. Denaturation decreases protein solubility compared to the native protein [35].…”
Section: Effect Of Cleaning Solution Temperaturementioning
confidence: 99%
“…On the other hand, polymer brushes with amine or imine groups, for example poly(2-(dimethylaminoethyl) methacrylate) PDMA [150] or poly(vinyl pyridine) [144,151] respectively, aggregate at high pH values. Interestingly, proteins are another interesting class of pH responsive coatings, due to their pH-dependent U-shape solubility behavior with a minimum at the isoelectric point (pI) [152] . Proteins are natural co-polymers made of polar, nonpolar, and ionic monomers (in total 21 aminoacids, including selenocysteine), and depending on the primary structure of the proteins, they can exhibit dissimilar sensitivity toward pH and different pI.…”
Section: Polymer Brushesmentioning
confidence: 99%