2009
DOI: 10.1016/j.foodres.2009.07.028
|View full text |Cite
|
Sign up to set email alerts
|

Impact of protein self-assemblages on foam properties

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

0
13
0

Year Published

2012
2012
2025
2025

Publication Types

Select...
6
2

Relationship

0
8

Authors

Journals

citations
Cited by 22 publications
(13 citation statements)
references
References 23 publications
0
13
0
Order By: Relevance
“…Besides, as reported earlier, during processing the thermal treatment can cause the denaturation of such type of compounds and result in the conformational changes. These changes might affect the solubility and stability of compound along with their long term storage [13,14]. Hence, the biofield treatment might be used as an effective measure to increase the thermal stability, thereby increasing the stability, efficacy and shelf-life of these compounds.…”
Section: Tga/dtg Analysismentioning
confidence: 99%
See 1 more Smart Citation
“…Besides, as reported earlier, during processing the thermal treatment can cause the denaturation of such type of compounds and result in the conformational changes. These changes might affect the solubility and stability of compound along with their long term storage [13,14]. Hence, the biofield treatment might be used as an effective measure to increase the thermal stability, thereby increasing the stability, efficacy and shelf-life of these compounds.…”
Section: Tga/dtg Analysismentioning
confidence: 99%
“…Besides, during processing such kind of products are subjected to various thermal treatments to inactivate the antinutritional factors, remove allergens, and to obtain the required solubility and texture [12]. However, they may face the problem of some conformational changes due to their thermal denaturation during heating that might affect their solubility, stability, and shelf-life [13,14]. Therefore, it creates the need for some alternative strategies that may help to improve the stability related issues of this compound in a cost-effective manner.…”
Section: Introductionmentioning
confidence: 99%
“…With addition of salt, particle average size of WPI aggregates increased from 180 to 327 nm associated with a morphological transformation (compact/spherical to fibrillar aggregates). In a series of articles, (Nicorescu et al, 2008a, b;Nicorescu et al, 2009) reported the effect of dynamic heat treatment (100°C) using a tubular heat exchanger of a WPI solution (20 g L À1 ) at pH 7 to investigate denaturation/aggregation and foaming properties, with and without NaCl addition (100 mM). It was shown that not only denaturation (10%) and size (less than 10 lm) of aggregates was reduced by the presence of NaCl, but also the aggregates (diameter about 200 nm) obtained in the presence of 0.1 M NaCl played a key role on the stabilization of gas-liquid interfaces.…”
Section: Effect Of Salt and Other Microenvironments On Whey Proteins mentioning
confidence: 99%
“…NaCl addition after a given coarsening time led to significantly smaller air bubble diameters for foam stabilized with WPI soluble aggregates if compared to aggregates generated without salts. Different foaming properties (overrun, foam stability and texture) of WPI (2% w/v) were studied by heating at 100°C with and without NaCl addition (0-100 mM) (Nicorescu et al, 2008b;Nicorescu et al, 2009). The aggregates (about 200 nm diameter) obtained in the presence of salt and heat treatment led to smaller and more homogeneous air bubble size distributions in foams, with improved texture and increased stability against drainage.…”
Section: Foaming Propertiesmentioning
confidence: 99%
“…[12][13][14][15][16] FPIA has a high detection throughput, and is therefore well-suited for estimating particle size in situ in turbid solutions such as suspensions and emulsions. Additionally, it can provide an assessment of not only particle number, but also particle size and shape by generating images of samples.…”
mentioning
confidence: 99%