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The effect of ethanol and heat on the functional hydrophobicity of casein micelles
R. Trejo,
F. Harte
Food Science
Research output
:
Contribution to journal
›
Article
›
peer-review
16
Scopus citations
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Dive into the research topics of 'The effect of ethanol and heat on the functional hydrophobicity of casein micelles'. Together they form a unique fingerprint.
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Agriculture & Biology
micelles
93%
hydrophobicity
87%
casein
74%
milk proteins
67%
ethanol
58%
sulfonic acids
56%
heat
46%
skim milk
37%
wavelengths
31%
fluorescence
24%
whey protein isolate
21%
sampling
17%
food industry
14%
ingredients
13%
physicochemical properties
13%
temperature
6%
proteins
5%
Medicine & Life Sciences
Micelles
100%
Hydrophobic and Hydrophilic Interactions
92%
Milk Proteins
88%
Ethanol
70%
Hot Temperature
64%
Sulfonic Acids
44%
1-anilino-8-naphthalenesulfonate
31%
Fluorescence
27%
Whey Proteins
23%
Food Industry
21%
Fluorescent Dyes
17%
Milk
15%
Temperature
11%
Proteins
6%