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Modification of Colloidal Stability of Casein Micelles by Enzymatic Hydrolysis
Šefčíková, M., Šefčík, J. and Šefčík, J. Modification of Colloidal Stability of Casein Micelles by Enzymatic Hydrolysis Chemical Papers, Vol.56, No. 6, 2002, 400-405
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Document type:
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Článok z časopisu / Journal Article |
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Collection:
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Chemical papers
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| Attached Files |
| Name |
Description |
MIMEType |
Size |
Downloads |
n566a400.pdf
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566a400.pdf |
application/pdf |
162.90KB |
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| Author(s) |
Šefčíková, M.
Šefčík, J.
Šefčík, J.
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| Title |
Modification of Colloidal Stability of Casein Micelles by Enzymatic Hydrolysis
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| Journal name |
Chemical Papers
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| Publication date |
2002
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| Year available |
2002
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| Volume number |
56
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| Issue number |
6
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| ISSN |
0366-6352
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| Start page |
400
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| End page |
405
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| Place of publication |
Poland
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| Publisher |
Versita
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| Collection year |
2002
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| Language |
english
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| Subject |
290000 Engineering and Technology
290600 Chemical Engineering
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| Abstract/Summary |
Destabilization of casein micelles in reconstituted skim milk due to the enzymatic hydrolysis was studied at 32ºC with solutions containing from 0.090 to 0.110 g cm−3 of skim milk powder at pH 6.4. Destabilized micelles were precipitated by the acetate bu er and dissolved in NaOH solutions, where their concentration was determined spectrophotometrically. Within the narrow range of skim milk concentrations around 0.10 g cm−3 the kinetics of the micelle destabilization process changed rapidly and qualitatively, indicating changes in the destabilization mechanism. While in the solution with the 0.090 g cm−3 skim milk concentration the destabilized micelles were produced shortly after beginning of the hydrolysis, in the more concentrated mixture a substantial lag phase exists, leading to a considerably di erent time evolution of the destabilized micelle concentration. According to the analysis based on the mathematical model of the destabilization process, these changes can be attributed to the shift of the hydrolysis kinetics from the rst order to a two-step mechanism and to the change of character of the spatial enzyme activity from the locally correlated action to the spatially random hydrolysis.
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