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Fluorescent probe and raman spectroscopic investigation of the effects of pH, heating, and [kappa]-carrageenan on whey protein structure Alizadeh-Pasdar, Nooshin
Abstract
Surface hydrophobicity (S₀) is an important structural parameter describing food proteins due to its correlation with functionality. A new method to measure S₀ was established based on the neutral fluorescent probe, 6-propionyl-2-(N,N-dimethylamino)naphthalene (PRODAN). S₀ was determined for whey protein isolate (WPI), bovine serum albumin (BSA)and β-lactoglobulin (BLG) at various pH (3.0, 5.0, 7.0 and 9.0) under heated (80°C for 30 min) or unheated conditions. S₀ values measured by PRODAN and cis-parinaric acid (CPA) were lower at pH 3.0 than at other pH, while values measured by 1-anilinonaphthalene-8-sulfonic acid (ANS) were highest at pH 3.0. The anionic probes ANS and CPA yielded opposing results on the effects of pH and heating on proteinhydrophobicity. Heating, pH and addition of K-carrageenan (KCG) at low (1.0:62.5), medium(1.0:6.0) or high (1.0:1.2) ratios of KCG:protein, as well as the interactions between these factors, significantly (P
Item Metadata
| Title |
Fluorescent probe and raman spectroscopic investigation of the effects of pH, heating, and [kappa]-carrageenan on whey protein structure
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| Creator | |
| Publisher |
University of British Columbia
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| Date Issued |
2001
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| Description |
Surface hydrophobicity (S₀) is an important structural parameter describing food proteins due to its correlation with functionality. A new method to measure S₀ was established based on the neutral fluorescent probe, 6-propionyl-2-(N,N-dimethylamino)naphthalene (PRODAN). S₀ was determined for whey protein isolate (WPI), bovine serum albumin (BSA)and β-lactoglobulin (BLG) at various pH (3.0, 5.0, 7.0 and 9.0) under heated (80°C for 30 min) or unheated conditions. S₀ values measured by PRODAN and cis-parinaric acid (CPA) were lower at pH 3.0 than at other pH, while values measured by 1-anilinonaphthalene-8-sulfonic acid (ANS) were highest at pH 3.0. The anionic probes ANS and CPA yielded opposing results on the effects of pH and heating on proteinhydrophobicity. Heating, pH and addition of K-carrageenan (KCG) at low (1.0:62.5), medium(1.0:6.0) or high (1.0:1.2) ratios of KCG:protein, as well as the interactions between these factors, significantly (P
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| Extent |
8632545 bytes
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| Genre | |
| Type | |
| File Format |
application/pdf
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| Language |
eng
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| Date Available |
2009-09-16
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| Provider |
Vancouver : University of British Columbia Library
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| Rights |
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.
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| DOI |
10.14288/1.0090598
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| URI | |
| Degree (Theses) | |
| Program (Theses) | |
| Affiliation | |
| Degree Grantor |
University of British Columbia
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| Graduation Date |
2001-05
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| Campus | |
| Scholarly Level |
Graduate
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| Aggregated Source Repository |
DSpace
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Rights
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.