- Library Home /
- Search Collections /
- Open Collections /
- Browse Collections /
- UBC Theses and Dissertations /
- A study of protein surface hydrophobicity and structure-function...
Open Collections
UBC Theses and Dissertations
UBC Theses and Dissertations
A study of protein surface hydrophobicity and structure-function analysis of proteins in spray dried egg albumen Cheng, Eugene S. Y.
Abstract
In examining functional properties of food proteins, the ultimate goal of all researchers is to understand basic information relating functional properties to particular conformational or structural features of the protein. It is generally accepted that the molecular property of hydrophobicity plays an important role in the function of food proteins. In the first part of the thesis, surface hydrophobicity (S₀) of 10 proteins, under varying conditions of pH (3.0, 7.0, and 9.0) and salt concentrations (0.01 and 1.0 M NaCl), measured using an uncharged fluorescent probe, PRODAN (6-propionyl-2- (dimethylamino)naphthalene) was compared with S₀ determined with an anionic probe, ANS (l-anilinonaphthalene-8- sulfonate). S₀ values measured by both PRODAN and ANS for each protein were statistically different (P < 0.05) as a function of pH and salt concentration. Overall, lowest S₀ values using PRODAN were found at pH 3.0, while S₀ values using ANS were generally higher at acidic than neutral or alkaline pH. These results demonstrate the need to consider charged probeprotein interactions when applying anionic fluorescent probes for surface hydrophobicity quantification. In the second part of the thesis, the structure-function relationships of spray dried egg albumen and its functional properties (e.g. gelation and foaming properties) were investigated. Protein structure was evaluated by measurement of surface hydrophobicity, net charge as zeta potential (ZP), sulfhydryl (SH) and disulfide (SS) groups, and by differential scanning calorimetry. Simple linear correlations were performed to better understand the structure-function relationship between structural parameters and functionality (gel strength and foam volume). In general, gel strength was positively correlated with S₀ determined by ANS, reactive S H groups, SS bonds and ZP (P < 0.001) and negatively correlated with total SH groups (P = 0.009). In general, foam volume was positively correlated with S₀ determined by PROD AN and ANS, reactive SH groups, and SS bonds (P < 0.05) and negatively correlated with total SH groups and ZP (P < 0.05). Significant correlations of structural properties to gel strength and foam volume were observed by multiple regression analysis using a full quadratic model (R² = 0.956 and R² = 0.918, respectively; P < 0.001; n = 53).
Item Metadata
Title |
A study of protein surface hydrophobicity and structure-function analysis of proteins in spray dried egg albumen
|
Creator | |
Publisher |
University of British Columbia
|
Date Issued |
2001
|
Description |
In examining functional properties of food proteins, the ultimate goal of all researchers
is to understand basic information relating functional properties to particular conformational or
structural features of the protein. It is generally accepted that the molecular property of
hydrophobicity plays an important role in the function of food proteins.
In the first part of the thesis, surface hydrophobicity (S₀) of 10 proteins, under varying
conditions of pH (3.0, 7.0, and 9.0) and salt concentrations (0.01 and 1.0 M NaCl), measured
using an uncharged fluorescent probe, PRODAN (6-propionyl-2- (dimethylamino)naphthalene)
was compared with S₀ determined with an anionic probe, ANS (l-anilinonaphthalene-8-
sulfonate).
S₀ values measured by both PRODAN and ANS for each protein were statistically
different (P < 0.05) as a function of pH and salt concentration. Overall, lowest S₀ values using
PRODAN were found at pH 3.0, while S₀ values using ANS were generally higher at acidic
than neutral or alkaline pH. These results demonstrate the need to consider charged probeprotein
interactions when applying anionic fluorescent probes for surface hydrophobicity
quantification.
In the second part of the thesis, the structure-function relationships of spray dried egg
albumen and its functional properties (e.g. gelation and foaming properties) were investigated.
Protein structure was evaluated by measurement of surface hydrophobicity, net charge as zeta
potential (ZP), sulfhydryl (SH) and disulfide (SS) groups, and by differential scanning
calorimetry.
Simple linear correlations were performed to better understand the structure-function
relationship between structural parameters and functionality (gel strength and foam volume).
In general, gel strength was positively correlated with S₀ determined by ANS, reactive S H
groups, SS bonds and ZP (P < 0.001) and negatively correlated with total SH groups (P =
0.009). In general, foam volume was positively correlated with S₀ determined by PROD AN
and ANS, reactive SH groups, and SS bonds (P < 0.05) and negatively correlated with total SH
groups and ZP (P < 0.05).
Significant correlations of structural properties to gel strength and foam volume were
observed by multiple regression analysis using a full quadratic model (R² = 0.956 and R² =
0.918, respectively; P < 0.001; n = 53).
|
Extent |
6078662 bytes
|
Genre | |
Type | |
File Format |
application/pdf
|
Language |
eng
|
Date Available |
2009-07-27
|
Provider |
Vancouver : University of British Columbia Library
|
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.
|
DOI |
10.14288/1.0099587
|
URI | |
Degree | |
Program | |
Affiliation | |
Degree Grantor |
University of British Columbia
|
Graduation Date |
2001-05
|
Campus | |
Scholarly Level |
Graduate
|
Aggregated Source Repository |
DSpace
|
Item Media
Item Citations and Data
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.