| Project/Area Number |
07660260
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Fisheries chemistry
|
|---|
| Research Institution | HOKKAIDO UNIVERSITY |
|---|
Principal Investigator |
KAWAI Yuji Hokkaido Univ., Fac.Fish., Assoc.Prof., 水産学部, 助教授 (60195039)
|
|---|
| Project Period (FY) |
1995 – 1996
|
| Project Status |
Completed (Fiscal Year 1996)
|
| Budget Amount *help |
¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1996: ¥500,000 (Direct Cost: ¥500,000)
|
|---|
| Keywords | parvalbumin / sarcoplasmic protein / carp / emulsifying property / disulfide bond / surface hydrophobicity / isoelectric point / 乳化活性 / 脂肪結合能 |
|---|
| Research Abstract |
Parvalbumin (PA) was separated from carp sarcoplasmic protein fraction with Sephadex G-75 chromatography. When dispersed with triolein, PA fraction had superior emulsifying properties to the other sarcoplasmic protein (Sp-P) fraction. Fat-binding capacity of PA fraction was higher at lower protein concentration. Surface hydrophobicity of PA fraction was significantly less than Sp-P fraction. Superiority of emulsifying activity in PA was suggested to be independent of hydrophobicity.
Three isoforms (a, b, c) of PA were obtained with DEAE-Sephacel chromatography in order of the elution time. Emulsifying activity of isoform c was the highest in the PA isoforms (c>b>a). Intermolecular disulfide bond was formed between the molecules of the isoforms to induce dimerization by heating above 80ﾟC.The dimerization somewhat affected the emulsifying activity. EDTA also led the PA isoforms to vary their emulsifying activity, surface hydrophobicity and electrostatic property (isoelectric point). Changes in the structural and electrostatic states of PA related to Ca^<2+> might have markedly affected the emulsifying properties.
|
