Abstract
A novel process using pH-shift to recover fish proteins has been intensively studied. However, little information of its frozen stability has been revealed. The highest gel texture was found for samples frozen at pH 5.5 (5) and 7.0 (7) with cryoprotectants (C) and without freeze/thaw (F), whereas the lowest gel texture was obtained from frozen/thawed samples without cryoprotectants (NC). 5NC-F and 7NC-F demonstrated the lowest surface hydrophobicity and total sulfhydryl (SH), perhaps suggesting more protein aggregation through hydrophobic interactions and disulfide bonds. A slightly less stability of alkali-treated protein isolates (AKPI) kept at pH 5.5 than at pH 7 was noticed. AKPI, whether kept at pH 5.5 or 7.0, requires cryoprotectants to maintain frozen stability for longer shelf life.
| Original language | English |
|---|---|
| Journal | Journal of Food Science |
| Volume | 71 |
| Issue number | 3 |
| Publication status | Published - 2006 Apr 1 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Food Science
Cite this
Frozen stability of fish protein isolate under various storage conditions. / Thawornchinsombut, Supawan; Park, Jae W.
In: Journal of Food Science, Vol. 71, No. 3, 01.04.2006.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Frozen stability of fish protein isolate under various storage conditions
AU - Thawornchinsombut, Supawan
AU - Park, Jae W.
PY - 2006/4/1
Y1 - 2006/4/1
N2 - A novel process using pH-shift to recover fish proteins has been intensively studied. However, little information of its frozen stability has been revealed. The highest gel texture was found for samples frozen at pH 5.5 (5) and 7.0 (7) with cryoprotectants (C) and without freeze/thaw (F), whereas the lowest gel texture was obtained from frozen/thawed samples without cryoprotectants (NC). 5NC-F and 7NC-F demonstrated the lowest surface hydrophobicity and total sulfhydryl (SH), perhaps suggesting more protein aggregation through hydrophobic interactions and disulfide bonds. A slightly less stability of alkali-treated protein isolates (AKPI) kept at pH 5.5 than at pH 7 was noticed. AKPI, whether kept at pH 5.5 or 7.0, requires cryoprotectants to maintain frozen stability for longer shelf life.
AB - A novel process using pH-shift to recover fish proteins has been intensively studied. However, little information of its frozen stability has been revealed. The highest gel texture was found for samples frozen at pH 5.5 (5) and 7.0 (7) with cryoprotectants (C) and without freeze/thaw (F), whereas the lowest gel texture was obtained from frozen/thawed samples without cryoprotectants (NC). 5NC-F and 7NC-F demonstrated the lowest surface hydrophobicity and total sulfhydryl (SH), perhaps suggesting more protein aggregation through hydrophobic interactions and disulfide bonds. A slightly less stability of alkali-treated protein isolates (AKPI) kept at pH 5.5 than at pH 7 was noticed. AKPI, whether kept at pH 5.5 or 7.0, requires cryoprotectants to maintain frozen stability for longer shelf life.
KW - Alkali-treated protein isolates
KW - Cryoprotectant
KW - DSC
KW - Frozen storage
KW - Surface hydrophobicity
UR - http://www.scopus.com/inward/record.url?scp=33646377204&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33646377204&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:33646377204
VL - 71
JO - Journal of Food Science
JF - Journal of Food Science
SN - 0022-1147
IS - 3
ER -