Abstract
This study was conducted to better understand biochemical changes offish muscle proteins as affected by novel surimi process, acid- or alkali-aided solubilization. At 10 mM NaCl, between pH 5 and 10, the solubility of Pacific whiting muscle proteins was low but increased dramatically as the pH was shifted to either acidic or alkaline pH. At 600 mM NaCl, the isoelectric point was shifted to the acidic direction by about 2 pH units, resulting in aggregation of proteins at low pH, but improving the solubility of MHC (myosin heavy chain) between pH 6 and 10. ANS surface hydrophobidty (ANS-S o showed much greater values than PRODAN surface hydrophobidty (PRODAN-S o) for samples treated at pH 2-4 perhaps due to an enhancement of the electrostatic interactions between the ANS probe and proteins. At very high pH, according to hydrophobicity results, proteins were partially refolded when the ionic strength increased. Under acidic conditions, SDS-PAGE demonstrated the degradation of MHC at 10 mM NaCl. The formation of MHC polymers was observed under alkaline treatment with a concomitant decrease of SH content.
| Original language | English |
|---|---|
| Pages (from-to) | 135-154 |
| Number of pages | 20 |
| Journal | Journal of Food Biochemistry |
| Volume | 28 |
| Issue number | 2 |
| Publication status | Published - 2004 May 1 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Food Science
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
Cite this
Role of pH in solubility and conformational changes of Pacific whiting muscle proteins. / Thawornchinsombut, Supawan; Park, Jae W.
In: Journal of Food Biochemistry, Vol. 28, No. 2, 01.05.2004, p. 135-154.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Role of pH in solubility and conformational changes of Pacific whiting muscle proteins
AU - Thawornchinsombut, Supawan
AU - Park, Jae W.
PY - 2004/5/1
Y1 - 2004/5/1
N2 - This study was conducted to better understand biochemical changes offish muscle proteins as affected by novel surimi process, acid- or alkali-aided solubilization. At 10 mM NaCl, between pH 5 and 10, the solubility of Pacific whiting muscle proteins was low but increased dramatically as the pH was shifted to either acidic or alkaline pH. At 600 mM NaCl, the isoelectric point was shifted to the acidic direction by about 2 pH units, resulting in aggregation of proteins at low pH, but improving the solubility of MHC (myosin heavy chain) between pH 6 and 10. ANS surface hydrophobidty (ANS-S o showed much greater values than PRODAN surface hydrophobidty (PRODAN-S o) for samples treated at pH 2-4 perhaps due to an enhancement of the electrostatic interactions between the ANS probe and proteins. At very high pH, according to hydrophobicity results, proteins were partially refolded when the ionic strength increased. Under acidic conditions, SDS-PAGE demonstrated the degradation of MHC at 10 mM NaCl. The formation of MHC polymers was observed under alkaline treatment with a concomitant decrease of SH content.
AB - This study was conducted to better understand biochemical changes offish muscle proteins as affected by novel surimi process, acid- or alkali-aided solubilization. At 10 mM NaCl, between pH 5 and 10, the solubility of Pacific whiting muscle proteins was low but increased dramatically as the pH was shifted to either acidic or alkaline pH. At 600 mM NaCl, the isoelectric point was shifted to the acidic direction by about 2 pH units, resulting in aggregation of proteins at low pH, but improving the solubility of MHC (myosin heavy chain) between pH 6 and 10. ANS surface hydrophobidty (ANS-S o showed much greater values than PRODAN surface hydrophobidty (PRODAN-S o) for samples treated at pH 2-4 perhaps due to an enhancement of the electrostatic interactions between the ANS probe and proteins. At very high pH, according to hydrophobicity results, proteins were partially refolded when the ionic strength increased. Under acidic conditions, SDS-PAGE demonstrated the degradation of MHC at 10 mM NaCl. The formation of MHC polymers was observed under alkaline treatment with a concomitant decrease of SH content.
UR - http://www.scopus.com/inward/record.url?scp=3042579438&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=3042579438&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:3042579438
VL - 28
SP - 135
EP - 154
JO - Journal of Food Biochemistry
JF - Journal of Food Biochemistry
SN - 0145-8884
IS - 2
ER -