1989
DOI: 10.1021/jf00087a012
|View full text |Cite
|
Sign up to set email alerts
|

Effect of storage temperatures on the formation of disulfides and denaturation of Tilapia hybrid actomyosin (Tilapia nilotica .times. Tilapia aurea)

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

0
11
0

Year Published

1994
1994
2016
2016

Publication Types

Select...
6
1

Relationship

0
7

Authors

Journals

citations
Cited by 15 publications
(11 citation statements)
references
References 12 publications
0
11
0
Order By: Relevance
“…The results were expressed as the percentage of protein solubilized with respect to the total protein content of the meat batter (AOAC 2000). This fraction was designated salt-soluble protein and it is considered to be essentially native protein (Jiang et al, 1989).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…The results were expressed as the percentage of protein solubilized with respect to the total protein content of the meat batter (AOAC 2000). This fraction was designated salt-soluble protein and it is considered to be essentially native protein (Jiang et al, 1989).…”
Section: Resultsmentioning
confidence: 99%
“…The results were expressed as the percentage of protein solubilized with respect to the total protein content of the meat batter (AOAC 2000). This fraction was designated salt-soluble protein and it is considered to be essentially native protein (Jiang et al, 1989).Texture profile analysis (TPA) Frozen meatballs were thawed at 2℃ for approximately 12 h. Once thawed, meatballs were heated at 80℃ in a water bath for 15 min and then cooled to room temperature. The texture profile analysis (TPA) attributes of the meatballs was determined using a texture analyzer (TA-XT.plus, Stable Micro system Ltd., Surry, UK).…”
mentioning
confidence: 99%
“…Uedaira and Uedaira (1980) tested the thermal denaturation of lysozyme in sugar solution and found that sugars could stabilize the protein structure by intensifying the hydrophobic interactions inside the protein molecule. Jiang, San, and Japit (1989) concluded that formation of new hydrogen and disulfide bonds and ionic interactions during frozen storage were the causes for protein coagulation and denaturation. Results from the RSo changes under the influences of heating and freezing concluded that XOS provided a more efficient protective effect on SSP than other cryoprotectants (i.e., sorbitol, sucrose).…”
Section: Saccharides Bmentioning
confidence: 99%
“…Low extractable AM in thawed fish might be due to the freeze‐denaturation of myofibrillar proteins during frozen storage. 49–54 The extractable AM of fish sol was higher than that of thawed fish due to the removal of water‐soluble protein during the washing treatment, which consequently increased the relative ratio of extractable AM of fish sol to that of fish meat. Although 3% sugar was added to prevent the denaturation of myofibrillar proteins, the AM extractability of fish sol decreased immediately after freezing and further decreased after freeze‐drying processing ( Table 1).…”
Section: Resultsmentioning
confidence: 99%
“…Low extractable AM in thawed fish might be due to the freeze-denaturation of myofibrillar proteins during frozen storage. [49][50][51][52][53][54] The extractable AM of fish sol was higher than that of thawed fish due to the removal of watersoluble protein during the washing treatment, which consequently increased the relative ratio of extractable quality meat binders. The objectives of this study were to evaluate the potential for making meat binders using freeze-thawed mackerel (Scomber australasicus), and to determine the effects of different reducing agents on the protein quality and binding ability of the meat binder.…”
Section: Effects Of Freezing Process and Reducing Agents On The Extramentioning
confidence: 99%