scholarly journals Rheological and Textural Properties of Sodium Reduced Salt Soluble Myofibrillar Protein Gels Containing Sodium Tri-Polyphosphate

2015 ◽  
Vol 47 (3) ◽  
pp. 181-187 ◽  
Author(s):  
E. Çarkcioğlu ◽  
A.J. Rosenthal ◽  
K. Candoğan
Keyword(s):  
Textural Properties ◽  
Myofibrillar Protein ◽  
Protein Gels ◽  
Reduced Salt

scholarly journals The Influence of Particle Size and Protein Content in Particle-Filled Myofibrillar Protein Gels

2017 ◽  
Vol 1 (1) ◽  
pp. 109 ◽  
Author(s):  
Andrew J. Gravelle ◽  
Alejandro G. Marangoni ◽  
Shai Barbut
Keyword(s):  
Particle Size ◽  
Protein Content ◽  
Myofibrillar Protein ◽  
Protein Gels

scholarly journals Evaluation of NaCl and KCl Salting Effects on Technological Properties of Pre- and Post-Rigor Chicken Breasts at Various Ionic Strengths

Foods ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 721
Author(s):  
Dong-Heon Song ◽  
Youn-Kyung Ham ◽  
Sin-Woo Noh ◽  
Koo Bok Chin ◽  
Hyun-Wook Kim
Keyword(s):  
Ionic Strength ◽  
Ph Value ◽  
Protein Solubility ◽  
Textural Properties ◽  
Myofibrillar Protein ◽  
Cooking Loss ◽  
Technological Properties ◽  
Raw Meat

The objective of this study is to evaluate the effects of NaCl and KCl salting on technological properties of pre- and post-rigor chicken breasts at various ionic strengths. The following factorial arrangement was used: 2 salt types (NaCl and KCl) × 2 rigor statuses (pre- and post-rigor) × 4 ionic strengths (0.086, 0.171, 0.257, and 0.342). Hot-boned and ground chicken breasts were salted within 30 min postmortem after slaughter (pre-rigor salting) or 24 h postmortem (post-rigor salting) with varying concentrations of NaCl (0.50%, 1.00%, 1.50%, and 2.00%) or KCl (0.64%, 1.28%, 1.91%, and 2.55%) corresponding to the four ionic strengths. KCl caused higher pH value in salted chicken breasts than NaCl (p < 0.05). However, KCl decreased total and myofibrillar protein solubilities in post-rigor salted chicken breasts compared to NaCl (p < 0.05), but those were similar to pre-rigor chicken breasts, regardless of the salt type (p > 0.05). Different salt types had no significant impact on cooking loss and textural properties. This study shows that NaCl and KCl had similar effects on technological properties at the same ionic strength (within 0.342), but the use of KCl may have the possibility to decrease protein solubility, depending on rigor status of raw meat at the different salting time.

Influence of particle size and interfacial interactions on the physical and mechanical properties of particle-filled myofibrillar protein gels

RSC Advances ◽  
2015 ◽  
Vol 5 (75) ◽  
pp. 60723-60735 ◽  
Author(s):  
Andrew J. Gravelle ◽  
Shai Barbut ◽  
Alejandro G. Marangoni
Keyword(s):  
Mechanical Properties ◽  
Particle Size ◽  
Elastic Moduli ◽  
Physical And Mechanical Properties ◽  
Surface Effects ◽  
Myofibrillar Protein ◽  
Interfacial Interactions ◽  
Filler Size ◽  
Protein Gels

The mechanical properties of glass and wax particle-filled myofibrillar protein gels were characterized based on filler size and surface effects. Increases in elastic moduli were explained using established models describing particle-filled networks.

Effects of three treatments on protein structure and gel properties of Perccottus glenii myofibrillar protein

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Guochuan Jiang ◽  
Lili Tian ◽  
Ruifeng Hu ◽  
Hongrui Sun ◽  
Yuan Fu ◽  
...  
Keyword(s):  
Protein Structure ◽  
Hydrophobic Interactions ◽  
Sulfhydryl Group ◽  
Myofibrillar Protein ◽  
Control Group ◽  
Perccottus Glenii ◽  
Scanning Calorimetry ◽  
Gel Properties ◽  
Protein Gels ◽  
Group Protein

Abstract In order to improve Perccottus glenii myofibrillar protein (MP) gel properties, three treatments were evaluated: ultrasonic, transglutaminase (TGase) and combined ultrasonic-transglutaminase treatments. Combined ultrasonic-transglutaminase treatment altered protein structure and gel properties most dramatically. As compared with untreated control group protein, treated protein gels possessed decreased sulfhydryl group content and increases in water holding capacity, whiteness value and hydrophobic interactions that increased gel strength value by up to 3.79 times that of untreated protein gel. Protein structural and Differential scanning calorimetry (DSC) analyses revealed that combined ultrasonic-TGase treatment increased both protein thermal denaturation temperature and UV absorbance (as compared to control and other treatment groups) that supported formation of MP gels with desirable characteristics. These results provide a theoretical basis for development of superior MP gels to promote greater utilization of this fish protein resource by the food industry.

Sign in / Sign up

Export Citation Format

Share Document