Modulating the aggregation of myofibrillar protein to alleviate the textural deterioration of protein gels at high temperature: The effect of hydrophobic interactions

2021 ◽  
Vol 341 ◽  
pp. 128274
Author(s):  
Bo Chen ◽  
Jie Guo ◽  
Yong Xie ◽  
Kai Zhou ◽  
Peijun Li ◽  
...  
2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Guochuan Jiang ◽  
Lili Tian ◽  
Ruifeng Hu ◽  
Hongrui Sun ◽  
Yuan Fu ◽  
...  

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.


2020 ◽  
Vol 330 ◽  
pp. 127186
Author(s):  
Bo Chen ◽  
Kai Zhou ◽  
Yu Wang ◽  
Yong Xie ◽  
Zhaoming Wang ◽  
...  

2017 ◽  
Vol 1 (1) ◽  
pp. 109 ◽  
Author(s):  
Andrew J. Gravelle ◽  
Alejandro G. Marangoni ◽  
Shai Barbut

1995 ◽  
Vol 62 (3) ◽  
pp. 479-489 ◽  
Author(s):  
Sylvie Marchesseau ◽  
Jean-Louis Cuq

SummaryIn order to predict the oozing susceptibility of heat-induced milk protein gels such as processed cheeses during storage, ultracentrifugation forces are required to accelerate the expulsion of water from the gel structure. Two predictive methods have been tested. Direct ultracentrifugation of processed cheese was used to study effects of centrifugal compression on the water-holding ability. The water release with optimal parameters (time, temperature and ultracentrifugation force) from a freshly manufactured processed cheese was correlated with visual assessment of oozing after 6 months storage. A second method was based on the susceptibility of gelled proteins to resist the dissociating action of solutions of chemical agents such as SDS, urea, EDTA and 2-mercaptoethanol. Most of the protein sedimented by ultracentrifugation in the presence of SDS represented that still in complexed form. This correlated with optimal water binding by the processed cheese. Response-surface methods, used to optimize the ultracentrifugation variables and the composition of the dissociation solutions, showed that the dissociation test was best with a dispersion of processed cheese in SDS solution (10 g/l) at a ratio of 1:6 (w/v) at 20°C, ultracentrifuged at 86000 g and 20°C for 25 min. Analysis of processed cheese cooked at 115°C and then dissociated in different solutions showed various protein–protein interactions in the gel network, whereas hydrophobic interactions were the most important stabilizers of the protein matrix of cheese cooked at higher temperature.


RSC Advances ◽  
2015 ◽  
Vol 5 (75) ◽  
pp. 60723-60735 ◽  
Author(s):  
Andrew J. Gravelle ◽  
Shai Barbut ◽  
Alejandro G. Marangoni

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.


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