Gel properties of myofibrillar protein as affected by gelatinization and retrogradation behaviors of modified starches with different crosslinking and acetylation degrees

In meat processing, changes in the myofibrillar protein (MP) structure can affect the quality of meat products. High hydrostatic pressure (HHP) has been widely utilized to change the conformational structure (secondary, tertiary and quaternary structure) of MP so as to improve the quality of meat products. However, a systematic summary of the relationship between the conformational structure (secondary and tertiary structure) changes in MP, gel properties and product quality under HHP is lacking. Hence, this review provides a comprehensive summary of the changes in the conformational structure and gel properties of MP under HHP and discusses the mechanism based on previous studies and recent progress. The relationship between the spatial structure of MP and meat texture under HHP is also explored. Finally, we discuss considerations regarding ways to make HHP an effective strategy in future meat manufacturing.

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Effect of emulsifying stability of myofibrillar protein on the gel properties of emulsified surimi gel

Food Science & Nutrition ◽

10.1002/fsn3.663 ◽

2018 ◽

Vol 6 (5) ◽

pp. 1229-1237 ◽

Cited By ~ 7

Author(s):

Yuanpei Gao ◽

Hideto Fukushima ◽

Shanggui Deng ◽

Ru Jia ◽

Kazufumi Osako ◽

...

Keyword(s):

Myofibrillar Protein ◽

Gel Properties ◽

Surimi Gel

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Gel properties of grass carp myofibrillar protein modified by low-frequency magnetic field during two-stage water bath heating

Food Hydrocolloids ◽

10.1016/j.foodhyd.2020.105920 ◽

2020 ◽

Vol 107 ◽

pp. 105920 ◽

Cited By ~ 2

Author(s):

Limei Wang ◽

Minquan Xia ◽

Yuanhua Zhou ◽

Xian Wang ◽

Jing Ma ◽

...

Keyword(s):

Magnetic Field ◽

Grass Carp ◽

Low Frequency ◽

Myofibrillar Protein ◽

Water Bath ◽

Two Stage ◽

Gel Properties ◽

Frequency Magnetic Field ◽

Water Bath Heating

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

International Journal of Food Engineering ◽

10.1515/ijfe-2021-0190 ◽

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.

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