Myofibrillar protein gel properties are influenced by oxygen concentration in modified atmosphere packaged minced beef

Ultrasonic freezing (UF) is an effective method to increase the freezing speed and improve the quality of frozen food. The effect of UF on myofibrillar protein oxidation and gel properties of common carp (Cyprinus carpio) during frozen storage were investigated with air freezing (AF) and immersion freezing (IF) as controls. The results showed that the carbonyl and dityrosine content of UF samples were lower and the free amine content was higher than those of AF and IF samples during frozen storage indicating that UF inhibited protein oxidation caused by frozen storage. The particle size of UF myofibrillar protein was the smallest among all the groups indicating that UF inhibited the protein aggregation. The UF sample had higher G’, G” value, gel strength and gel water holding capacity than AF and IF groups showing that UF reduced the loss of protein gel properties. The gel microstructure showed that UF protein gel was characterized by smaller and finer pores than other samples, which further proves that UF inhibited loss of gel properties during frozen storage. The UF sample had shorter T2 transition time than other samples demonstrating that UF decreased the mobility of water. In general, UF is an effective method to reduce protein oxidation and gel properties loss caused by frozen storage.

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Effects of Transgluninase and GDL on Gel Properties of Chicken Myofibrillar Proteins

Advanced Materials Research ◽

10.4028/www.scientific.net/amr.554-556.1148 ◽

2012 ◽

Vol 554-556 ◽

pp. 1148-1151

Author(s):

Kun Sheng Zhang ◽

Yun Xia Ren ◽

Na Liu ◽

Yong Qing Tao

Keyword(s):

Protein Concentration ◽

Myofibrillar Protein ◽

Gel Strength ◽

Myofibrillar Proteins ◽

Optimum Conditions ◽

Gel Properties ◽

Protein Gel ◽

Nacl Concentration

Myofibrillar protein gel properties were studied. Based on which Box-Benhnken center-united experiment was designed for optimization of ratio scheme for gelation strength. The optimum conditions for best gel strength were found to the transgluninase 0.37% of myofibrillar proteins, GDL 1.19%, in 0.88mol/L NaCl concentration at pH 5.96 to form 40mg/ml protein concentration solution. The gel strength was 316.953g. The study showed that transgluninase and GDL could interact significantly in improving gel strength (P <0.01).

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Inhibitory effect of microwave heating on cathepsin l-induced degradation of myofibrillar protein gel

Food Chemistry ◽

10.1016/j.foodchem.2021.129745 ◽

2021 ◽

Vol 357 ◽

pp. 129745

Author(s):

Qian Wang ◽

Xidong Jiao ◽

Bowen Yan ◽

Linglu Meng ◽

Hongwei Cao ◽

...

Keyword(s):

Microwave Heating ◽

Cathepsin L ◽

Inhibitory Effect ◽

Myofibrillar Protein ◽

Protein Gel

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Effects of the structure and gel properties of myofibrillar protein on chicken breast quality treated with ultrasound-assisted potassium alginate

Food Chemistry ◽

10.1016/j.foodchem.2021.129873 ◽

2021 ◽

pp. 129873

Author(s):

Haibo Shi ◽

Ting Zhou ◽

Xin Wang ◽

Ye Zou ◽

Daoying Wang ◽

...

Keyword(s):

Myofibrillar Protein ◽

Chicken Breast ◽

Gel Properties ◽

Ultrasound Assisted

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Evaluation of Acid-treated Fish Sarcoplasmic Proteins on Physicochemical and Rheological Characteristics of Pork Myofibrillar Protein Gel Mediated by Microbial Transglutaminase

Korean Journal for Food Science of Animal Resources ◽

10.5851/kosfa.2015.35.1.50 ◽

2015 ◽

Vol 35 (1) ◽

pp. 50-57 ◽

Cited By ~ 4

Author(s):

Bung-Orn Hemung ◽

Koo Bok Chin

Keyword(s):

Myofibrillar Protein ◽

Microbial Transglutaminase ◽

Rheological Characteristics ◽

Sarcoplasmic Proteins ◽

Protein Gel ◽

Treated Fish

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Effects of High Hydrostatic Pressure on the Conformational Structure and Gel Properties of Myofibrillar Protein and Meat Quality: A Review

Foods ◽

10.3390/foods10081872 ◽

2021 ◽

Vol 10 (8) ◽

pp. 1872

Author(s):

Huipeng Liu ◽

Yiyuan Xu ◽

Shuyu Zu ◽

Xuee Wu ◽

Aimin Shi ◽

...

Keyword(s):

Hydrostatic Pressure ◽

High Hydrostatic Pressure ◽

Tertiary Structure ◽

Quaternary Structure ◽

Meat Products ◽

Myofibrillar Protein ◽

Conformational Structure ◽

Gel Properties ◽

The Relationship

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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