Exploring the potential of fibrinogen hydrolysates as enhancers for myofibrillar protein gelation: Insights into molecular assembly behavior.

Food Chem

Key Laboratory of Geriatric Nutrition and Health (Beijing Technology and Business University), Ministry of Education, 100048 Beijing, China; Beijing Engineering and Technology Research Center of Food Additives, School of Food and Health, Beijing Technology and Business University, 100048 Beijing, China. Electronic address:

Published: February 2025

AI Article Synopsis

  • - This study investigated how pig blood fibrinogen hydrolysates, processed with trypsin and flavorzyme, can enhance the quality of myofibrillar protein gels typically used in meat products, focusing on improving gel strength and reducing water loss.
  • - By varying the amounts of fibrinogen hydrolysates in the protein gels, researchers observed better textural properties, increased water-holding capacity, and changes in the internal structure of the gels as seen through scanning and atomic force microscopy.
  • - The research also found shifts in the secondary structure of proteins during gel formation and highlighted the role of hydrophobic interactions and disulfide bonds in strengthening the gels, suggesting the potential for using fibrinogen hydrolysates to boost the quality

Article Abstract

This study explored the use of pig blood fibrinogen hydrolysates, enzymatically hydrolyzed with trypsin and flavorzyme, to enhance myofibrillar protein gels, addressing issues like poor gel strength and water loss in meat products. By incorporating varying concentrations of fibrinogen hydrolysates into myofibrillar proteins, heat-induced gels were prepared. The composite gels showed improved textural properties, rheological characteristics and water-holding capacity. Scanning electron microscopy and atomic force microscopy analyses revealed a uniform, dense surface and an orderly internal structure in the composite gels. The study also noted decreased α-helix and random coil and increased β-sheet and β-turn contents, indicating a more ordered secondary structure. Hydrophobic interactions and disulfide bonds were identified as key factors in enhancing gelation, and a model was proposed to explain these molecular effects. This research demonstrates a potential of fibrinogen hydrolysates to improve quality and structure of myofibrillar protein gels designed for high-quality meat products.

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http://dx.doi.org/10.1016/j.foodchem.2024.141587DOI Listing

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Exploring the potential of fibrinogen hydrolysates as enhancers for myofibrillar protein gelation: Insights into molecular assembly behavior.

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February 2025

Key Laboratory of Geriatric Nutrition and Health (Beijing Technology and Business University), Ministry of Education, 100048 Beijing, China; Beijing Engineering and Technology Research Center of Food Additives, School of Food and Health, Beijing Technology and Business University, 100048 Beijing, China. Electronic address:

Article Synopsis
  • - This study investigated how pig blood fibrinogen hydrolysates, processed with trypsin and flavorzyme, can enhance the quality of myofibrillar protein gels typically used in meat products, focusing on improving gel strength and reducing water loss.
  • - By varying the amounts of fibrinogen hydrolysates in the protein gels, researchers observed better textural properties, increased water-holding capacity, and changes in the internal structure of the gels as seen through scanning and atomic force microscopy.
  • - The research also found shifts in the secondary structure of proteins during gel formation and highlighted the role of hydrophobic interactions and disulfide bonds in strengthening the gels, suggesting the potential for using fibrinogen hydrolysates to boost the quality
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