Abstract

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.

Highlights

  • Protein is one of the most important elements of nutrition for humans, providing energy and essential amino acids

  • A new processing technology was developed in the recent years known as high hydrostatic pressure (HHP), which shows the possibility for achieving better processing and preservation of meat, poultry and seafood [5]

  • The hardness, springiness, chewiness and cohesiveness have significantly increased above 400 MPa.The texture profiles of eel balls showed a negative relationship with the α-helix, β-sheet and SH content

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Summary

Introduction

Protein is one of the most important elements of nutrition for humans, providing energy and essential amino acids. Safety and natural flavors with no additives (i.e., preservatives and moisturizers) are their primary requirements [4] Based on this demand, a new processing technology was developed in the recent years known as high hydrostatic pressure (HHP), which shows the possibility for achieving better processing and preservation of meat, poultry and seafood [5]. The relatively high protein content (i.e., 16–40%) in meat plays an important role in food flavor, nutrition, and health [8,9]. HHP can dissociate the non-covalent, ionic, hydrophobic, and hydrogen bonds to change the secondary, tertiary, and quaternary structure of MP [22]. HHP induces variable alterations on protein conformational structures depending on the applied pressure level [26].

Secondary Structure
Tertiary and Quaternary Structure
Results
Effect of HHP on Meat Quality
Conclusions and Prospect
Full Text
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