Effect of high pressure processing on the gel properties of salt-soluble meat protein containing CaCl2 and κ-carrageenan

Meat Sci. 2013 Sep;95(1):22-6. doi: 10.1016/j.meatsci.2013.04.025. Epub 2013 Apr 16.

Abstract

The effects of high pressure processing (HPP) on the water-binding capacity and texture profile (TPA) of salt-soluble meat protein (SSMP) containing 0.2% CaCl2 and 0.6% κ-carrageenan (SSMP-CK) gels were investigated. The results showed that 300-400 MPa improved water-binding capacity and decreased TPA parameters of SSMP-CK gels (P<0.05), while 100 MPa could increase hardness and chewiness of the gels. The thermal transition temperature peak for the myosin head (Tpeak1) of SSMP disappeared on addition of CaCl2 and κ-carrageenan. 300 MPa produced a new peak, and caused a shift of the NH-stretching left peak and amide I and the disappearance of NH-stretching right peak. The destruction of network structure and the weakening of molecular interaction within the pressurized gels could result in the decrease of TPA parameters. Thus gelling properties could be modified by HPP, κ-carrageenan and Ca(2+). It is of interest to develop low-fat and sodium-reduced meat products.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcium Chloride / chemistry
  • Calorimetry, Differential Scanning
  • Carrageenan / chemistry*
  • Cooking
  • Gels / chemistry*
  • Hardness
  • Meat Products / analysis*
  • Microscopy, Confocal
  • Myosins / chemistry
  • Polysaccharides / chemistry
  • Pressure*
  • Proteins / chemistry
  • Salts / chemistry
  • Spectroscopy, Fourier Transform Infrared
  • Water / chemistry

Substances

  • Gels
  • Polysaccharides
  • Proteins
  • Salts
  • Water
  • Carrageenan
  • Myosins
  • Calcium Chloride