Microbial transglutaminase (MTGase) modified fish gelatin-γ-polyglutamic acid (γ-PGA): Rheological behavior, gelling properties, and structure

Food Chem. 2021 Jun 30:348:129093. doi: 10.1016/j.foodchem.2021.129093. Epub 2021 Jan 19.

Abstract

Fish gelatin (FG) has been extensively studied as a potential substitute for mammal gelatin. However, FG often requires different modification methods to change its physical and chemical properties due to its low gelling properties. Here, γ-polyglutamic acid (γ-PGA) and microbial transglutaminase (MTGase) were combined to modify FG to improve its gelling properties. The γ-PGA at 0.04% (w/v) and MTGase of different concentrations (0.02-0.08%, w/v) were used to modify FG, and the effects of complex modification on the gelling properties and structure of FG were studied. When the MTGase content was 0.08% (w/v), FG had the best gelling properties. In addition, the complex modification of MTGase and γ-PGA hindered the formation of the triple helix during the FG gel process. This reduced the gel rate, but significantly increased its viscosity. A schematic model was also proposed to illustrate the complex modifications of FG by MTGase and γ-PGA.

Keywords: Fish gelatin; Gelling properties; Microbialtransglutaminase; Rheological behavior; Structure; γ-polyglutamic acid.

MeSH terms

  • Animals
  • Fishes*
  • Gelatin / chemistry*
  • Gels
  • Polyglutamic Acid / analogs & derivatives*
  • Polyglutamic Acid / chemistry
  • Rheology*
  • Transglutaminases / chemistry*
  • Viscosity

Substances

  • Gels
  • poly(gamma-glutamic acid)
  • Polyglutamic Acid
  • Gelatin
  • Transglutaminases