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

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

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

Zi-Zi Hu et al. Food Chem. .

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.

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