Microbial transglutaminase (MTGase) modified fish gelatin-γ-polyglutamic acid (γ-PGA): Rheological behavior, gelling properties, and structure
Microbial transglutaminase (MTGase) modified fish gelatin-γ-polyglutamic acid (γ-PGA): Rheological behavior, gelling properties, and structure
复制标题
微生物转谷氨酰胺酶 (MTGase) 改性鱼明胶-γ-聚谷氨酸 (γ-PGA)：流变行为、胶凝特性和结构
DOI：
10.1016/j.foodchem.2021.129093
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发表时间：
2021-01-24
期刊：
影响因子：
8.8
通讯作者：
Tu, Zong-Cai
中科院分区：
文献类型：
--
作者：
Hu, Zi-Zi;Sha, Xiao-Mei;Tu, Zong-Cai
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, gamma-polyglutamic acid (gamma-PGA) and microbial transglutaminase (MTGase) were combined to modify FG to improve its gelling properties. The gamma-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 gamma-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 gamma-PGA.
