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Effects of γ‐polyglutamic acid on the gelling properties and non‐covalent interactions of fish gelatin
Author(s) -
Hu ZiZi,
Sha XiaoMei,
Ye YunHua,
Xiao WanRong,
Tu ZongCai
Publication year - 2020
Publication title -
journal of texture studies
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.593
H-Index - 54
eISSN - 1745-4603
pISSN - 0022-4901
DOI - 10.1111/jtxs.12495
Subject(s) - gelatin , polyglutamic acid , hydrogen bond , covalent bond , molecule , chemistry , fish <actinopterygii> , polymer chemistry , chemical engineering , materials science , organic chemistry , biochemistry , fishery , engineering , biology
The effects of γ‐polyglutamic aid (γ‐PGA) on the gelling properties and non‐covalent interactions of fish gelatin were investigated. The gel strength and melting temperature of fish gelatin gradually increased, with increasing γ‐PGA concentration, although there was no significant change when the γ‐PGA concentration was greater than 0.04%. As the concentration of γ‐PGA increased, the electrostatic interaction of fish gelatin increased and the hydrophobic interaction between gelatin molecules decreased. The fish gelatin system was comprised of γ‐PGA concentrations of 0.04 and 0.06% showing a strong hydrogen bond. When the γ‐PGA concentration increased from 0 to 0.04%, more phenolic hydroxyl groups in the tyrosine residue tended to form hydrogen bonds with the protein. However, an additional increase in γ‐PGA concentration to 0.1% led to enhanced hydrogen bonding with water molecules. The results of this study showed that hydrogen bonds played an important role in improving the gelling properties of gelatin by γ‐PGA.