2019
DOI: 10.1111/jtxs.12495
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Effects of γ‐polyglutamic acid on the gelling properties and non‐covalent interactions of fish gelatin

Abstract: 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 fis… Show more

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Cited by 19 publications
(10 citation statements)
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“…The physicochemical, functional, technological, and sensory attributes of gelatin prepared from beef, pork, and/or fish are determined by the method of preparation used as well as the intrinsic character of the collagen from the respective sources (Hu et al., 2020). There are two approaches generally adopted to prepare gelatin commercially.…”
Section: Strategies To Improve the Functionality Of Fish Gelatinmentioning
confidence: 99%
“…The physicochemical, functional, technological, and sensory attributes of gelatin prepared from beef, pork, and/or fish are determined by the method of preparation used as well as the intrinsic character of the collagen from the respective sources (Hu et al., 2020). There are two approaches generally adopted to prepare gelatin commercially.…”
Section: Strategies To Improve the Functionality Of Fish Gelatinmentioning
confidence: 99%
“…This can be attributed to the formation of carrageenan double helices firstly, followed by their aggregation and finally forming a strong gel network structure with strong mechanical strength [ 24 ]. Theoretically, the anion-polysaccharide could interact with polymers by electrostatic and hydrogen bonds, improving the strength of gel structure [ 25 , 26 ]. However, AG addition decreased the plateau constant values of G′ and G″ compared with control sample ( Figure 1 ), suggesting that AG decreased the mechanical strength of ink samples.…”
Section: Resultsmentioning
confidence: 99%
“…The variations of the TPA parameters of all FG samples may also because of the differences of alcohol solutions. For example, the effects of ethanol on protein denaturation becomes weaker with the number of OH increased due to the increase of hydrogen bonds (Romero, Lozano, Sancho, & Giraldo, 2007), which is the non‐covalent source dominating the stability of native protein structure (Hu, Sha, Ye, Xiao, & Tu, 2020). Consequently, it can be concluded here that when FG was pretreated with low concentrations of alcohol solutions, FG could still remain higher gel strength and hardness even after removing the alcohol solutions.…”
Section: Resultsmentioning
confidence: 99%