2020
DOI: 10.1111/ijfs.14487
|View full text |Cite
|
Sign up to set email alerts
|

Improving the physical properties of fish gelatin by high hydrostatic pressure (HHP) and ultrasonication (US)

Abstract: Summary In this study, it was aimed to improve the physical properties of fish gelatin by using high hydrostatic pressure (HHP) and ultrasonication (US). Gelatin solutions were exposed to different pressures and ultrasonication separately and gelled afterwards. The physicochemical measurements based on gel strength, turbidity and rheology experiments showed that HHP treatment on fish and bovine gelatin stabilized the gelatin network by organising the structure and reducing the free volume. Both processing meth… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

0
8
0

Year Published

2021
2021
2025
2025

Publication Types

Select...
8

Relationship

0
8

Authors

Journals

citations
Cited by 13 publications
(8 citation statements)
references
References 27 publications
0
8
0
Order By: Relevance
“…Gelatine is a denatured form of collagen but differs from collagen in its chemical composition (Sun et al ., 2021), with origins from bone and skin collagen of bovine, porcine, rabbit, camel, fish, etc. (Ghaderi, Hosseini, Keyvani, & Gómez‐Guillén, 2019; Benbettaieb, Mahfoudh, Moundanga, Brachais, Chambin, & Debeaufort, 2020; Dai et al ., 2020; Huang, Tu, Sha, Wang, Hu, & Hu, 2020; Sezer, Okur, Oztop, & Alpas, 2020; Hosseini et al ., 2021). Gelatine origin could lead to different number of triple‐helixes structure, solubility, interactions nature, variable contents of proteins, peptides and nucleic acids (Duconseille, Astruc, Quintana, Meersman, & Sante‐Lhoutellier, 2015).…”
Section: Affecting Factorsmentioning
confidence: 99%
“…Gelatine is a denatured form of collagen but differs from collagen in its chemical composition (Sun et al ., 2021), with origins from bone and skin collagen of bovine, porcine, rabbit, camel, fish, etc. (Ghaderi, Hosseini, Keyvani, & Gómez‐Guillén, 2019; Benbettaieb, Mahfoudh, Moundanga, Brachais, Chambin, & Debeaufort, 2020; Dai et al ., 2020; Huang, Tu, Sha, Wang, Hu, & Hu, 2020; Sezer, Okur, Oztop, & Alpas, 2020; Hosseini et al ., 2021). Gelatine origin could lead to different number of triple‐helixes structure, solubility, interactions nature, variable contents of proteins, peptides and nucleic acids (Duconseille, Astruc, Quintana, Meersman, & Sante‐Lhoutellier, 2015).…”
Section: Affecting Factorsmentioning
confidence: 99%
“…Turbidity increases when the process is carried out at a high temperature for a long time as a result of random protein aggregation and also smaller peptides or proteins that hinder the transmission of light 23,41 . In addition to the clarification process, non‐thermal processing methods such as high pressure and ultrasound have been proposed to reduce protein aggregation that causes turbidity in gelatin solution by disrupting hydrophobic and electrostatic interactions, resulting in conformational changes in the protein structure 42 …”
Section: Resultsmentioning
confidence: 99%
“…23,41 In addition to the clarification process, non-thermal processing methods such as high pressure and ultrasound have been proposed to reduce protein aggregation that causes turbidity in gelatin solution by disrupting hydrophobic and electrostatic interactions, resulting in conformational changes in the protein structure. 42 Color Table 3 shows the color parameters of gelatin extracted from turkey skin at various extraction temperatures and times, expressed as L, a, and b. The samples with the highest L value (lighter color) were extracted at 70 °C for 9 h. Higher extraction temperature and time were found to have a significant effect on sample L values (P < 0.05).…”
Section: Turbiditymentioning
confidence: 99%
“…This pressure provokes the deformation of cells and the damage of their membranes and protein structures, thus allowing for the penetration of the solvent within cells and increasing the transfer rate of its intracellular components [73]. HHP processing, also known as "cold pasteurization", has been traditionally used in the food industry to reduce the microbial charge and improve the shelf-life of different food systems [74]. However, in recent years, HHP processing has been extended to other innovative uses, such as the selective recovery of phenolic compounds, polysaccharides, fats, and proteins, among others [75][76][77].…”
Section: High Hydrostatic Pressure-assisted Extractionmentioning
confidence: 99%