2021
DOI: 10.1016/j.tca.2021.178896
|View full text |Cite
|
Sign up to set email alerts
|

Hydrothermal shrinkage behavior of pigskin

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

0
2
0

Year Published

2021
2021
2024
2024

Publication Types

Select...
4

Relationship

0
4

Authors

Journals

citations
Cited by 4 publications
(4 citation statements)
references
References 31 publications
0
2
0
Order By: Relevance
“…It is generally believed that the overall influence of the longitudinal and transverse shrinkage of myofibrils caused by the denaturation of myofibrillar proteins on meat products was toughening, whereas the denaturation and degradation of collagen in connective tissue could cause meat to tenderizing (Dominguez‐Hernandez, Salaseviciene, & Ertbjerg, 2018). Collagen underwent protein denaturation (involving the rupture of hydrogen bonds in collagen triple helix), the increase in the diameter of fibrils (due to the water molecules entering the space of three α‐chains), and the shrinkage of collagen fibers (up to one‐quarter of their resting length) during hydrothermal treatment (50–70°C) (Miao et al, 2021; Tornberg, 2005). The thermal shrinkage of collagen fibers in intramuscular connective tissue contributed considerably to the increase of meat toughness (Latorre et al, 2019).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…It is generally believed that the overall influence of the longitudinal and transverse shrinkage of myofibrils caused by the denaturation of myofibrillar proteins on meat products was toughening, whereas the denaturation and degradation of collagen in connective tissue could cause meat to tenderizing (Dominguez‐Hernandez, Salaseviciene, & Ertbjerg, 2018). Collagen underwent protein denaturation (involving the rupture of hydrogen bonds in collagen triple helix), the increase in the diameter of fibrils (due to the water molecules entering the space of three α‐chains), and the shrinkage of collagen fibers (up to one‐quarter of their resting length) during hydrothermal treatment (50–70°C) (Miao et al, 2021; Tornberg, 2005). The thermal shrinkage of collagen fibers in intramuscular connective tissue contributed considerably to the increase of meat toughness (Latorre et al, 2019).…”
Section: Resultsmentioning
confidence: 99%
“…The collagen fiber in cooked chicken claw showed the disappearance of regular wave structure, a significant decrease in number, and an increase in fiber gap and fiber diameter (Figure 2b). It is speculated that the increase in fiber gap and diameter was due to the dissolution of collagen during stewing and the entry of water molecules into the collagen triple helix (Dong et al, 2019; Miao et al, 2021). The collagen fibers in chicken claw became short, loose, and disordered after thermal processing, which indicated that the collagen fibers were thermally decomposed (Figure 2c–f).…”
Section: Resultsmentioning
confidence: 99%
“…The first peak indicates the leather's denaturation temperature (Td), and the second peak indicates collagen network decomposition (Tm) (Valeika, 2020). The weakening of the mechanical stability of the leather occurs as the fiber network of the grown tissue undergoes degradation (Meyer et al, 2021;Miao et al, 2021). Cowhide and pigskin leather have similar chemical compositions as they are both animal skin types.…”
Section: Thermal Analysismentioning
confidence: 99%
“…Tannery has been an essential industry since ancient times (Liu et al, 2016). Chemically modifying animal skin results in more robust and more flexible materials, which can prevent further damage (Miao et al, 2021). These materials have been widely used in the fashion industry, footwear, automotive, technical materials, and other applications (Hermiyati et al, 2017;Meyer et al, 2021).…”
Section: Introductionmentioning
confidence: 99%