2020
DOI: 10.1016/j.ultsonch.2020.105053
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Extraction of collagen-II with pepsin and ultrasound treatment from chicken sternal cartilage; physicochemical and functional properties

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Cited by 58 publications
(46 citation statements)
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“…6 , the EAI of oxhide gelatin samples increased after 0–400-W ultrasonication ( P < 0.05) and peaked with 300-W ultrasonication—indicating that 300-W ultrasonication improved the migration ability of oxhide gelatin from water to the oil–water interface. The results were consistent with those of Akram and Zhang [48] , who found that the EAI increased after ultrasonication.…”
Section: Resultssupporting
confidence: 92%
See 1 more Smart Citation
“…6 , the EAI of oxhide gelatin samples increased after 0–400-W ultrasonication ( P < 0.05) and peaked with 300-W ultrasonication—indicating that 300-W ultrasonication improved the migration ability of oxhide gelatin from water to the oil–water interface. The results were consistent with those of Akram and Zhang [48] , who found that the EAI increased after ultrasonication.…”
Section: Resultssupporting
confidence: 92%
“…In collagen, thermal stability differences are correlated with structure diversification [48] . The changes in DSC thermograms in our control and treated group are presented in Fig.…”
Section: Resultsmentioning
confidence: 99%
“…In the control samples of gizzards, at the initial time, the matrix surface is more uniform and visually denser (Figure 6-B) and the collagen fibers have a multi-layered aggregated structure (Figure 6(a2)-C). A similar structure of collagen was observed by Akram and Zhang [31] when studying the microstructure of collagen extracted from chicken sternal cartilage. The destruction of structural components under the influence of ultrasound has been noted by several authors, which confirms a similar effect of exposure to the fibrillar proteins of a complex of proteolytic enzymes of bacteria [31][32][33].…”
Section: Scanning Electron Microscopy (Sem)supporting
confidence: 78%
“…The sample was ≈100-fold concentrated by ultrafiltration on a Microcon Centrifugal filter unit with a 10 kDa molecular cut-off (MRCPRT010, Millipore, Burlington, MA, USA) to obtain the final collagen at 10 mg/mL. Collagen from GSCM and Type I collagen from the cattle dermis were isolated using a protocol described in [82], while Type II collagen was isolated from the tracheal cartilage by a protocol described in [83] omitting the use of pepsin. An amount of 10 µg of the proteins were diluted with an SDS-loading buffer supplemented with 100 mM DTT (20710, SERVA, Heidelberg, Germany) and heated at 95 • C for 5 min.…”
Section: Collagen Molecular Weight Estimation (Sds-page)mentioning
confidence: 99%