2014
DOI: 10.1016/j.fbio.2013.10.004
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Physicochemical properties of skin gelatin from farmed Amur sturgeon (Acipenser schrenckii) as influenced by acid pretreatment

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Cited by 55 publications
(38 citation statements)
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“…The β chain has a molecular weight of approximately 175 kDa, and the two α-chains were about 127 and 117 kDa, respectively. This is similar to what has been observed for other fish species [1,4,8,11]. In addition to the presence of a thick band corresponding to the β-components proteins, molecular weights higher than β-chains (γ-components) were observed for alkaline-acid gelatin, which may contribute to the different rheological properties.…”
Section: Sds-pagesupporting
confidence: 84%
See 1 more Smart Citation
“…The β chain has a molecular weight of approximately 175 kDa, and the two α-chains were about 127 and 117 kDa, respectively. This is similar to what has been observed for other fish species [1,4,8,11]. In addition to the presence of a thick band corresponding to the β-components proteins, molecular weights higher than β-chains (γ-components) were observed for alkaline-acid gelatin, which may contribute to the different rheological properties.…”
Section: Sds-pagesupporting
confidence: 84%
“…There have been many reports about the processing of gelatin from different kinds of seafood processing waste. Physicochemical, textural, rheological, and sensory properties of gelatin extracted from skins of channel catfish [5], sturgeon (Acipenser baeri) [6], cultured freshwater fish (live red tilapia (O. nilotica), walking catfish (C. batrachus), and striped catfish (P. sutchi fowler)) [7], unicorn leatherjacket (Aluterus monoceros) [8], tilapia (Oreochromis niloticus) [9], rainbow trout [10], and farmed Amur sturgeon (Acipenser schrenckii) [11] were studied as a function of various pretreatments. According to Ahmad and Benjakul [8] characteristics of gelatin from the skins of unicorn leatherjacket were correlated with the acid pretreatment.…”
Section: Introductionmentioning
confidence: 99%
“…With 314 increasing fish age, the cross-linking of collagen in skin can be enhanced [20]. Those functional groups and the secondary structure of gelatin [10]. All gelatin samples 324 showed similar spectra, which had the major peaks in amide region.…”
mentioning
confidence: 99%
“…This condition is used in the extraction process resulting in collagen solubility (Johnston-Banks, 1990). Acid pretreatment at different acid concentrations has an impact on yield and gel strength (Ahmed and Benjakul, 2011;Nikoo et al, 2014). An acid helps the release and dissolve of some proteins, fat and other components of collagen.…”
Section: Introductionmentioning
confidence: 99%