Isolation and Characterization of Collagen and Antioxidant Collagen Peptides from Scales of Croceine Croaker (Pseudosciaena crocea)
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چکیده
منابع مشابه
Isolation and Characterization of Collagen and Antioxidant Collagen Peptides from Scales of Croceine Croaker (Pseudosciaena crocea)
Acid soluble collagen (ASC) from scales of croceine croaker (ASC-C) was successfully isolated with the yield of 0.37% ± 0.08% (dry weight basis), and characterized as type I collagen on the basis of amino acid analysis and electrophoretic pattern. The antioxidant hydrolysate of ASC-C (ACH) was prepared through a two-stage in vitro digestion (4-h trypsin followed by 4-h pepsin), and three antiox...
متن کاملPurification and Characterization of Antioxidant Peptides of Pseudosciaena crocea Protein Hydrolysates.
Two peptides with antioxidant activity were isolated from Pseudosciaena crocea proteins. Pseudosciaena crocea muscle was hydrolyzed with neutral protease to obtain Pseudosciaena crocea protein hydrolysates (PCPH). After ultrafiltration through molecular weight cut-off membranes of 10, 5 and 3 kDa and assessment of free radical scavenging ability, the fraction (PCPH-IV) with the highest antioxid...
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Acid-soluble collagen could be isolated from fish skin using acetic acid. In recent years, much attention has been paid to collagen from marine sources, mainly arising from the fact that there is no risk of contagious diseases. Moreover, by processing the fish, significant amounts of waste materials are produced which can be considered as a substitute for these collagen sources. Thunnus tonggol...
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This study proceeds to extract collagen from the skin of Rutilus kutum, one of the main and economical species of the Caspian Sea. Acid-soluble collagen (ASC) from the skin of R. kutum was extracted and characterized by SDS-PAGE, FTIR and UV spectrophotometry. Based on the data from the SDS-PAGE and the composition of amino acid, it was probable that the obtained collagen classified as type I...
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ژورنال
عنوان ژورنال: Marine Drugs
سال: 2013
ISSN: 1660-3397
DOI: 10.3390/md11114641