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Isolation and characterization of collagen from the cartilage of Amur sturgeon (Acipenser schrenckii)

Paper ID Volume ID Publish Year Pages File Format Full-Text
34800 45048 2014 6 PDF Available
Title
Isolation and characterization of collagen from the cartilage of Amur sturgeon (Acipenser schrenckii)
Abstract

•The collagen in Amur sturgeon cartilage was isolated by salt, acid and pepsin.•The collagen appeared to be dense sheet-like film linked by filaments under SEM.•The thermal stability of collagen was high assessed by CD and DSC.•The molecular species was mainly type I and II shown by SDS-PAGE.•The considerable differences in secondary structure were found from FTIR.

The collagen in Amur sturgeon cartilage was isolated using sodium chloride (salt-solubilized collagen, SSC, 2.18%), followed by acetic acid (acid-solubilized collagen, ASC, 27.04%) and then pepsin (pepsin-solubilized collagen, PSC, 55.92%). These collagens appeared to be dense sheet-like film linked by random-coiled filaments under SEM. The denaturation and melting temperatures of PSC (35.71 and 123.90 °C) were significantly higher than SSC (32.64 and 114.51 °C) and ASC (32.98 and 120.72 °C) assessed by circular dichroism and differential scanning calorimetry, which could be attributed to its high imino acid content (22.57%) and degree of hydroxylation (47.29%). Electrophoresis pattern showed that the SSC and ASC were type I collagen, while PSC was predominantly type II collagen along with other minor types. Infrared spectra confirmed their triple helical structure, and indicated more hydrogen bonding in ASC and more intermolecular crosslinks in PSC. These results provide some basis for their large-scale production and further application as alternatives to mammalian collagen.

Keywords
Amur sturgeon (Acipenser schrenckii); Collagen; Cartilage; Isolation; Characterization
First Page Preview
Isolation and characterization of collagen from the cartilage of Amur sturgeon (Acipenser schrenckii)
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 49, Issue 2, February 2014, Pages 318–323
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering