Characterization of Acid- and Pepsin-Soluble Collagens from the Cuticle of Perinereis nuntia (Savigny)

Characterization of Acid- and Pepsin-Soluble Collagens from the Cuticle of Perinereis nuntia... To extend the practical applications of collagen, alternatives to mammalian sources are needed. In this study, acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted from the cuticle of Perinereis nuntia (Savigny), and their physicochemical features and structures were examined. The yields of ASC and PSC were 3.89% and 6.74%, respectively. The glycine contents of both collagens accounted for approximately one-third of the total amino acid residues, and the sum totals of proline and hydroxyproline in ASC and PSC were 212 and 214 residues/1000 residues, respectively. However, the proline hydroxylation rates of ASC and PSC were 84.0% and 83.6%, respectively. The maximum absorption peaks of both ASC and PSC were detected at 233 nm. Zeta potential studies indicated that ASC and PSC have a net zero charge at pH 4.89 and 4.95, respectively. Fourier-transform infrared spectroscopy, circular dichroism, and X-ray diffraction confirmed the triple helical structure of the collagen. The denaturation temperatures (T d) of ASC and PSC were 36.5 °C and 33 °C, respectively. Moreover, the collagens appeared to be loose, fibrous, and porous by scanning electron microscopy. These results suggested that collagen from the cuticle of Perinereis nuntia (Savigny) has potential commercial applications in the food, nutraceutical, and pharmaceutical industries. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Food Biophysics Springer Journals

Characterization of Acid- and Pepsin-Soluble Collagens from the Cuticle of Perinereis nuntia (Savigny)

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Publisher
Springer US
Copyright
Copyright © 2018 by Springer Science+Business Media, LLC, part of Springer Nature
Subject
Chemistry; Food Science; Biological and Medical Physics, Biophysics; Analytical Chemistry
ISSN
1557-1858
eISSN
1557-1866
D.O.I.
10.1007/s11483-018-9533-8
Publisher site
See Article on Publisher Site

Abstract

To extend the practical applications of collagen, alternatives to mammalian sources are needed. In this study, acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted from the cuticle of Perinereis nuntia (Savigny), and their physicochemical features and structures were examined. The yields of ASC and PSC were 3.89% and 6.74%, respectively. The glycine contents of both collagens accounted for approximately one-third of the total amino acid residues, and the sum totals of proline and hydroxyproline in ASC and PSC were 212 and 214 residues/1000 residues, respectively. However, the proline hydroxylation rates of ASC and PSC were 84.0% and 83.6%, respectively. The maximum absorption peaks of both ASC and PSC were detected at 233 nm. Zeta potential studies indicated that ASC and PSC have a net zero charge at pH 4.89 and 4.95, respectively. Fourier-transform infrared spectroscopy, circular dichroism, and X-ray diffraction confirmed the triple helical structure of the collagen. The denaturation temperatures (T d) of ASC and PSC were 36.5 °C and 33 °C, respectively. Moreover, the collagens appeared to be loose, fibrous, and porous by scanning electron microscopy. These results suggested that collagen from the cuticle of Perinereis nuntia (Savigny) has potential commercial applications in the food, nutraceutical, and pharmaceutical industries.

Journal

Food BiophysicsSpringer Journals

Published: May 30, 2018

References

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