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Isolation and Comparative Study on the Characterization of Guanidine Hydrochloride Soluble Collagen and Pepsin Soluble Collagen from the Body of Surf Clam Shell (Coelomactra antiquata)
The aim of this study was to characterize the collagens from the body of surf clam shell (Coelomactra antiquata). Guanidine hydrochloride and pepsin were used to extract collagens. Guanidine hydrochloride soluble collagen (GSC) and pepsin soluble collagen (PSC) were separately isolated from the body...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6352192/ https://www.ncbi.nlm.nih.gov/pubmed/30609640 http://dx.doi.org/10.3390/foods8010011 |
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author | Wu, Jiulin Guo, Xiaoban Liu, Hui Chen, Li |
author_facet | Wu, Jiulin Guo, Xiaoban Liu, Hui Chen, Li |
author_sort | Wu, Jiulin |
collection | PubMed |
description | The aim of this study was to characterize the collagens from the body of surf clam shell (Coelomactra antiquata). Guanidine hydrochloride and pepsin were used to extract collagens. Guanidine hydrochloride soluble collagen (GSC) and pepsin soluble collagen (PSC) were separately isolated from the body of surf clam shell. Results showed that the moisture, protein, carbohydrate, and ash contents of the body of surf clam shell were 82.46%, 11.56%, 3.05%, and 2.38%, respectively, but the fat content was only 0.55%. The yields were 0.59% for GSC and 3.78% for PSC. Both GSC and PSC were composed of α(1) and α(2) chains and a β chain, however, GSC and PSC showed distinct differences from each other and the type I collagen from grass carp muscle on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). GSC and PSC contained glycine as the major amino acid and had imino acid of 150 and 155 residues/1000 residues, respectively. Fourier transform infrared spectroscopy (FTIR) spectra of GSC and PSC revealed the presence of a triple helix. The GSC appeared to have a dense sheet-like film linked by random-coiled filaments and PSC had fine globular filaments under scanning electron microscopy (SEM). The maximum transition temperature (T(max)) of GSC and PSC was 33.05 °C and 31.33 °C, respectively. These results provide valuable scientific information for the texture study and development of surf clam shell or other bivalve mollusks. |
format | Online Article Text |
id | pubmed-6352192 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-63521922019-02-01 Isolation and Comparative Study on the Characterization of Guanidine Hydrochloride Soluble Collagen and Pepsin Soluble Collagen from the Body of Surf Clam Shell (Coelomactra antiquata) Wu, Jiulin Guo, Xiaoban Liu, Hui Chen, Li Foods Article The aim of this study was to characterize the collagens from the body of surf clam shell (Coelomactra antiquata). Guanidine hydrochloride and pepsin were used to extract collagens. Guanidine hydrochloride soluble collagen (GSC) and pepsin soluble collagen (PSC) were separately isolated from the body of surf clam shell. Results showed that the moisture, protein, carbohydrate, and ash contents of the body of surf clam shell were 82.46%, 11.56%, 3.05%, and 2.38%, respectively, but the fat content was only 0.55%. The yields were 0.59% for GSC and 3.78% for PSC. Both GSC and PSC were composed of α(1) and α(2) chains and a β chain, however, GSC and PSC showed distinct differences from each other and the type I collagen from grass carp muscle on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). GSC and PSC contained glycine as the major amino acid and had imino acid of 150 and 155 residues/1000 residues, respectively. Fourier transform infrared spectroscopy (FTIR) spectra of GSC and PSC revealed the presence of a triple helix. The GSC appeared to have a dense sheet-like film linked by random-coiled filaments and PSC had fine globular filaments under scanning electron microscopy (SEM). The maximum transition temperature (T(max)) of GSC and PSC was 33.05 °C and 31.33 °C, respectively. These results provide valuable scientific information for the texture study and development of surf clam shell or other bivalve mollusks. MDPI 2019-01-01 /pmc/articles/PMC6352192/ /pubmed/30609640 http://dx.doi.org/10.3390/foods8010011 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Wu, Jiulin Guo, Xiaoban Liu, Hui Chen, Li Isolation and Comparative Study on the Characterization of Guanidine Hydrochloride Soluble Collagen and Pepsin Soluble Collagen from the Body of Surf Clam Shell (Coelomactra antiquata) |
title | Isolation and Comparative Study on the Characterization of Guanidine Hydrochloride Soluble Collagen and Pepsin Soluble Collagen from the Body of Surf Clam Shell (Coelomactra antiquata) |
title_full | Isolation and Comparative Study on the Characterization of Guanidine Hydrochloride Soluble Collagen and Pepsin Soluble Collagen from the Body of Surf Clam Shell (Coelomactra antiquata) |
title_fullStr | Isolation and Comparative Study on the Characterization of Guanidine Hydrochloride Soluble Collagen and Pepsin Soluble Collagen from the Body of Surf Clam Shell (Coelomactra antiquata) |
title_full_unstemmed | Isolation and Comparative Study on the Characterization of Guanidine Hydrochloride Soluble Collagen and Pepsin Soluble Collagen from the Body of Surf Clam Shell (Coelomactra antiquata) |
title_short | Isolation and Comparative Study on the Characterization of Guanidine Hydrochloride Soluble Collagen and Pepsin Soluble Collagen from the Body of Surf Clam Shell (Coelomactra antiquata) |
title_sort | isolation and comparative study on the characterization of guanidine hydrochloride soluble collagen and pepsin soluble collagen from the body of surf clam shell (coelomactra antiquata) |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6352192/ https://www.ncbi.nlm.nih.gov/pubmed/30609640 http://dx.doi.org/10.3390/foods8010011 |
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