Isolation and characterization of pepsin-solubilized collagen from the integument of sea cucumber (Stichopus vastus)

BACKGROUND: Sea cucumber (Stichopus vastus) is considered an underutilized resource, since only its stomach and intestines are eaten raw as salad in a few countries and the remaining parts, especially the integument rich in collagen, is discarded.Hence a valuable by-product having potential nutrac...

Full description

Bibliographic Details
Main Authors: Zainul Abedin, Md, A Karim, Alias, Ahmed, Faiyaz, A Latiff, Aishah, Chee-Yuen, Gan, Che Ghazali, Farid, Sarker, Md. Zaidul Islam
Format: Article
Language:English
Published: John Wiley & Sons 2012
Subjects:
Online Access:http://irep.iium.edu.my/27817/
http://irep.iium.edu.my/27817/
http://irep.iium.edu.my/27817/
http://irep.iium.edu.my/27817/1/JSFA_Zainul.pdf
id iium-27817
recordtype eprints
spelling iium-278172012-12-26T05:57:19Z http://irep.iium.edu.my/27817/ Isolation and characterization of pepsin-solubilized collagen from the integument of sea cucumber (Stichopus vastus) Zainul Abedin, Md A Karim, Alias Ahmed, Faiyaz A Latiff, Aishah Chee-Yuen, Gan Che Ghazali, Farid Sarker, Md. Zaidul Islam QD Chemistry BACKGROUND: Sea cucumber (Stichopus vastus) is considered an underutilized resource, since only its stomach and intestines are eaten raw as salad in a few countries and the remaining parts, especially the integument rich in collagen, is discarded.Hence a valuable by-product having potential nutraceutical and pharmaceutical applications is wasted. In the present investigation, pepsin-solubilized collagen (PSC) from the integument of S. vastus was isolated, purified and characterized. RESULTS: Sodium dodecyl sulfate–polyacrylamide gel electrophoretic analysis showed that the purified collagen was of type I, consisting of three α1 chains of approximately 122 kDa each. The peptide map of PSC digested by V8 protease was different from that of calf skin type I collagen. Fourier transform infrared spectroscopy revealed that the triple helical structure was well preserved in isolated collagen. The denaturation temperature of PSC was 21.23 ◦C and showed good gel-forming capability at pH 6.5 and 300 mmol L−1 NaCl. CONCLUSION: It is inferred that the collagen isolated from S. vastus integument has potential for use as an alternative to land-based mammalian collagen in food, nutraceuticals and pharmaceutical industries. �c 2012 Society of Chemical Industry Keywords: integument collagen; sea cucumber; gel John Wiley & Sons 2012-08-30 Article PeerReviewed application/pdf en cc_by_nd http://irep.iium.edu.my/27817/1/JSFA_Zainul.pdf Zainul Abedin, Md and A Karim, Alias and Ahmed, Faiyaz and A Latiff, Aishah and Chee-Yuen, Gan and Che Ghazali, Farid and Sarker, Md. Zaidul Islam (2012) Isolation and characterization of pepsin-solubilized collagen from the integument of sea cucumber (Stichopus vastus). Journal of the Science of Food and Agriculture. ISSN 1097-0010 (Online) http://onlinelibrary.wiley.com/doi/10.1002/jsfa.5854/abstract 10.1002/jsfa.5854
repository_type Digital Repository
institution_category Local University
institution International Islamic University Malaysia
building IIUM Repository
collection Online Access
language English
topic QD Chemistry
spellingShingle QD Chemistry
Zainul Abedin, Md
A Karim, Alias
Ahmed, Faiyaz
A Latiff, Aishah
Chee-Yuen, Gan
Che Ghazali, Farid
Sarker, Md. Zaidul Islam
Isolation and characterization of pepsin-solubilized collagen from the integument of sea cucumber (Stichopus vastus)
description BACKGROUND: Sea cucumber (Stichopus vastus) is considered an underutilized resource, since only its stomach and intestines are eaten raw as salad in a few countries and the remaining parts, especially the integument rich in collagen, is discarded.Hence a valuable by-product having potential nutraceutical and pharmaceutical applications is wasted. In the present investigation, pepsin-solubilized collagen (PSC) from the integument of S. vastus was isolated, purified and characterized. RESULTS: Sodium dodecyl sulfate–polyacrylamide gel electrophoretic analysis showed that the purified collagen was of type I, consisting of three α1 chains of approximately 122 kDa each. The peptide map of PSC digested by V8 protease was different from that of calf skin type I collagen. Fourier transform infrared spectroscopy revealed that the triple helical structure was well preserved in isolated collagen. The denaturation temperature of PSC was 21.23 ◦C and showed good gel-forming capability at pH 6.5 and 300 mmol L−1 NaCl. CONCLUSION: It is inferred that the collagen isolated from S. vastus integument has potential for use as an alternative to land-based mammalian collagen in food, nutraceuticals and pharmaceutical industries. �c 2012 Society of Chemical Industry Keywords: integument collagen; sea cucumber; gel
format Article
author Zainul Abedin, Md
A Karim, Alias
Ahmed, Faiyaz
A Latiff, Aishah
Chee-Yuen, Gan
Che Ghazali, Farid
Sarker, Md. Zaidul Islam
author_facet Zainul Abedin, Md
A Karim, Alias
Ahmed, Faiyaz
A Latiff, Aishah
Chee-Yuen, Gan
Che Ghazali, Farid
Sarker, Md. Zaidul Islam
author_sort Zainul Abedin, Md
title Isolation and characterization of pepsin-solubilized collagen from the integument of sea cucumber (Stichopus vastus)
title_short Isolation and characterization of pepsin-solubilized collagen from the integument of sea cucumber (Stichopus vastus)
title_full Isolation and characterization of pepsin-solubilized collagen from the integument of sea cucumber (Stichopus vastus)
title_fullStr Isolation and characterization of pepsin-solubilized collagen from the integument of sea cucumber (Stichopus vastus)
title_full_unstemmed Isolation and characterization of pepsin-solubilized collagen from the integument of sea cucumber (Stichopus vastus)
title_sort isolation and characterization of pepsin-solubilized collagen from the integument of sea cucumber (stichopus vastus)
publisher John Wiley & Sons
publishDate 2012
url http://irep.iium.edu.my/27817/
http://irep.iium.edu.my/27817/
http://irep.iium.edu.my/27817/
http://irep.iium.edu.my/27817/1/JSFA_Zainul.pdf
first_indexed 2023-09-18T20:41:13Z
last_indexed 2023-09-18T20:41:13Z
_version_ 1777409377875001344