Extraction and characterization of collagen and gelatin from body wall of sea cucumbers stichopus horrens and holothuria arenicola

Background: Marine invertebrates, including sponges, molluscs, jellyfish, mussels, and sea cucumbers, are abundant sources of high-quality collagen and offer advantages such as availability, ease of processing, lower inflammatory response, and good metabolic compatibility. Approximately 70% of the t...

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Main Authors: Noora Barzkar, Gilan Attaran-Fariman, Ali Taheri, Balu Alagar Venmathi Maran
Format: Article
Language:English
Published: PeerJ, Inc. 2024
Subjects:
Online Access:https://eprints.ums.edu.my/id/eprint/42890/1/FULL%20TEXT.pdf
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author Noora Barzkar
Gilan Attaran-Fariman
Ali Taheri
Balu Alagar Venmathi Maran
author_facet Noora Barzkar
Gilan Attaran-Fariman
Ali Taheri
Balu Alagar Venmathi Maran
author_sort Noora Barzkar
collection UMS
description Background: Marine invertebrates, including sponges, molluscs, jellyfish, mussels, and sea cucumbers, are abundant sources of high-quality collagen and offer advantages such as availability, ease of processing, lower inflammatory response, and good metabolic compatibility. Approximately 70% of the total protein in the body wall of sea cucumbers is collagen. Gelatin is a water-soluble protein produced from heat-denatured collagen and has various industrial applications. Methods: Pepsin-solubilized collagen was extracted from the body wall of two sea cucumber Stichopus horrens and Holothuria arenicola, species found in the Oman Sea and characterized with SDS-PAGE and amino acid composition. Then gelatin was extracted from pepsin-solubilized collagen of S. horrens and some rheological properties were measured. Results: Amino acid composition and SDS-PAGE analysis showed that the collagen from both species was type I, with one a1 chain and β chains, with molecular weights of 125 and 250 kDa, respectively. Glycine was the most abundant amino acid in the collagen from both sea cucumber species. The pepsin-soluble collagens from both species had high levels of glycine, proline, alanine, glutamic acid, and hydroxyproline. The gelatin from S. horrens had a melting point of 30 °C and displayed exceptional thermal stability, surpassing that of mammalian gelatin. Its gelling point was 5 °C, like that of cold-water fish gelatin, with a viscosity of 2.065 cp-lower than mammal gelatins. These findings suggested that collagen and gelatin from sea cucumbers could be useful in nutraceutical, pharmaceutical and cosmetic industries.
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spelling ums.eprints-428902025-02-18T01:31:05Z https://eprints.ums.edu.my/id/eprint/42890/ Extraction and characterization of collagen and gelatin from body wall of sea cucumbers stichopus horrens and holothuria arenicola Noora Barzkar Gilan Attaran-Fariman Ali Taheri Balu Alagar Venmathi Maran Q1-390 Science (General) QP501-801 Animal biochemistry Background: Marine invertebrates, including sponges, molluscs, jellyfish, mussels, and sea cucumbers, are abundant sources of high-quality collagen and offer advantages such as availability, ease of processing, lower inflammatory response, and good metabolic compatibility. Approximately 70% of the total protein in the body wall of sea cucumbers is collagen. Gelatin is a water-soluble protein produced from heat-denatured collagen and has various industrial applications. Methods: Pepsin-solubilized collagen was extracted from the body wall of two sea cucumber Stichopus horrens and Holothuria arenicola, species found in the Oman Sea and characterized with SDS-PAGE and amino acid composition. Then gelatin was extracted from pepsin-solubilized collagen of S. horrens and some rheological properties were measured. Results: Amino acid composition and SDS-PAGE analysis showed that the collagen from both species was type I, with one a1 chain and β chains, with molecular weights of 125 and 250 kDa, respectively. Glycine was the most abundant amino acid in the collagen from both sea cucumber species. The pepsin-soluble collagens from both species had high levels of glycine, proline, alanine, glutamic acid, and hydroxyproline. The gelatin from S. horrens had a melting point of 30 °C and displayed exceptional thermal stability, surpassing that of mammalian gelatin. Its gelling point was 5 °C, like that of cold-water fish gelatin, with a viscosity of 2.065 cp-lower than mammal gelatins. These findings suggested that collagen and gelatin from sea cucumbers could be useful in nutraceutical, pharmaceutical and cosmetic industries. PeerJ, Inc. 2024 Article NonPeerReviewed text en https://eprints.ums.edu.my/id/eprint/42890/1/FULL%20TEXT.pdf Noora Barzkar and Gilan Attaran-Fariman and Ali Taheri and Balu Alagar Venmathi Maran (2024) Extraction and characterization of collagen and gelatin from body wall of sea cucumbers stichopus horrens and holothuria arenicola. PeerJ. pp. 1-23. ISSN 2167-8359 http://dx.doi.org/10.7717/peerj.18149
spellingShingle Q1-390 Science (General)
QP501-801 Animal biochemistry
Noora Barzkar
Gilan Attaran-Fariman
Ali Taheri
Balu Alagar Venmathi Maran
Extraction and characterization of collagen and gelatin from body wall of sea cucumbers stichopus horrens and holothuria arenicola
title Extraction and characterization of collagen and gelatin from body wall of sea cucumbers stichopus horrens and holothuria arenicola
title_full Extraction and characterization of collagen and gelatin from body wall of sea cucumbers stichopus horrens and holothuria arenicola
title_fullStr Extraction and characterization of collagen and gelatin from body wall of sea cucumbers stichopus horrens and holothuria arenicola
title_full_unstemmed Extraction and characterization of collagen and gelatin from body wall of sea cucumbers stichopus horrens and holothuria arenicola
title_short Extraction and characterization of collagen and gelatin from body wall of sea cucumbers stichopus horrens and holothuria arenicola
title_sort extraction and characterization of collagen and gelatin from body wall of sea cucumbers stichopus horrens and holothuria arenicola
topic Q1-390 Science (General)
QP501-801 Animal biochemistry
url https://eprints.ums.edu.my/id/eprint/42890/1/FULL%20TEXT.pdf
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