Extraction and characterization of pepsin-soluble collagen from different mantis shrimp species
The objective of this study was to investigate the yield and characteristics of collagen protein extracted from the muscle of four different species of mantis shrimp: Miyakella nepa, Harpiosquilla harpax, Erugosquilla woodmasoni, and Od...
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| Format: | Article |
| Language: | English |
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The Korean Society of Fisheries and Aquatic Science
2021-12-01
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| Series: | Fisheries and Aquatic Sciences |
| Subjects: | |
| Online Access: | http://www.e-fas.org/archive/view_article?pid=fas-24-12-406 |
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| author | Rachanimuk Hiransuchalert Nakaweerada Oonwiset Yolrawee Imarom Parinya Chindudsadeegul Penchan Laongmanee Sukchai Arnupapboon |
| author_facet | Rachanimuk Hiransuchalert Nakaweerada Oonwiset Yolrawee Imarom Parinya Chindudsadeegul Penchan Laongmanee Sukchai Arnupapboon |
| author_sort | Rachanimuk Hiransuchalert |
| collection | DOAJ |
| description | The objective of this study was to investigate the yield and characteristics of
collagen protein extracted from the muscle of four different species of mantis
shrimp: Miyakella nepa, Harpiosquilla harpax, Erugosquilla
woodmasoni, and Odontodactylus cultrifer. Mantis
shrimp muscle was extracted by using a pepsin-solubilization technique, with 0.5
M acetic acid and 5% pepsin enzyme. The highest collagen yield was from
M. nepa muscle (0.478 ± 0.06%), which was
significantly greater (p < 0.05) than that from
H. harpax, O. cultrifer, and E. woodmasoni
(0.313 ± 0.03%, 0.123 ± 0.02%, and 0.015 ± 0.00%,
respectively). The freeze-dried collagen appeared as thin fibers, and formed an
opaque film. The pepsin-soluble collagen (PSC) from four mantis shrimp species
was analyzed by gel electrophoresis. The results showed that all species of
mantis shrimp contained type I collagen, consisting of β, α1, and
α2 subunits with average molecular weights of 250, 145, and 118 kDa,
respectively. The study of the solubility of collagen showed that, for NaCl,
collagen had the highest relative solubility in 2% NaCl (80.20 ± 4.95%).
In contrast, the solubility decreased at higher NaCl concentrations. However, in
terms of pH, collagen had the highest relative solubility at pH 3 (91.32
± 5.14%), and its solubility decreased at higher pH. FT-IR spectroscopy
was used to compare the collagen with a model compound. Five wavenumbers in the
spectrum for model collagen were identified: Amide A (3,406–3,421
cm−1), amide B (2,916–2,940
cm−1), amide I (1,639–1,640 cm−1),
amide II (1,539–1,570 cm−1), and amide III
(1,234–1,250 cm−1). |
| first_indexed | 2024-12-11T14:56:09Z |
| format | Article |
| id | doaj.art-9b056cc7fc924c48a3547d4a965c2e57 |
| institution | Directory Open Access Journal |
| issn | 2234-1757 |
| language | English |
| last_indexed | 2024-12-11T14:56:09Z |
| publishDate | 2021-12-01 |
| publisher | The Korean Society of Fisheries and Aquatic Science |
| record_format | Article |
| series | Fisheries and Aquatic Sciences |
| spelling | doaj.art-9b056cc7fc924c48a3547d4a965c2e572022-12-22T01:01:19ZengThe Korean Society of Fisheries and Aquatic ScienceFisheries and Aquatic Sciences2234-17572021-12-01241240641410.47853/FAS.2021.e42fas-24-12-406Extraction and characterization of pepsin-soluble collagen from different mantis shrimp speciesRachanimuk Hiransuchalert0Nakaweerada Oonwiset1Yolrawee Imarom2Parinya Chindudsadeegul3Penchan Laongmanee4Sukchai Arnupapboon5Faculty of Marine Technology, Burapha University Chanthaburi Campus, Faculty of Marine Technology, Burapha University Chanthaburi Campus, Faculty of Marine Technology, Burapha University Chanthaburi Campus, Faculty of Gems, Burapha University Chanthaburi Campus, Faculty of Marine Technology, Burapha University Chanthaburi Campus, Training Department, Southeast Asian Fisheries Development Center, The objective of this study was to investigate the yield and characteristics of collagen protein extracted from the muscle of four different species of mantis shrimp: Miyakella nepa, Harpiosquilla harpax, Erugosquilla woodmasoni, and Odontodactylus cultrifer. Mantis shrimp muscle was extracted by using a pepsin-solubilization technique, with 0.5 M acetic acid and 5% pepsin enzyme. The highest collagen yield was from M. nepa muscle (0.478 ± 0.06%), which was significantly greater (p < 0.05) than that from H. harpax, O. cultrifer, and E. woodmasoni (0.313 ± 0.03%, 0.123 ± 0.02%, and 0.015 ± 0.00%, respectively). The freeze-dried collagen appeared as thin fibers, and formed an opaque film. The pepsin-soluble collagen (PSC) from four mantis shrimp species was analyzed by gel electrophoresis. The results showed that all species of mantis shrimp contained type I collagen, consisting of β, α1, and α2 subunits with average molecular weights of 250, 145, and 118 kDa, respectively. The study of the solubility of collagen showed that, for NaCl, collagen had the highest relative solubility in 2% NaCl (80.20 ± 4.95%). In contrast, the solubility decreased at higher NaCl concentrations. However, in terms of pH, collagen had the highest relative solubility at pH 3 (91.32 ± 5.14%), and its solubility decreased at higher pH. FT-IR spectroscopy was used to compare the collagen with a model compound. Five wavenumbers in the spectrum for model collagen were identified: Amide A (3,406–3,421 cm−1), amide B (2,916–2,940 cm−1), amide I (1,639–1,640 cm−1), amide II (1,539–1,570 cm−1), and amide III (1,234–1,250 cm−1).http://www.e-fas.org/archive/view_article?pid=fas-24-12-406mantis shrimppepsin-soluble collagensodium dodecyl sulfate-polyacrylamide gel electrophoresis (sds-page)fourier transform-infrared (ft-ir)solubility |
| spellingShingle | Rachanimuk Hiransuchalert Nakaweerada Oonwiset Yolrawee Imarom Parinya Chindudsadeegul Penchan Laongmanee Sukchai Arnupapboon Extraction and characterization of pepsin-soluble collagen from different mantis shrimp species Fisheries and Aquatic Sciences mantis shrimp pepsin-soluble collagen sodium dodecyl sulfate-polyacrylamide gel electrophoresis (sds-page) fourier transform-infrared (ft-ir) solubility |
| title | Extraction and characterization of pepsin-soluble collagen from
different mantis shrimp species |
| title_full | Extraction and characterization of pepsin-soluble collagen from
different mantis shrimp species |
| title_fullStr | Extraction and characterization of pepsin-soluble collagen from
different mantis shrimp species |
| title_full_unstemmed | Extraction and characterization of pepsin-soluble collagen from
different mantis shrimp species |
| title_short | Extraction and characterization of pepsin-soluble collagen from
different mantis shrimp species |
| title_sort | extraction and characterization of pepsin soluble collagen from different mantis shrimp species |
| topic | mantis shrimp pepsin-soluble collagen sodium dodecyl sulfate-polyacrylamide gel electrophoresis (sds-page) fourier transform-infrared (ft-ir) solubility |
| url | http://www.e-fas.org/archive/view_article?pid=fas-24-12-406 |
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