3
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Extraction and Characterization of Type I Collagen from Parrotfish ( Scarus sordidus Forsskål, 1775) Scale solubilized with the Aid of Acetic Acid and Pepsin

      research-article

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Waste from marine fish processing is an important source of valuable products. Fish collagen is considered a alternative biomaterial due to its excellent properties, and it is widely used for industrial purposes. Thus, this present study aimed to characterize acid and pepsin-soluble collagens from the waste of parrotfish ( Scarus sordidus Forsskål, 1775) scales. The yields ( p > 0.05) of acid-soluble collagen (ASC-PFS) and pepsin-soluble collagen (PSC-PFS) were 1.17 g/100 g and 1.00 g/100 g, respectively. Both collagen samples were categorized as type I owing to the presence of two alpha chain subunits ( α1 and α1) after being confirmed by a sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Under the fourier transform infrared (FTIR) test, the triple helical structure of type I collagens from the ASC-PFS and PSC-PFS was maintained. Moreover, the study of UV visible spectra and X-ray diffraction (XRD) showed the similarity of collagens derived from different fish species, and the thermostability ( T max) evaluation of all extracted collagens was in the range of 36.22–37.78°C, and their values were comparable to previous research on the fish scale collagens. The effect of various pH and sodium chloride (NaCl) treatments on solubility exhibited that the ASC-PFS and PSC-PFS were highly soluble in an acidic condition (pH < 5.0) and low concentration of sodium chloride (<30 g/L). Taken together, collagens extracted from parrotfish scale waste can be an alternative source for industries.

          Related collections

          Most cited references57

          • Record: found
          • Abstract: not found
          • Article: not found

          Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

            Bookmark
            • Record: found
            • Abstract: not found
            • Article: not found
            Is Open Access

            PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT

              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Collagen structure and stability.

              Collagen is the most abundant protein in animals. This fibrous, structural protein comprises a right-handed bundle of three parallel, left-handed polyproline II-type helices. Much progress has been made in elucidating the structure of collagen triple helices and the physicochemical basis for their stability. New evidence demonstrates that stereoelectronic effects and preorganization play a key role in that stability. The fibrillar structure of type I collagen-the prototypical collagen fibril-has been revealed in detail. Artificial collagen fibrils that display some properties of natural collagen fibrils are now accessible using chemical synthesis and self-assembly. A rapidly emerging understanding of the mechanical and structural properties of native collagen fibrils will guide further development of artificial collagenous materials for biomedicine and nanotechnology.
                Bookmark

                Author and article information

                Contributors
                Journal
                Int J Biomater
                Int J Biomater
                ijbm
                International Journal of Biomaterials
                Hindawi
                1687-8787
                1687-8795
                2023
                26 April 2023
                : 2023
                : 7312447
                Affiliations
                1Faculty of Food Science and Nutrition, Universiti Malaysia Sabah, Kota Kinabalu 88400, Sabah, Malaysia
                2Faculty of Fisheries and Marine Science, Universitas Brawijaya, Malang 65145, Indonesia
                3Borneo Marine Research Institute, Universiti Malaysia Sabah, Kota Kinabalu 88400, Sabah, Malaysia
                4Biotechnology Research Institute, Universiti Malaysia Sabah, Kota Kinabalu 88400, Sabah, Malaysia
                5Fisheries Research Institute, Batu Maung, Penang 11960, Malaysia
                6Faculty of Sustainable Agriculture, Universiti Malaysia Sabah, Sandakan 90509, Sabah, Malaysia
                Author notes

                Academic Editor: Fu-Gen Wu

                Author information
                https://orcid.org/0000-0001-7121-4055
                https://orcid.org/0000-0003-1548-3327
                https://orcid.org/0000-0001-5217-7607
                https://orcid.org/0000-0002-7684-4360
                https://orcid.org/0000-0001-9867-6401
                Article
                10.1155/2023/7312447
                10156459
                304d27f2-a3aa-44af-87bc-77a27bc4ef3a
                Copyright © 2023 Abdul Aziz Jaziri et al.

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 1 December 2022
                : 1 February 2023
                : 3 March 2023
                Funding
                Funded by: Ministry of Higher Education, Malaysia
                Award ID: FRGS/1/2019/STG03/UMS/02/5
                Funded by: Universiti Malaysia Sabah
                Categories
                Research Article

                Biomaterials & Organic materials
                Biomaterials & Organic materials

                Comments

                Comment on this article