Dergiler / Turkish Journal of Veterinary and Animal Sciences / 2015 / Cilt: 39 - Sayı: 1

Functional properties of gelatin recovered from scales of farmed sea bass (Dicentrarchus labrax)

Sayfa
102–109
Yayın Tarihi
2015-03-15
DOI
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⚡ TL;DR(1 Cümlede Hızlı Çıkarım)

Fourier transform infrared spectroscopic analysis showed the characteristic similarities of gelatin produced from sea bass scales and calf skin.

📌 3 Maddede Bu Makale

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Amaç & Hipotez:In the current study gelatin was recovered from scales of farmed sea bass (Dicentrarchus labrax).
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Temel Bulgular & Veri:The first part of the study was planned to determine the yield of acid-soluble collagen and pepsin-soluble collagen from the scales.
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Sonuç & Katkı:Fourier transform infrared spectroscopic analysis showed the characteristic similarities of gelatin produced from sea bass scales and calf skin.
🔬Tür:Araştırma Makalesi
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:Collagen · gelatin · gel strength

Özet

In the current study gelatin was recovered from scales of farmed sea bass (Dicentrarchus labrax). The first part of the study was planned to determine the yield of acid-soluble collagen and pepsin-soluble collagen from the scales. Both collagens were characterized as type I collagen, containing a-1 and a-2 chains. In the second part, gelatin was extracted using acetic acid and functional properties were determined in this product. Gelatin protein value was found to be 96% and the yield was found to be 18.49%. Proline and hydroxyproline values in the amino acid were found to be high. The gel strength of gelatin was 305 g and viscosity of the gelatin was 33 cP. The gelatin was identified as type A gelatin due to its properties. Fourier transform infrared spectroscopic analysis showed the characteristic similarities of gelatin produced from sea bass scales and calf skin.

Abstract

In the current study gelatin was recovered from scales of farmed sea bass (Dicentrarchus labrax). The first part of the study was planned to determine the yield of acid-soluble collagen and pepsin-soluble collagen from the scales. Both collagens were characterized as type I collagen, containing a-1 and a-2 chains. In the second part, gelatin was extracted using acetic acid and functional properties were determined in this product. Gelatin protein value was found to be 96% and the yield was found to be 18.49%. Proline and hydroxyproline values in the amino acid were found to be high. The gel strength of gelatin was 305 g and viscosity of the gelatin was 33 cP. The gelatin was identified as type A gelatin due to its properties. Fourier transform infrared spectroscopic analysis showed the characteristic similarities of gelatin produced from sea bass scales and calf skin.

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Bu Makaleye Atıf Yap

DİNÇER, M. T., AĞÇAY, Ö. Y., SARGIN, H., BAYRAM, H. (2015). Functional properties of gelatin recovered from scales of farmed sea bass (Dicentrarchus labrax). Turkish Journal of Veterinary and Animal Sciences, Cilt: 39 - Sayı: 1, 102–109. https://ajindex.com/articles/121692

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Kaynakça (14)

  1. Gelatin Manufacturers Institute of America. Gelatin Handbook. Woburn, MA, USA: GMIA; 2012.
  2. Aewsiri T, Benjakul S, Visessanguan W, Tanaka M. Chemical compositions and functional properties of gelatin from pre- cooked tuna fin. Int J Food Sci Technol 2008; 43: 685–693.
  3. Zhou P, Regenstein JM. Optimization of extraction conditions for pollock skin gelatin. J Food Sci 2004; 69: 393–398.
  4. Yang H, Wang Y, Jiang M, Oh JH, Herring J, Zhou P. 2-Step optimization of the extraction and subsequent physical properties of channel catŞsh (Ictalurus punctatus) skin gelatin. J Food Sci 2007; 72: 188–195.
  5. Muyonga JH, Cole CGB, Duodu KG. Fourier transform infrared (FTIR) spectroscopic study of acid soluble collagen and gelatin from skins and bones of young and adult Nile perch (Lates niloticus). Food Chem 2004; 86: 325–332.
  6. Zeng S, Yan X, Cao W, Hong P, Zhang C, Li L. Optimisation of extraction conditions and characteristics of skin gelatin from Nile tilapia (Oreochromis niloticus). Int J Food Sci Technol 2010; 45: 1807–1813.
  7. Wang L, An X, Yang F, Xin Z, Zhao L, Hu Q. Isolation and characterization of collagens from the skin, scale and bone of deep - sea redŞsh (Sebastes mentella). Food Chem 2008; 108: 616–623.
  8. Zhang J, Duan R, Ye C, Konno K. Isolation and characterization of collagens from scale of silver carp (Hypophthalmichthys molitrix). J Food Biochem 2010; 34: 1343–1354.
  9. Nikoo M, Xu X, Benjakul S, Xu G, Ramirez-Suarez JC, Ehsani A, Kasankala LM, Duan X, Abbas S. Characterization of gelatin from the skin of farmed Amur sturgeon Acipenser schrenckii. Int Aquat Res 2011; 8: 135–145.
  10. Gomez-Guillen C, Turnay J, Fernandez-Diaz MD, Lizarbe MA, Montero P. Structural and physical properties of gelatin extracted from different marine species: a comparative study. Food Hydrocoll 2002; 16: 25–34.
  11. Karim AA, Bhat R. Fish gelatin: properties, challenges, and prospects as an alternative to mammalian gelatins. Food Hydrocoll 2009; 23: 563–576.
  12. Zhou P, Mulvaney SJ, Regenstein JM. Properties of Alaska pollock skin gelatin: a comparison with tilapia and pork skin gelatins. J Food Sci 2006; 71: 313–321.
  13. Jamilah B, Harvinder KG. Properties of gelatins from skins of Şsh - black tilapia (Oreochromis mossambicus) and red tilapia (Oreochromis nilotica). Food Chem 2002; 77: 81–84. Poppe J. Gelatin in Thickening and Gelling Agents for Food. 2nd ed. London, UK: Blackie Academic; 1997.
  14. Wangtueai S, Noomhorm A. Processing optimization and characterization of gelatin from lizardfish (Saurida spp.) scal