Effects of Pre-Treatment Durations on Properties of Black Tilapia (Oreochromis mossambicus) Skin Gelatin

Article Preview

Abstract:

Black tilapia (Oreochromis mossambicus) fish skins are good alternatives sources of gelatin. Vast variations in extraction procedures affect the properties of fish gelatin such as yield and gel strength. Thus, this study explores the effect of pretreatment durations on the properties of black tilapia skin gelatin. Gelling properties such as gel strength (bloom value) of the gelatin samples had been determined. Highest gel strength had been detected for gelatin treated at 24 h (390.1 g), followed by 16 h (287.1 g) and 8 h (141.2 g). In contrast, gelatin treated at 24 h indicates lower yield on wet weight basis (14.12 %) than those treated at 16 h (14.96 %) and 8 h (16.90 %). The possible interactions and characteristics between the functional groups in the gelatin samples have also been perceived via Fourier Transform Infrared Spectroscopy (FTIR) analysis.

You might also be interested in these eBooks

Info:

Periodical:

Pages:

146-150

Citation:

Online since:

January 2016

Export:

Price:

Permissions CCC:

Permissions PLS:

Сopyright:

© 2016 Trans Tech Publications Ltd. All Rights Reserved

Share:

Citation:

* - Corresponding Author

[1] N. Ktari, M. Jridi, R. Nasri, I. Lassoued, H. B. Ayed, A. Barkia, M. Nasri, Characteristics and functional properties of gelatin from zebra blenny (Salaria basilisca) skin, LWT. Food Sci. Technol. 58 (2014) 602-608.

DOI: 10.1016/j.lwt.2014.03.036

Google Scholar

[2] M. Jridi, R. Nasri, I. Lassoued, N. Souissi, A. Mbarek, A. Barkia, M. Nasri, Screening of factors influencing the extraction of gelatin from the skin of cuttlefish using supersaturated design, Food Res. Int. 54 (2013): 1680–1687.

DOI: 10.1016/j.foodres.2013.09.026

Google Scholar

[3] A.T. Alfaro, F. C. Biluca, C. Marquetti, I.B. Tonial, N.E. de Souza, African catfish (Clarias gariepinus) skin gelatin: Extraction optimization and physical–chemical properties, Food Res. Int. 65 (2014): 416–422.

DOI: 10.1016/j.foodres.2014.05.070

Google Scholar

[4] M. Nikoo, S. Benjakul, M. Bashari, M. Alekhorshied, A. Idrissa Cissouma, N. Yang, X. Xu, Molecular characteristics and properties of gelatin 2 from skin of seabass with different sizes, Food Bio Sci. 5 (2014): 19–26.

DOI: 10.1016/j.fbio.2013.10.004

Google Scholar

[5] I. Ratnasari, S. Y. Sudarminto, H. Nusyam, S. B. Widjanarko, Extraction Process Modification to Enhance Properties of Skin Gelatin of Pangas Catfish (Pangasius pangasius), Food Public Health. 4 (2014): 140–150.

Google Scholar

[6] K. Shyni, G. S. Hema, G. Ninan, S. Mathew, C. G. Joshy, P. T. Lakshmanan, Isolation and characterization of gelatin from the skins of skipjack tuna (Katsuwonus pelamis), dog shark (Scoliodon sorrakowah), and rohu (Labeo rohita), Food Hydrocoll. 39 (2014).

DOI: 10.1016/j.foodhyd.2013.12.008

Google Scholar

[7] S. Sinthusamran, S. Benjakul, H. Kishimura, Characteristics and gel properties of gelatin from skin of seabass (Lates calcarifer) as influenced by extraction conditions, Food Chem. 152 (2014): 276–284.

DOI: 10.1016/j.foodchem.2013.11.109

Google Scholar

[8] A.T. Alfaro, G.G. Fonseca, E. Balbinot, C. Prentice, Physical and chemical properties of wami tilapia skin gelatine, Food Sci. Technol. Int. 33 (2013): 1–9.

DOI: 10.1590/s0101-20612013005000069

Google Scholar

[9] B. Jamilah, K. G. Harvinder, Properties of gelatins from skins of fish—black tilapia (Oreochromis mossambicus) and red tilapia (Oreochromis nilotica), Food Chem. 77 (2002): 81–84.

DOI: 10.1016/s0308-8146(01)00328-4

Google Scholar

[10] A.A. Karim, R. Bhat, Fish gelatin: Properties, challenges, and prospects as an alternative to mammalian gelatins, Food Hydrocoll. 23 (2009): 563-576.

DOI: 10.1016/j.foodhyd.2008.07.002

Google Scholar

[11] F.A. de Wolf, Collagen and gelatin, Prog. Biotech. 23 (2003): 133-218.

Google Scholar

[12] P. Montero, M. C. Gómez-Guillén, Extracting Conditions for Megrim (Lepidorhombus boscii) Skin Collagen Affect Functional Properties of the Resulting Gelatin, Food Chem. Toxicol. 65 (2000): 434–438.

DOI: 10.1111/j.1365-2621.2000.tb16022.x

Google Scholar

[13] BSI (British Standards Institution), 1975. Methods for Sampling and Testing Gelatin (Physical and Chemical Methods). BSI, London, United Kingdom.

Google Scholar

[14] C.S. Cheow, M.S. Norizah, Z.Y. Kyaw, N.K. Howell, Preparation and characterisation of gelatins from the skins of sin croaker (Johnius dussumieri) and shortfin scad (Decapterus macrosoma), Food Chem. 101 (2007): 386–391.

DOI: 10.1016/j.foodchem.2006.01.046

Google Scholar

[15] P. Kittiphattanabawon, S. Benjakul, W. Visessanguan, T. Nagai, M. Tanaka, Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus), Food Chem. 89 (2005): 363-372.

DOI: 10.1016/j.foodchem.2004.02.042

Google Scholar

[16] M. C. Gómez-Guillén, B. Giménez, M. E. López-Caballero, M. P. Montero, Functional and bioactive properties of collagen and gelatin from alternative sources: A review, Food Hydrocoll. 25 (2011): 1813–1827.

DOI: 10.1016/j.foodhyd.2011.02.007

Google Scholar

[17] B. Jamilah, K.W. Tan, M.R.U. Hartina, A. Azizah, Gelatins from three cultured freshwater fish skins obtained by liming process, Food Hydrocoll. 25 (2011): 1256–1260.

DOI: 10.1016/j.foodhyd.2010.11.023

Google Scholar

[18] R.S.G. Silva, S.F. Bandeira, L.A.A. Pinto, Characteristics and Chemical Composition of Skin Gelatin from Cobia (Rachycentron Canadum), LWT - Food Sci. Technol. 57 (2014): 580–585.

DOI: 10.1016/j.lwt.2014.02.026

Google Scholar

[19] F. Pati, B. Adhikari, S. Dhara, Isolation and characterization of fish scale collagen of higher thermal stability, Bioresour. Technol. 101 (2010): 3737–3742.

DOI: 10.1016/j.biortech.2009.12.133

Google Scholar