Physicochemical and Rheological Properties of Gelatin Extracted from Tilapia (Oreochromis niloticus) Skin and Concentration Effect

Abstract:

Tilapia skin gelatins were extracted with optimal acetic or citric acid concentrations which provide similar optimum protein yield (22g/100 wet weight), and rheological properties of gelatin solutions with various concentrations were measured and characterized. Commercial valued properties including bloom strength, gelling and melting point, viscosity were measured to compare the samples of the two gelatins. Liner viscoelastic range (LVR) of gelatin preparations with increasing concentration and decreasing temperature were determined. Temperature sweep was conducted for comparison and characterization the relationships between concentration and gelling/melting point of gelatin extracted by citric acid or acetic acid. The results showed that the melting and gelling point varying with concentration followed exponential curve (R2 as high as 0.99), and there were rarely molecular fractions in extracted gelatins. Elastic modulus (G′) of gelatin gels was mainly a function of cold temperature and time, while the discrepancy between the melting behaviors of gelatin extracted by two acids may stem from the composition and molecular weight of gelatin chains. In conclusion, the tilapia skin gelatin extracted in our study is of high qualities and rheological analysis is a critical tool for material of gelatin differentiation from varied molecular properties.

• Periodical: Advanced Materials Research (Volumes 941-944)
• Pages: 1128-1132
• DOI: https://doi.org/10.4028/www.scientific.net/AMR.941-944.1128
• Online since: June 2014
• Authors: Yun Bai, Shuai Peng, Yi Qun Huang, Ke Qiang Lai*
• Keywords: Commercial Valued Property, Gelling Point, Melting Point, Rheological Analysis, Tilapia Skin Gelatin

References

[1] M.C. Gómez-Guillén, B. Giménez and M.E. López-Caballero: Functional and bioactive properties of collagen and gelatin from alternative sources: A review, Food Hydrocolloids Vol. 2 (2011), pp.1-15.

DOI: 10.1016/j.foodhyd.2011.02.007

[2] S. Grossman, R. Gan, M. Bergman and Holon, Process for the production of gelatin from fish skins, U.S. Patent 5093474. (1992).

[3] B. Jamilah and K.G. Harvinder: Properties of gelatins from skins of fish-black tilapia (Oreochromis mossambicus) and red tilapia (Oreochromis nilotica), Food Chemistry Vol. 77 (2002), p.81–84.

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

[4] P. Zhou and J. M. Regenstein: Properties of Alaska Pollock skin gelatin: a comparison with Tilapia and pork skin gelatins, Journal of Food Science Vol. 71 (2006), pp.313-321.

DOI: 10.1111/j.1750-3841.2006.00065.x

[5] M. Ladislaus, Y.X. Kasankala, Y. Weilong, D.H. Sun and H. Qian: Optimization of gelatine extraction from grass carp (Catenopharyngodon idella) fish skin by response surface methodology, Bioresource Technology Vol. 98 (2007), p.3338–3343.

DOI: 10.1016/j.biortech.2006.03.019

[6] A.A. Karim and R. Bhat: Fish gelatin: properties, challenges, and prospects as an alternative to mammalian gelatins, Food Hydrocolloids Vol 23 (2009), pp.563-576.

DOI: 10.1016/j.foodhyd.2008.07.002

[7] D. Holzer, Gelatin production, US patent 5, 484, 888. (1996).

[8] X. Zhou, L.H. Niu, Y. Bai and Y. Wang: Effect of different acid treatment on yield and physicochemical properties of gelatin derived from tilapia skin, Journal of Beijing technology and Business University (natural science edition) Vol. 30 (2012).

[9] P. Zhou and J.M. Regenstein: Optimization of extraction conditions for Pollock skin gelatin, Journal of food science Vol. 69 (2004), pp.393-398.

[10] A.G. Gornall and C.J. Bardawill: Determination of serum proteins by means of the Biuret Reaction, J Biol Chem Vol. 177 (1949), pp.751-766.

DOI: 10.1016/s0021-9258(18)57021-6

[11] S.B. Ross-Murphy: Incipient behaviour of gelatin gels, Rheologica Acta Vol. 30 (1991), p.401–411.

DOI: 10.1007/bf00396526

[12] M. Gudmundsson: Rheological properties offish gelatins, Journal of Food Science Vol. 76 (2002), p.2172–2176.

[13] F. Badii and N.K. Howell: Fish gelatin: Structure, gelling properties and interaction with egg albumen proteins, Food Hydrocolloids Vol. 20 (2006), p.630–640.

DOI: 10.1016/j.foodhyd.2005.06.006

[14] S. L. Kosaraju, A. Puvanenthiran and P. Lillford: Naturally crosslinked gelatin gels with modified material properties, Food Research International Vol. 43 (2010), p.2385–2389.

DOI: 10.1016/j.foodres.2010.09.008

[15] B. Horecker, N. O. Kaplan and H. A. Scheraga, in: Molecular Biology, edited by A. Veis, volume 5 of The Macromolecular Chemistry of Gelatin, chapter, 1, Academic Press Inc. (1964).

[16] G. Stainsby, in: Gelatin gels, edited by A.M. Pearson, T.R. Dutson, & A.J. Bailey, volume 1 of Collagen as a food, chapter, 3, Van Nostrand Reinhold Co. Inc. (1987).

[17] M. Ahmad and S. Benjakul: Characteristics of gelatin from the skin of unicorn leatherjacket (Aluterus monoceros) as influenced by acid pretreatment and extraction time, Food Hydrocolloids Vol. 25 (2011), pp.381-388.

DOI: 10.1016/j.foodhyd.2010.07.004