Improving the Physicochemical Properties of Commercial Bovine Gelatin using Succinylation

Nur Aliyana Binti Alias, Benedict Oludare Omosebi, Wahyudi David, Nurul Huda


Commercial bovine gelatin was modified by using succinic anhydride and resultant changes in physicochemical properties such as Bloom strength, foaming properties and extent of succinylation were investigated. The result indicated that addition of succinic anhydride at varying concentrations of 0.04, 0.08, 0.12 and 0.16 g/g of sample increased the degree of succinylation from 0% to 14%, while Bloom strength increased from 131.97% to148.60% but at higher concentration decreased from 133.50% to128.0%. Foaming capacity increased from 171.67% to 210.70%   but a substantial constant decrease in foaming stability with time.

Keywords- Gelatin,  Succinic anhydride, gel strength, foaming capacity,  physicochemical properties,



Arnesen, J. A. and Gildberg, A. 2007. Extraction and characterisation of gelatine from Atlantic salmon (Salmo salar) skin. Bioresource Technology, 98(1):53-57.

Bora, P. S. 2002. Functional properties of native and succinylated lentil (Lens culinaris) globulins. Food Chemistry, 77(2): 171-176.

Cheftel, J. C., Cug, J. L. and Lorient, D. 1985. Amino acids, peptides and proteins. In. Fennema, O.R. (Ed.). Food chemistry: Second edition, revised and expanded, pp. 245-370. New York: Marcel Dekker, Inc.

El-Adawy, T. A. 2000. Functional properties and nutritional quality of acetylated and succinylated mung bean protein isolate. Food Chemistry, 70(1): 83-91.

Franzen, K. L. and Kinsella, J. E. 1976. Functional properties of succinylated and acetylated soy protein. Journal of Agricultural and Food Chemistry, 24(4): 788-795.

GMIA (Gelatin Manufactures Institute of America). 2014. Gelatin handbook. Available from: http://www. _2012.pdf [Accessed on 26 Nov. 2014].

Gómez-Guillén, M. C., Giménez, B., López-Caballero, M. A., and Montero, M. P. 2011. Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food Hydrocolloids, 25(8): 1813-1827.

Grand View Research. 2014. Gelatin Market Analysis by Raw Material (Pig Skin, Bovine Hides, Bones), by Application (Food & Beverage, Nutraceuticals, Pharmaceuticals, Photography, Cosmetics) and Segment Forecasts to 2020.[Accessed on 26 Nov. 2014].

Groninger Jr, H. S. 1973. Preparation and properties of succinylated fish myofibrillar protein. Journal of Agricultural and Food Chemistry, 21(6), 978-981.

Jongjareonrak, A., Benjakul, S., Visessanguan, W. and Tanaka, M. 2006. Skin gelatin from bigeye snapper and brownstripe red snapper: Chemical compositions and effect of microbial transglutaminase on gel properties. Food Hydrocolloids 20 (8): 1216-1222.

Kabirullah, M., & Wills, R. B. H. 1982. Functional properties of acetylated and succinylated sunflower protein isolate. International Journal of Food Science and Technology, 17(2), 235-249.

Karim, A. A., & Bhat, R. 2008. Gelatin alternatives for the food industry: recent developments, challenges and prospects. Trends in Food Science and Technology, 19(12): 644-656.

Kinsella, J. E. 1976. Functional properties of protein in food: a survey. Critical Reviews in Food and Nutrition. 7:219-280.

Klapper, M. H. and and Klotz, I. M. 1972. Acylation with dicarboxylic acid anhydrides. Methods in Enzymology, 25:531-536.

Lawal, O. S. 2005. Functionality of native and succinylated Lablab bean (Lablab purpureus) protein concentrate. Food Hydrocolloids, 19(1), 63-72.

Liu, J., Ru, Q. and Ding, Y., 2012. Glycation a promising method for food protein modification: Physicochemical properties and structure, a review. Food Research International 49, 170–183.

Mahajan, A., Neetu and Ahluwalia, A. S. 2010. Effect of processing on functional properties of Spirulina protein preparations. African Journal of Microbiology Research, 4 (1):55-60.

Means, G. E., and Feeney, R. E., 1971. Chemical Modification of Proteins. Holden-Day, Inc.: San Francisco.

Miedzianka, J., Peksa, A. and Aniołowska, M. 2012. Properties of acetylated potato protein preparations. Food Chemistry 133: 1283–1291.

Mirmoghtadaie, L., Kadivar, M., and Shahidi, M. 2009. Effects of succinylation and deamidation on functional properties of oat protein isolate. Food Chemistry, 114 (1), 127-131.

Oppenheimer. H., Baranv. K.. Hamoir. G. and Fenton. J. 1967. Succinylation of myosin. Archives of Biochernistry and Biophysics. 120:108-118.

Paulson, A. T., and Tung, M. A. 1987. Solubility, hydrophobicity and net charge of succinylated canola protein isolate. Journal of Food Science, 52(6), 1557-1561.

Schrieber, R., and Gareis, H. 2007. Gelatine handbook. Weinhem: Wiley-VCH GmbH & Co.

Shahidi, F., Han Xiao-Qing, H., and Synowieck, J. 1995. Production and characteristics of hydrolysates from capelin (Mallotus villosus). Food Chem. 53:285-293.

Shilpashreea, B.G., Arora, S., Prince Chawla, P. and Tomar, S.K. 2015. Effect of succinylation on physicochemical and functional properties of milk protein concentrate. Food Research International, 72:223–230.

Townsend, A. A., and Nakai, S. 1983. Relationships between hydrophobicity and foaming characteristics of food proteins. Journal of Food Science, 48(2), 588-594.

Wanasundar, P. K. J. P. D. and Shahidi, F. 1997. Functional properties of acylated flax protein isolates. Journal of Agriiculture and Food Chemistry, 45:2431-2440.

Zayas, J. F. 1997. Functionality of proteins in food. Berlin: Springer,

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