Characteristics of Gelatin Extracted from Indonesian Local Cattle Hides Using Acid and Base Curing
DOI:
https://doi.org/10.3923/pjn.2019.443.454Keywords:
Amino acid, Bali cattle, gelatin quality, Madura cattle, Ongole crossbred cattleAbstract
Background and Objective: Gelatin quality is affected by factors including the animal source materials, the age of the animal and curing and extraction processes. However, the effects of the cattle breed on gelatin quality have not been reported. This study aimed to determine the characteristics of gelatin from Indonesian local cattle [Bali, Madura and Ongole Crossbred (OC)] hides with acid and base curing. Materials and Methods: The hides were treated with 0.25 M hydrochloric acid and 0.25 M sodium hydroxide. The data were analyzed using a completely randomized design with a nested pattern and three replicates. The mean differences in the data were analyzed using Duncan’s multiple range test. Results: The highest gelatin yield was 11.04%, the pH was 9.91, the protein content was 83.45%, the soluble protein content was 12.82 mg mL–1, the viscosity was 8 cP and the gel strength was 166 Bloom. The Aw, moisture content, fat content and color values of the gelatins did not differ significantly (p>0.05) among the cattle breeds or between the curing treatments. The molecular weight determinations of the HCl-derived gelatin showed clearer bands than those from NaOH, including showing a band for low-molecular weight proteins (size range between 10 and 25 kDa). Fourier transform infrared (FTIR) spectroscopy showed that while the absorbance intensities of the O-H, C-H, C ≡ C, C ≡ N, C = C, C-C and C-O functional groups from the gelatin samples varied, the peaks were still indicative of the functional groups typically present in gelatin. The most abundant amino acid was glycine at 48.73 g/100 g, followed by glutamic acid at 18.69 g/100 g and arginine at 14.77 g/100 g and histidine was not detected. Conclusion: The use of 0.25 M HCl was more effective and efficient than using 0.25 M NaOH. The amino acid content from the OC hide treated with NaOH was higher than those obtained with the other treatments.
References
Schrieber, R. and H. Gareis, 2007. Gelatine Handbook: Theory and Industrial Practice. Wiley-VCH, Germany, ISBN: 3527315489, pp: 66-93.
De Wolf, F.A., 2003. Collagen and Gelatin. In: Progress in Biotechnology, Aalbersberg, W.Y., R.J. Hamer, P. Jasperse, H.H.J. de Jongh, C.G. de Kruif, P. Walstra and F.A. de Wolf (Eds.). B.V. Elsevier Science, Amsterdam, Netherlands, ISBN: 978-0-444-51394-6, pp: 133-218.
Haug, I.J. and K.I. Draget, 2009. Gelatin. In: Handbook of Hydrocolloids, Philips, G.O. and P.A. Williams (Eds.). 2nd Edn., Woodhead Publishing Limited, Cambridge, pp: 142-163.
Ahmad, T., A. Ismail, S.A. Ahmad, K.A. Khalil and E.A. Awad et al., 2018. Characterization of gelatin from bovine skin extracted using ultrasound subsequent to bromelain pretreatment. Food Hydrocolloids, 80: 264-273.
Gilsenan, P.M. and S.B. Ross-Murphy, 2000. Viscoelasticity of thermoreversible gelatin gels from mammalian and piscine collagens. J. Rheol., 44: 871-883.
Wang, L.Z., B. Yang, R. Wang and X.Q. Du, 2008. Extraction of pepsin-soluble collagen from grass carp (Ctenopharyngodon idella) skin using an artificial neural network. Food Chem., 111: 683-685.
Bhat, R. and A.A. Karim, 2009. Ultraviolet irradiation improves gel strength of fish gelatin. Food Chem., 113: 1160-1164.
Gimenez, B., M.C. Gomez-Guillen and P. Montero, 2005. Storage of dried fish skins on quality characteristics of extracted gelatin. Food Hydrocolloids, 19: 958-963.
AOAC., 2005. Official Methods of Analysis. 18th Edn., Association of Officials Analytical Chemist Inc., Washington, DC., pp: 1-3.
Owusu-Apenten, R., 2002. Food Protein Analysis: Quantitative Effects on Processing. Marcel Dekker Inc., Switzerland, ISBN: 9780824744670, Pages: 488.
Arnesen, J.A. and A. Gildberg, 2002. Preparation and characterisation of gelatine from the skin of harp seal (Phoca groendlandica). Bioresour. Technol., 82: 191-194.
Muyonga, J.H., C.G.B. Cole and K.G. Duodo, 2004. Extraction and physico-chemical characterisation of Nile perch (Lates niloticus) skin and bone gelatin. Food Hydrocolloid, 18: 581-592.
Liu, H.Y., J. Han and S.D. Guo, 2009. Characteristics of the gelatin extracted from Channel Catfish (Ictalurus punctatus) head bones. LWT-Food Sci. Technol., 42: 540-544.
Arsyanti, L., Y. Erwanto, A. Rohman and Y. Pranoto, 2018. Chemical composition and characterization of skin gelatin from buffalo (Bubalus bubalis). Int. Food Res. J., 25: 1095-1099.
Said, M.I., 2011. Optimation goat skin gelatin production process as a raw material for edible film packaging material medicine (capsule). Ph.D. Thesis, Graduate Program Faculty of Animal Husbandry, Universitas Gadjah Mada, Yogyakarta, Indonesia.
Laemmli, U.K., 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227: 680-685.
Pranoto, Y., C.M. Lee and H.J. Park, 2007. Characterizations of fish gelatin films added with gellan and κ-carrageenan. LWT-Food Sci. Technol., 40: 766-774.
Anonymus, 1993. Waters ACCQ tag chemistry package. Manual Number WAT 052874, Water Millipore Coorporation, 34 Maple Street Milford, MA 01757, USA.
Chamidah, A. and C. Elita, 2002. The effect of treatment on quality of gelatin sharks. Proceedings of the National Seminar PATPI, July 30-31, 2002, Malang, Indonesia.
Handoko, T., S.O. Rusli and I. Sandy, 2011. Effect of type and acid concentration, temperature and extraction time on the characteristics of the waste fish glue fish mackerel. Reactor. J., 14: 237-241.
Mulyani, S., F.M.C.S. Setyabudi, Y. Pranoto and U. Santoso, 2017. Physicochemical properties of gelatin extracted from buffalo hide pretreated with different acids. Korean J. Food Sci. Anim. Resour., 35: 708-715.
Wulandari, D., S. Triatmojo, Y. Erwanto and Y. Pranoto, 2016. Physicochemical Properties and Amino Acid and Functional Group Profiles of Gelatin Extracted from Bovine Split Hide Cured by Acid Pak. J. Nutr., 15: 655-661.
Mad-Ali, S., S. Benjakul, T. Prodpran and S. Maqsood, 2016. Characteristics and gel properties of gelatin from goat skin as influenced by alkaline-pretreatment conditions. Asian-Aust. J. Anim. Sci., 29: 845-854.
Ulfah, M., 2011. Influence of the concentration of acetic acid solution and the duration of immersion to the properties of gelatin scribble. Agric. J., 31: 161-167.
Anonymous, 2005. Mutu dan cara uji gelatin. The Indonesian National Standard (SNI) No. 06-3735-1995, The National Standards Council.
GMIA., 2012. Gelatin Handbook. Gelatin Manufacturers Institute of America, USA., Pages: 26.
Rosli, N. and N.M. Sarbon, 2015. Physicochemical and structural properties of Asian Swamp eel (Monopterus albus) skin gelatin as compared to bovine gelatin. Int. Food. Res. J., 22: 699-706.
Wulandari, D., 2006. Extraction and characteristics of the skin gelatin chicken legs. M.Sc. Thesis, Animal Science Studies Program, Gadjah Mada University, Yogyakarta, Indonesia.
Sompie, M., 2014. Characteristics of edible film made from pig skin gelatin as a packaging pork. Ph.D. Thesis, Graduate Program Faculty of Animal Husbandry, Gadjah Mada University, Yogyakarta, Indonesia.
Choi, S.S. and J.M. Regenstein, 2000. Physicochemical and sensory characteristics of fish gelatin. J. Food Sci., 65: 194-199.
Amiza, M.A., W.M. Shima, N.I. Hayati and N.M. Juhaida, 2015. Optimization of gelatinextractiob condition from Cobia (Rachycentron canadum) skin and its physicochemical characteristics as compared to bovine gelatin. Int. Food. Res. J., 22: 213-224.
Jamhari, 2014. Study of bioactive peptides from local cattle meat protein angensia Indonesia as an antihypertensive. Ph.D. Thesis, Graduate Program Faculty of Animal Husbandry, Universitas Gadjah Mada, Yogyakarta, Indonesia.
Leiner Davis Gelatin Co., 2000. Gelatine structure. Leiner Davis Gelatin Co. http://www.gelatin.com.
Muyonga, J.H., C.G.B. Cole and K.G. Duodu, 2004. 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., 86: 325-332.
Kolodziejska, I., K. Kaczorowski, B. Piotrowska and M. Sadows, 2004. Modification of the properties of gelatin from skins of Baltic cod (Gadus morhua) with transglutaminase. Food Chem., 86: 203-209.
Binsi, P.K., B.A. Shamasundar, A.O. Dileep, F. Badii and N.K. Howell, 2009. Rheological and functional properties of gelatin from the skin of Bigeye snapper (Priacanthus hamrur) fish: Influence of gelatin on the gel-forming ability of fish mince. Food Hydrocolloids, 23: 132-145.
Astawan, M. and T. Aviana, 2002. The effect of this type of submersion solution as well as the drying method on the physical, chemical and functional properties of gelatin from the skin of a coke. Proceedings of the National Seminar PATPI, July 30-31, 2002, Malang, Indonesia.
Jridi, M., R. Nasri, R.B.S.B. Salem, I. Lassoued, A. Barkia, M. Nasri and N. Souissi, 2015. Chemical and biophysical properties of gelatins extracted from the skin of octopus (Octopus vulgaris). LWT-Food Sci. Technol., 60: 881-889.
Mulyani, S., F.M.C.S. Setyabudi, Y. Pranoto and U. Santoso, 2016. The physical properties of gelatin from buffalo hide by pretreatment using citric acid. Proceedings of the 1st International Conference on Biodiversity, Food Security and Health, November 22-23, 2016, Gadjah Mada University, Yogyakarta, Indonesia.
Baynes, J.W., V.M. Monier, J.M. Ames and S.R. Thorpe, 2007. The Maillard Reaction: Chemistry at the Interface of Nutrition, Aging and Diseases. New York Academy of Science, New York, ISBN: 1-57331-1043-954.
Son, S.M., K.D. Moon and C.Y. Lee, 2000. Rhubarb juice as a natural antibrowning agent. J. Food Sci., 65: 1288-1289.
Harrison, T.J. and G.R. Dake, 2005. An expeditious, high-yielding construction of the food aroma compounds 6-acetyl-1,2,3,4-tetrahydropyridine and 2-acetyl-1-pyrroline. J. Org. Chem., 70: 10872-10874.
Lee, C.Y., 2000. Book review: Fruit and vegetable quality: An integrated view 'ed. By T.L. Shewfelt & Bruchner, Technomic Publishing Co. Texture Stud., 31: 356-359.
Badii, F. and K.H. Nazlin, 2006. Fish gelatin: Structure, gelling properties and interaction with egg albumen proteins. Food Hydrocolloids, 20: 630-640.
Nagai, T., N. Suzuki and T. Nagashima, 2008. Collagen from common minke whale (Balaenoptera acutorostrata) unesu. Food Chem., 111: 296-301.
Duan, R., J. Zhang, X. Dua, X. Yao and K. Konno, 2009. Properties of collagen from skin, scale and bone of carp (Cyprinus carpio). Food Chem., 112: 702-706.
Azira, T.N., I. Amin and Y.B.C. Man, 2012. Differentiation of bovine and porcine gelatins in processed products via Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) and principal component analysis (PCA) techniques. Int. Food Res. J., 19: 1175-1180.
Nurul, A.G. and N.M. Sarbon, 2015. Effects of pH on functional, rheological and structural properties of eel (Monopterus sp.) skin gelatin compared to bovine gelatin. Int. Food Res. J., 22: 572-583.
Rohman, A., 2014. Vibrational Spectroscopy. 1st Edn., Gadjah Mada University Press, Indonesia, pp: 1-27.
Charley, H., 1982. Encyclopedia of Food Science and Technology. John Wiley and Sons Inc., New York, pp: 1183-1188.
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