References

• AOAC. (2005). Official Methods of Analysis of Association of Official analytical Chemists International (18th ed.). Gaithersburg, USA: AOAC International.
   Google Scholar
• Belitz, H.D., Grosch, W., & Schieberle, P. (2009). Food Chemistry (4th Revised and Extended ed.). Berlin, Germany: Springer Verlag.
   Google Scholar
• Bessho, M., Furuta, M., Kojima, T., Okuda, S., & Hara, M. (2005). Gelatin hydrogels cross-linked by γ-ray irradiation: Materials for absorption and release of dye. Journal of Biomaterials Science Polymer Edition, 16, 715–724. doi:10.1163/1568562053992478
   PubMed Web of Science ®Google Scholar
• Bhat, R., & Karim, A.A. (2009). Ultraviolet irradiation improves gel strength of fish gelatin. Food Chemistry, 113, 1160–1164. doi:10.1016/j.foodchem.2008.08.039
   Web of Science ®Google Scholar
• Bigi, A., Cojazzi, G., Panzavolta, S., Roveria, N., & Rubini, K. (2002). Stabilization of gelatin films by crosslinking with genipin. Biomaterials, 23, 4827–4832. doi:10.1016/S0142-9612(02)00235-1
   PubMed Web of Science ®Google Scholar
• Bigi, A., Cojazzi, G., Panzavolta, S., Rubini, K., & Roveri, N. (2001). Mechanical and thermal properties of gelatin films at different degrees of glutaraldehyde crosslinking. Biomaterials, 22, 763–768. doi:10.1016/S0142-9612(00)00236-2
   PubMed Web of Science ®Google Scholar
• Boanini, E., Rubini, K., Panzavolta, S., & Bigi, A. (2010). Chemico-physical characterization of gelatin films modified with oxidized alginate. Acta Biomaterialia, 6, 383–388. doi:10.1016/j.actbio.2009.06.015
   PubMed Web of Science ®Google Scholar
• Cao, N., Fu, Y., & He, J. (2007). Mechanical properties of gelatin films cross-linked, respectively, by ferulic acid and tannin acid. Food Hydrocolloids, 21, 575–584. doi:10.1016/j.foodhyd.2006.07.001
   Web of Science ®Google Scholar
• Chang, C.-H., & Zhao, X.-H. (2012). In vitro digestibility and rheological properties of caseinates treated by an oxidative system containing horseradish peroxidase, glucose oxidase and glucose. International Dairy Journal, 27, 47–52. doi:10.1016/j.idairyj.2012.07.004
   Web of Science ®Google Scholar
• Comfort, S., & Howell, N.K. (2002). Gelation properties of soya and whey protein isolate mixtures. Food Hydrocolloids, 16, 661–672. doi:10.1016/S0268-005X(02)00033-4
   Web of Science ®Google Scholar
• Damodaran, S., & Agyare, K.K. (2013). Effect of microbial transglutaminase treatment on thermal stability and pH-solubility of heat-shocked whey protein isolate. Food Hydrocolloids, 30, 12–18. doi:10.1016/j.foodhyd.2012.04.012
   Web of Science ®Google Scholar
• Davies, K.J., Delsignore, M.E., & Lin, S.W. (1987). Protein damage and degradation by oxygen radical. II. Modification of amino acids. Journal of Biological Chemistry, 262, 9902–9907.
   PubMed Web of Science ®Google Scholar
• De Carvalho, R.A., & Grosso, C.R.F. (2004). Characterization of gelatin based films modified with transglutaminase, glyoxal and formaldehyde. Food Hydrocolloids, 18, 717–726. doi:10.1016/j.foodhyd.2003.10.005
   Web of Science ®Google Scholar
• Derkatch, S.R., Petrova, L.A., Izmailova, V.N., & Tarasevitch, B.N. (1999). Properties of emulsion films made from binary aqueous mixtures of gelatin-surfactant: The effect of concentration and pH. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 152, 189–197. doi:10.1016/S0927-7757(98)00615-3
   Web of Science ®Google Scholar
• Gilsenan, P.M., & Ross-Murphy, S.B. (2000). Rheological characterisation of gelatins from mammalian and marine sources. Food Hydrocolloids, 14, 191–195. doi:10.1016/S0268-005X(99)00050-8
   Web of Science ®Google Scholar
• Gómez-Guillén, M.C., Sarabia, A.I., Solas, M.T., & Montero, P. (2001). Effect of microbial transglutaminase on the functional properties of megrim (Lepidorhombus boscii) skin gelatin. Journal of the Science of Food & Agriculture, 81, 665–673. doi:10.1002/jsfa.865
   Web of Science ®Google Scholar
• Gómez-Guillén, M.C., Turnay, J., Fernández-Díaz, M.D., Ulmo, N., Lizarbe, M.A., & Montero, P. (2002). Structural and physical properties of gelatin extracted from different marine species: A comparative study. Food Hydrocolloids, 16, 25–34. doi:10.1016/S0268-005X(01)00035-2
   Web of Science ®Google Scholar
• Hunter, R.J. (1981). Zeta Potential in Colloid Science. London: Academic Press.
   Google Scholar
• Jiang, P., & Zhao, X.-H. (2014). Gelation and in vitro Digestibility of Soybean Protein Isolate Treated by a Ternary System Containing Horseradish Peroxidase, Glucose Oxidase, and Glucose. International Journal of Food Properties, 17, 2284–2297. doi:10.1080/10942912.2013.798737
   Web of Science ®Google Scholar
• Jongjareonrak, A., Benjakul, S., Visessanguan, W., & 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, 1216–1222. doi:10.1016/j.foodhyd.2006.01.006
   Web of Science ®Google Scholar
• Kadar, E., Batalha, Í.L., Fisher, A., & Roque, A.C.A. (2014). The interaction of polymer-coated magnetic nanoparticles with seawater. Science of the Total Environment, 487, 771–777. doi:10.1016/j.scitotenv.2013.11.082
   PubMed Web of Science ®Google Scholar
• Kaewruang, P., Benjakul, S., & Prodpran, T. (2013). Molecular and functional properties of gelatin from the skin of unicorn leatherjacket as affected by extracting temperatures. Food Chemistry, 138, 1431–1437. doi:10.1016/j.foodchem.2012.09.114
   PubMed Web of Science ®Google Scholar
• Karim, A.A., & Bhat, R. (2009). Fish gelatin: Properties, challenges, and prospects as an alternative to mammalian gelatins. Food Hydrocolloids, 23, 563–576. doi:10.1016/j.foodhyd.2008.07.002
   Web of Science ®Google Scholar
• Kuijpers, A.J., Engbers, G.H.M., Feijen, J., De Smedt, S.C., Meyvis, T.K.L., Demeester, J., … Dankert, J. (1999). Characterization of the network structure of carbodiimide cross-linked gelatin gels. Macromolecules, 32, 3325–3333. doi:10.1021/ma981929v
   Web of Science ®Google Scholar
• Kuraishi, C., Yamazaki, K., & Susa, Y. (2001). Transglutaminase: Its utilization in the food industry. Food Reviews International, 17, 221–246. doi:10.1081/FRI-100001258
   Web of Science ®Google Scholar
• Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685. doi:10.1038/227680a0
   PubMed Web of Science ®Google Scholar
• Lam, R.S.H., & Nickerson, M.T. (2014). The effect of pH and heat pre-treatments on the physicochemical and emulsifying properties of β-lactoglobulin. Food Biophysics, 9, 20–28. doi:10.1007/s11483-013-9313-4
   Web of Science ®Google Scholar
• Luo, Z.L., & Zhao, X.H. (2014). Caseinate-gelatin and caseinate-hydrolyzed gelatin composites formed via transglutaminase: Chemical and functional properties. Journal of the Science of Food & Agriculture. doi:10.1002/jsfa.7042
   Web of Science ®Google Scholar
• Matsuda, S., Iwata, H., Se, N., & Ikada, Y. (1999). Bioadhesion of gelatin films crosslinked with glutaraldehyde. Journal of Biomedical Materials Research, 45, 20–27. doi:10.1002/(ISSN)1097-4636
   PubMed Web of Science ®Google Scholar
• Matthews, B.A., & Rhodes, C.T. (1968). The use of the Coulter Counter for investigating the coagulation kinetics of mixed monodisperse particulate systems. Journal of Colloid & Interface Science, 28, 71–81. doi:10.1016/0021-9797(68)90209-9
   Web of Science ®Google Scholar
• Mohtar, N.F., Perera, C.O., Quek, S.-Y., & Hemar, Y. (2013). Optimization of gelatine gel preparation from New Zealand hoki (Macruronus novaezelandiae) skins and the effect of transglutaminase enzyme on the gel properties. Food Hydrocolloids, 31, 204–209. doi:10.1016/j.foodhyd.2012.10.011
   Web of Science ®Google Scholar
• Muyonga, J.H., Cole, C.G.B., & Duodu, K.G. (2004). Extraction and physico-chemical characterisation of Nile perch (Lates niloticus) skin and bone gelatine. Food Hydrocolloids, 18, 581–592. doi:10.1016/j.foodhyd.2003.08.009
   Web of Science ®Google Scholar
• Olijve, J., Mori, F., & Toda, Y. (2001). Influence of the molecular-weight distribution of gelatin on emulsion stability. Journal of Colloid & Interface Science, 243, 476–482. doi:10.1006/jcis.2001.7816
   Web of Science ®Google Scholar
• Schrieber, R., & Gareis, H. (2007). Gelatine handbook: Theory and industrial practice. Weinheim: Wiley-VCH Verlag GmbH. KGaA.
   Google Scholar
• Silverstein, P.M., Webster, F.X., & Kiemle, D.J. (2005). Spectrometric Identification of Organic Compounds. Hoboken, NJ: John Wiley & Sons Press.
   Google Scholar
• Sobral, P.J.A., Menegalli, F.C., Hubinger, M.D., & Roques, M.A. (2001). Mechanical, water vapor barrier and thermal properties of gelatin based edible films. Food Hydrocolloids, 15, 423–432. doi:10.1016/S0268-005X(01)00061-3
   Web of Science ®Google Scholar
• Stahmann, M.A., Spencer, A.K., & Honold, G.R. (1977). Cross linking of proteins in vitro by peroxidase. Biopolymers, 16, 1307–1318. doi:10.1002/(ISSN)1097-0282
   PubMed Web of Science ®Google Scholar
• Vemulapalli, V., & Hoseney, R.C. (1998). Glucose Oxidase Effects on Gluten and Water Solubles 1. Cereal Chemistry, 75, 859–862. doi:10.1094/CCHEM.1998.75.6.859
   Web of Science ®Google Scholar
• Weber, C., Coester, C., Kreuter, J., & Langer, K. (2000). Desolvation process and surface characterisation of protein nanoparticles. International Journal of Pharmaceutics, 194, 91–102. doi:10.1016/S0378-5173(99)00370-1
   PubMed Web of Science ®Google Scholar
• Wu, D., Xu, G., Sun, Y., Zhang, H., Mao, H., & Feng, Y. (2007). Interaction between proteins and cationic gemini surfactant. Biomacromolecules, 8, 708–712. doi:10.1021/bm061033v
   PubMed Web of Science ®Google Scholar
• Zhang, J.-J., Gu, M.-M., Zheng, T.-T., & Zhu, J.-J. (2009). Synthesis of gelatin-stabilized gold nanoparticles and assembly of carboxylic single-walled carbon nanotubes/Au composites for cytosensing and drug uptake. Analytical Chemistry, 81, 6641–6648. doi:10.1021/ac900628y
   PubMed Web of Science ®Google Scholar