Abstract
Physicochemical properties of giant salamander skin gelatin (GSSG) prepared at 45, 50, 55, 60, 65 °C were studied in comparison with those of tiger puffer skin gelatin (TPSG) and commercial bovine gelatin (CBG). It is showed that GSSG contained lower content of imino acid (179–181 residues/1000) than CBG (204 residues/1000) and TPSG (188 residues/1000). GSSG45 exhibited a protein pattern with α1- and β-chain, which attenuated along with the formation of fragments with molecule weight < 97.2 KD when extraction temperature increased. Amide I and II of GSSG were shifted to higher wavenumber while amide A and B to lower wavenumber in parallel with declined peak (7.3°) intensity by X-ray analysis as temperature increased. Gel strength, gelling temperature and melting temperature of GSSG (47–122 g, 9.30–12.18 °C and 16.87–21.34 °C) were lower than those of CBG (160 g, 22.01 °C and 28.70 °C) and TPSG (151 g, 13.90 °C and 21.34 °C) (p < 0.05). They decreased as temperature elevated in consistent with their gel microstructure with big size voids. These also coincided with their longer relaxation time showed by low field-nuclear magnetic resonance. GSSG50 (62.3 m2/g, 57.5 min) and GSSG55 (55.6 m2/g, 60.8 min) showed higher emulsion activity index and emulsion stability index (p < 0.05) as well as smaller size emulsion droplets than others. Results indicate that GSSG has poor gelling properties, but excellent emulsifying properties. They are greatly affected by extraction temperature. GSSG is proposed to be extracted at a temperature between 45 and 50 °C.
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P. Kaewruang, S. Benjakul, T. Prodpran, S. Nalinanon, Food Biosci. 2, 1–9 (2013)
G. Boran, J.M. Regenstein, J. Food Sci. 74(8), 432–441 (2009)
T. Aewsiri, S. Benjakul, W. Visessanguan, Food Chem. 115(1), 243–249 (2009)
M. Nikoo, S. Benjakul, M. Bashari et al., Food Biosci. 5(5), 19–26 (2014)
I. Kołodziejska, E. Skierka, M. Sadowska, W. Kołodziejski, C. Niecikowska, Food Chem. 107(2), 700–706 (2008)
J. Pan, Q. Li, H. Jia et al., Int. J. Biol. Macromol. 109, 1045–1053 (2018)
S. Sinthusamran, S. Benjakul, H. Kishimura, Food Chem. 152, 276–284 (2014)
P. Kittiphattanabawon, S. Benjakul, S. Sinthusamran, H. Kishimura, LWT - Food Sci. Technol. 66, 186–192 (2016)
Y. Liu, L. Xia, H. Jia et al., J. Sci. Food Agric. 97(15), 5406–5413 (2017)
Z. Qi, Q. Zhang, Z. Wang et al., Vet. Immunol. Immunopathol. 169, 85–95 (2016)
A.A. Cunningham, S.T. Turvey, F. Zhou et al., Oryx 50(2), 265–273 (2015)
B. Zhu, X. Dong, D. Zhou et al., Food Hydrocolloids 28(1), 182–188 (2012)
BSI, Methods for Sampling and Testing Gelatin (Physical and Chemical Methods) (British Standard Institution, BS 757, London, 1975)
G. Boran, S.J. Mulvaney, J.M. Regenstein, J. Food Sci. 75(8), E565–E571 (2010)
X. Dong, Y. Li, Y. Li et al., Food Anal. Methods 10(7), 2207–2216 (2017)
B.E. Abdelmalek, J. Gómez-Estaca, A. Sila et al., LWT - Food Sci. Technol. 65, 924–931 (2016)
J.M. Koli, S. Basu, B.B. Nayak, S.B. Patange, A.U. Pagarkar, V. Gudipati, Food Bioprod. Process. 90(3), 555–562 (2012)
Q. Zhang, Q. Wang, S. Lv et al., Food Biosci. 13, 41–48 (2016)
D.A. Ledward, Gelation of gelatin, in Functional Properties of Food Macromolecules, ed. by J.R. Mitchell, D.A. Ledward (Elsevier Applied Science Publishers, London, 1986), pp. 171–201
M.C. Gómez-Guillén, J. Turnay, M.D. Fernández-Dı́az, N. Ulmo, M.A. Lizarbe, P. Montero, Food Hydrocolloids 16(1), 25–34 (2002)
P. Kittiphattanabawon, S. Benjakul, W. Visessanguan, F. Shahidi, Food Hydrocolloids 24(2–3), 164–171 (2010)
J.H. Muyonga, C.G.B. Cole, K.G. Duodu, Food Chem. 85(1), 81–89 (2004)
J. Bandekar, Biochem. Biophys. Acta 1120(2), 123–143 (1992)
M. Jackson, L.-P.I. Choo, P.H. Watson, W.C. Halliday, H.H. Mantsch, Biochem. Biophys. Acta 1270(1), 1–6 (1995)
J.H. Muyonga, C.G.B. Cole, K.G. Duodu, Food Chem. 86(3), 325–332 (2004)
M. Nagarajan, S. Benjakul, T. Prodpran, P. Songtipya, H. Kishimura, Food Hydrocolloids 29(2), 389–397 (2012)
B.B. Doyle, E.G. Bendit, E.R. Blout, Biopolymers 14(5), 937–957 (1975)
X.-M. Sha, Z.-C. Tu, W. Liu et al., Food Hydrocolloids 36, 173–180 (2014)
A. Bigi, S. Panzavolta, K. Rubini, Biomaterials 25(25), 5675–5680 (2004)
T. Sae-leaw, S. Benjakul, N.M. O'Brien, LWT - Food Sci. Technol. 65, 661–667 (2016)
P. Kaewruang, S. Benjakul, T. Prodpran, Food Chem. 138(2–3), 1431–1437 (2013)
A.M.M. Ali, H. Kishimura, S. Benjakul, Food Hydrocolloids 82, 164–172 (2018)
Z. Khiari, D. Rico, A.B. Martin-Diana, C. Barry-Ryan, J. Mater. Cycles Waste Manag. 19(1), 180–191 (2017)
U. Erikson, I.B. Standal, I.G. Aursand, E. Veliyulin, M. Aursand, Magn. Reson. Chem. 50(7), 471–480 (2012)
H.C. Bertram, A.H. Karlsson, M. Rasmussen, O.D. Pedersen, S. Dønstrup, H.J. Andersen, J. Agric. Food Chem. 49(6), 3092–3100 (2001)
M. Han, P. Wang, X. Xu, G. Zhou, Food Res. Int. 62, 1175–1182 (2014)
Acknowledgements
This work was supported by the National Key R&D Program of China (2016YFD0400700, 2016YFD0400703), Dalian Municipality Youth Science and Technology Star Fund (2018RQ17). J.P. was financially supported by the Ministry of Education, Youth and Sports of the Czech Republic—project CENAKVA (LM2018099), CENAKVA Center Development (CZ.1.05/2.1.00/19.0380) and Biodiversity (CZ.02.1.01/0.0/0.0/16_025/0007370) for analyses in Czech.
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Pan, J., Lian, H., Shang, M. et al. Physicochemical properties of Chinese giant salamander (Andrias davidianus) skin gelatin as affected by extraction temperature and in comparison with fish and bovine gelatin. Food Measure 14, 2656–2666 (2020). https://doi.org/10.1007/s11694-020-00512-2
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DOI: https://doi.org/10.1007/s11694-020-00512-2