PMID- 29580524 OWN - NLM STAT- MEDLINE DCOM- 20190930 LR - 20190930 IS - 1873-7145 (Electronic) IS - 0963-9969 (Linking) VI - 107 DP - 2018 May TI - Investigation on complex coacervation between fish skin gelatin from cold-water fish and gum arabic: Phase behavior, thermodynamic, and structural properties. PG - 596-604 LID - S0963-9969(18)30146-7 [pii] LID - 10.1016/j.foodres.2018.02.053 [doi] AB - The study is aimed to investigate phase behavior, thermodynamic, and structural properties based on complex coacervation between fish skin gelatin (FSG) from cold-water fish and gum arabic (GA). Phase separation behavior between FSG and GA was investigated as a function of pH through varying mixing ratios from 4:1 to 1:4 at 25  degrees C and 1.0 wt% of total biopolymer concentration. The turbidity of FSG-GA mixture reached the maximum (1.743) at the 1:2 of mixing ratio and pH(opt) 3.5, and stabilized at zero. Then physicochemical properties of FSG-GA coacervates at pH(opt) 3.5 and FSG-GA mixtures at pH 6.0 (>pH(c)) were evaluated. Scanning electron microscope (SEM) and X-ray diffraction (XRD) showed that the interactions between FSG and GA occurred at pH(opt) 3.5 and were very weak at pH 6.0 (>pH(c)). The isothermal titration calorimetry (ITC) results including the negative Gibbs free energy change (DeltaG = -18.71 +/- 1.300 kJ/mol), binding enthalpy (DeltaH = -41.81 +/- 1.300 kJ/mol) and binding entropy (TDeltaS = -23.10 kJ/mol) indicated that the complexation between FSG and GA was spontaneous and driven by negative enthalpy owing to the electrostatic interaction and hydrogen bondings. The zeta potential (ZP) of FSG-GA coacervates at pH(opt) 3.5 was -9.00 +/- 0.79 mV that was not close to electrically neutral, indicating other interactions besides electronic interaction. Hydrogen bondings in FSG-GA mixtures at pH 6.0 and 3.5 were found to be stronger than pure FSG at pH 6.0 and 3.5 owing to that the amide II peaks shifted to high wavenumbers. Electronic interaction was proven to exist in FSG-GA mixtures at pH 6.0 through the vanishment of asymmetric COO(-) stretching. However, the electronic interaction in FSG-GA coacervates at pH(opt) 3.5 was obviously stronger than FSG-GA mixtures at pH 6.0, resulting from the vanishment of asymmetric and symmetric COO(-) stretching vibration and the positively charged FSG and GA. The intrinsic fluorescence represented that the introduction of GA changed the microenvironment of tyrosine residues in FSG, which may be owing to the unfolding of the tertiary conformation. Moreover, the decrease of pH could promote the formation of random coils of FSG through circular dichroism (CD). Therefore the addition of GA into FSG and decrease of pH might enhance the conformation freedom of FSG, which would bring about favorable entropic effects and contribute to the complexation. CI - Copyright (c) 2018 Elsevier Ltd. All rights reserved. FAU - Li, Yong AU - Li Y AD - National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, PR China. FAU - Zhang, Xiyue AU - Zhang X AD - National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, PR China. FAU - Zhao, Yu AU - Zhao Y AD - National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, PR China. FAU - Ding, Jie AU - Ding J AD - National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, PR China. FAU - Lin, Songyi AU - Lin S AD - National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, PR China. Electronic address: linsongyi730@163.com. LA - eng PT - Comparative Study PT - Journal Article PT - Research Support, Non-U.S. Gov't DEP - 20180321 PL - Canada TA - Food Res Int JT - Food research international (Ottawa, Ont.) JID - 9210143 RN - 9000-01-5 (Gum Arabic) RN - 9000-70-8 (Gelatin) SB - IM MH - Animals MH - Calorimetry MH - Circular Dichroism MH - *Fishes MH - Food Handling/*methods MH - Gelatin/*chemistry/isolation & purification MH - Gum Arabic/*chemistry MH - Hydrogen Bonding MH - Hydrogen-Ion Concentration MH - Light MH - Microscopy, Electron, Scanning MH - Protein Structure, Tertiary MH - Protein Unfolding MH - Scattering, Radiation MH - Skin/*chemistry MH - Spectroscopy, Fourier Transform Infrared MH - Static Electricity MH - Structure-Activity Relationship MH - Thermodynamics MH - Time Factors MH - X-Ray Diffraction OTO - NOTNLM OT - Complex coacervation OT - Fish skin gelatin OT - Gum arabic EDAT- 2018/03/28 06:00 MHDA- 2019/10/01 06:00 CRDT- 2018/03/28 06:00 PHST- 2017/10/02 00:00 [received] PHST- 2018/01/30 00:00 [revised] PHST- 2018/02/21 00:00 [accepted] PHST- 2018/03/28 06:00 [entrez] PHST- 2018/03/28 06:00 [pubmed] PHST- 2019/10/01 06:00 [medline] AID - S0963-9969(18)30146-7 [pii] AID - 10.1016/j.foodres.2018.02.053 [doi] PST - ppublish SO - Food Res Int. 2018 May;107:596-604. doi: 10.1016/j.foodres.2018.02.053. Epub 2018 Mar 21.