Investigation on the coacervation of fish scale gelatin hydrogel with seafood waste hydrolysates for the development of artificial fish bait: Physico-chemical, thermodynamic, and morpho-structural properties

Abstract

The study dealt with the development of biopolymer based hydrogel artificial fish bait with hydrolysates derived from fish processing wastes. Fish scale gelatin (FSG) was used for the development of a hydrogel to which bioattractants extracted from seafood processing wastes of fish, squid and shrimp were added to prepare composite gels such as FSG-FH, FSG-SH and FSG-SPH, respectively. To understand the homogenesity and cross linking complexation of composite gels, the study aimed at investigating physico-chemical, thermodynamic, molecular and structural properties were analysed. The gel strength, melting point and thermal stability of the composite hydrogels were found to decrease marginally compared to the control gel, FSG. It could be understood that the crystalline structure at 2θ = 23° of the FSG-SH, and FSG-FH were not much altered compared to FSG gel. However, alteration in the crystalline structure in FSG-SPH was evident at 2θ = 27.3°. The TGA and DSC analysis revealed the reduction in the thermal stability of FSG on the addition of protein hydrolysates in the process of coacervation to get hydrogel based fish bait. Further, FESEM and AFM analysis indicated FSG-SH as the composite hydrogel with most compact and smooth surface was evident by Ra and Rq values. Among the composite gels, FSG-SH was found to have higher hydrophobicity due to enhanced gel structure. FTIR spectra of FSG and composite gels exhibitted similarity corresponding to amide-A, B, I, II and III bands. However, NMR analysis revealed the existence of notable difference with respect to chemical shift in the range of 7.0–7.75 ppm expressing the presence of aromatic protons of the amino acid phe and N–H protons of amide in all the composite gels. Further, NMR analysis confirmed the role of imino acids (δ CH2 & β CH2 protons) and hydrophobic amino acids (α-CH2 protons) in decrease the physical and thermal properties of the composite gels. The addition of protein hydrolysates with FSG was found to decrease the physical, thermal and structural properties, however improve the aromatic compounds of the composite gels.