Bioactivity Potentials and General Applications of Fish Protein Hydrolysates

International Journal of Peptide Research and Therapeutics - Fish protein hydrolysates (FPHs) are rich source of amino acids and peptides that are beneficial to human health. Industrially, when...     

Physical and chemical properties of gelatin from the skin of cultured Amur sturgeon (Acipenser schrenckii)

To expand the usefulness of cultured Amur sturgeon, Acipenser schrenckii, its skin was used to explore the production of gelatin. After acetic acid pre‐treatment (0.05 m for 3 h), gelatin was extracted at temperatures of 50 or 70°C for 1 or 6 h. Gelatin yield ranged from 9.42 to 12.47% (wet weight basis) (P < 0.05). With increasing extraction time and temperature, the content of imino acids (proline + hydroxyproline), gel strength and L*‐value (lightness) decreased, while the a*‐value (redness) and b*‐value (yellowness) of gelatin gel increased (P < 0.05). Electrophoretic analysis revealed that α‐chains and β‐chains were predominant components in all extracted gelatins. Higher molecular weight proteins (γ‐chain) were also observed. Gelling and melting temperatures of gelatin were 13.6–14.6°C and 20.3–22.6°C, respectively. Circular dichroism (CD) spectra and Fourier transform infrared (FTIR) spectroscopy revealed the triple helix loss in gelatin (A₁₂₃₅ (AIII)/A₁₄₅₁ < 1). Extraction conditions caused secondary structure changes in the gelatin. More likely due to the differences in the culture water temperature, gelatin exhibited gelling and melting temperatures intermediate between those of cold‐ and warm‐water fish gelatins. The obtained gelatin can be used in food products or in the production of bioactive compounds.     

Properties of blend film based on cuttlefish (Sepia pharaonis) skin gelatin and mungbean protein isolate

Blend films based on cuttlefish (Sepia pharaonis) ventral skin gelatin (CG) and mungbean protein isolate (MPI) at different blend ratios (CG/MPI = 10:0, 8:2, 6:4, 4:6, 2:8 and 0:10, w/w) prepared at pH 11 using 50% glycerol (based on total protein) as plasticizer were characterized. CG films incorporated with MPI at increasing amounts had the decreases in tensile strength (TS) (p < 0.05). The increases in elongation at break (EAB) were observed when CG/MPI ratios of 6:4 or 4:6 were used (p < 0.05). Decreased water vapor permeability (WVP) was obtained for films having the increasing proportion of MPI (p < 0.05). CG/MPI blend films with higher MPI proportion had lower film solubility and L*-values (lightness) but higher b*-values (yellowness) and ΔE*-values (total color difference) (p < 0.05). Electrophoretic study revealed that disulfide bond was present in MPI and CG/MPI blend films. However, hydrogen bonds between CG and MPI in the film matrix were dominant, as elucidated from FTIR spectroscopic analysis. Moreover, thermal stability of CG/MPI blend film was improved as compared to that of films from respective single proteins. Differential scanning calorimetry result suggested solid-state morphology of CG/MPI (6:4) blend film that consisted of amorphous phase of partially miscible CG/MPI mixture and the coexisting two different order phases of individual CG and MPI domains. Thus, the incorporation of MPI into gelatin film could improve the properties of resulting blend film, which were governed by CG/MPI ratio.