Functional properties of enzymatically modified protein from fish waste

Fish flour from dried waste consisting of head, tail, fins and entrails was enzimatically hydrolysed using various proteases and the hydrolysate was spray dried. The functional properties such as water-fat absorption ratio, foaming and solubility index of the hydrolysates and fish flour revealed that some of the products might find significant uses in the food and/or cosmetics industry. Electrophoretic separation of the proteins from the fish flour and of the hydrolysates indicated that almost all the flour proteins are susceptible to proteolytic cleavage with the exception of one or two. The extent of degree of hydrolysis from 43-70.3% with a simultaneous decrease in unpleasant smell suggest an economical tool for minimizing odour pollution due to fish industry waste deterioration.

Comparative evaluation of fish protein concentrate and functional fish protein concentrate from cat fish

Fish protein concentrate and functional fish protein concentrate samples were prepared from eviscerated meat of cat fish (Tachysurus jella Day). Functional fish protein concentrate is found to be lighter, less gritty and rehydrates more rapidly than fish protein concentrate. Functional FPC is seen to have higher PER and biscuits containing it at levels of 5 and 7 percent are less hard compared to FPC.

Structural and functional properties of the hemoglobin components from the Caspian Sea Acipenser persicus and Acipenser stellatus

Hemoglobin (Hb) variability is a commonly used index of phylogenetic differentiation and molecular adaptation in fish. In the current study, the structural and functional characteristics of Hbs from two Sturgeon species of the Southern Caspian Sea Basin were investigated. After extraction and separation of hemoglobin from whole blood , the polyacrylamide gel electrophoresis (SDSPAGE), native-PAGE and isoelectric focusing (IEF) were used to confirm Hb variability in these fishes. Ion-exchange on CM-cellulose chromatography was used for purification of the dominant Hbs from these fishes. The accuracy of the methods was confirmed by IEF and SDS-PAGE. Spectral studies using fluorescence spectrophotometery, circular dichroism spectropolarimetry (CD) analysis and UV–vis spectrophotometery. Oxygen affinities of these Hbs were compared using Hb-oxygen dissociation curves. Also, the dominant Hbs from these blood fishes were utilized for further experiments. The behavior of Hbs during the denaturation process by n-dodecyl trimethylammonium bromide (DTAB) is investigated by UV–vis spectrophotometer and circular dichroism spectropolarimetry. The thermal denaturation properties of the Hbs wereinvestigated by differential scanning calorimetry (DSC) and Hbs aggregation performed chemically in the presence of dithiotreitol (DTT) by UV–vis spectrophotometer and chemometric study. The results demonstrate a significant relationship between stability of fish hemoglobins and the ability of fish for entering to deeper depths. The UV–Vis absorption spectra identified species of hemoglobin and showed the concentration of oxyHb and metHb decreases and deoxyHb increases upon interaction with DTAB. Besides the UV–vis spectrophotometry, the interaction of DTAB with hemoglobins has been studied using circular dichroism spectropolarimetry analysis. This experiment was utilized to measure the unfolding mechanism and compared alpha-helix secondary structure under different conditions for Hbs. The results reveal that the Acipenser stellatus Hb in comparison with Acipenser persicus Hb has more stability and more structural compactness. Besides, the results confirm the hypothesis that there is a meaningful relation between average habitat depth, partial oxygen pressure, oxygen affinity, structural compactness of Hb, and its stability.