Biological and functional properties of peptide fractions obtained from collagen hydrolysate derived from mixed by-products of different fish species.

Fish by-products are excellent sources of collagen. Acid-soluble collagen (ASC) derived from a mixed by-product of different fish species was hydrolyzed to obtain peptide fractions and evaluate their biological and functional activities. All fractions obtained (F1: ≥30, F2: 10-30, F3: 5-10, F4: 1-5, and F5: ≤1kDa) exhibited antioxidant activity at concentrations of 5, 10, and 15 mg/mL. However, F5 registered the highest reducing power (absorbance 0.366) and hydroxyl-radical-scavenging activity (91%) at 15 mg/mL; whereas the highest DPPH scavenging activity (81%) was also detected in F5 at 5 mg/mL. The solubility of F1, F2, and F3 was ≥ 95% at pH 7. The highest foaming capacity (78%), foaming stability (60%), and emulsion stability index (42 min) were registered for F1. However, the highest emulsifying activity index (130 m2/g) was for F3. These results place collagen obtained from a mixed by-product of different fish species as a potential biotechnological alternative for the industry.

Partial Characterization of a Low-Molecular-Mass Fraction with Cryoprotectant Activity from Jumbo Squid (Dosidicus gigas) Mantle Muscle.

Freezing conditions affect fish muscle protein functionality due to its denaturation/aggregation. However, jumbo squid (Dosidicus gigas) muscle protein functionality remains stable even after freezing, probably due to the presence of low-molecular-mass compounds (LMMC) as cryoprotectants. Thus, water-soluble LMMC (<1 kDa) fraction obtained from jumbo squid muscle was evaluated by Fourier transform infrared spectrometry. From its spectra, total carbohydrates, free monosaccharides, free amino acids and ammonium chloride were determined. Cryoprotectant capacity and protein cryostability conferred by LMMC were investigated by differential scanning calorimetry. Fraction partial characterization showed that the main components are free amino acids (18.84 mg/g), carbohydrates (67.1 µg/mg) such as monosaccharides (51.1 µg/mg of glucose, fucose and arabinose in total) and ammonium chloride (220.4 µg/mg). Arginine, sarcosine and taurine were the main amino acids in the fraction. LMMC, at the mass fraction present in jumbo squid muscle, lowered the water freezing point to -1.2 °C, inhibiting recrystallization at 0.66 °C. Significant myofibrillar protein stabilization by LMMC was observed after a freeze-thaw cycle compared to control (muscle after extraction of LMMC), proving the effectiveness on jumbo squid protein muscle cryo- stability. Osmolytes in LMMC fraction inhibited protein denaturation/aggregation and ice recrystallization, maintaining the muscle structure stable under freezing conditions. LMMC conferred protein cryostability even at the very low mass fraction in the muscle.

Effect of acid treatment on extraction yield and gel strength of gelatin from whiptail stingray (Dasyatis brevis) skin.

Chemical properties of fish gelatins differ from those of conventional mammalian sources, representing an attractive technological alternative for the food industry. Ray filleting generates a considerable amount of skin waste that can be used as a collagen source for gelatin extraction. Thus, this research evaluated the HCl and CH3COOH effect, at 0.01, 0.025, 0.05, 0.075, 0.1, 0.15, and 0.2 M, on extraction yield, molecular weight distribution, and gel strength (GS) of whiptail stingray (Dasyatis brevis) skin gelatins. Results showed differences (P < 0.05) between acid type and concentration used. CH3COOH (0.15 M) gave the highest extraction yield (7.0% vs. 5.5% at 0.15 M HCl) and GS (653 ± 71 g vs. 619.5 ± 82 g at 0.2 M HCl). Gelatin electrophoretic profile from CH3COOH revealed α-/ß-components and high molecular weight (> 200 kDa) polymers. Ray gelatin GS was higher than commercial bovine gelatin, suggesting its possible use for technological food applications.

Effect of ante-mortem hypoxia on the physicochemical and functional properties of white shrimp (Litopenaeus vannamei) muscle stored on ice.

The effect of ante-mortem hypoxia on the physicochemical and functional properties of raw and cooked white shrimp was studied. Hue angle was greater (p ≤ 0.05) for stressed raw shrimp compared to control (greener color); whereas a lower angle was detected for cooked stressed shrimp (redder/orange coloration). In addition, hue angle increased (p ≤ 0.05) over the ice storage period for control and stressed shrimp (raw and/or cooked). Muscle hardness and shear force showed no differences when comparing control and stressed shrimp (raw and/or cooked). However, during ice storage, shear force increased (p ≤ 0.05) by 22% and 9% for control and stressed raw shrimp, respectively; in contrast, shear force and muscle hardness decreased for cooked shrimp (p ≤ 0.05). Control showed more (p ≤ 0.05) elasticity than stressed cooked shrimp. Stressed raw shrimp showed a water holding capacity 10.8% lower (p ≤ 0.05) than control. However, during the storage, water holding capacity increased (p ≤ 0.05) reaching similar values to control after day 4. Muscle protein solubility of stressed shrimp was 31% lower than control; however, no differences (p > 0.05) were observed after the second day. The thermal stability of myosin (T max) showed differences (p ≤ 0.05) among control and stressed shrimp, whereas no differences for ΔH were observed. Results showed the influence of ante-mortem hypoxia on the physicochemical and functional properties of white shrimp muscle.