Food functionality of protein isolates extracted from Yellowfin Tuna (Thunnus albacares) roe using alkaline solubilization and acid precipitation process

Abstract

Four types of roe protein isolates (RPIs) were prepared through the alkaline solubilization and acid precipitation (ASAP) process, and their functional properties and in vitro bioactivities were evaluated. Higher buffer capacity in pH‐shift range of 8–12 was found in RPI‐1 (pH 11/4.5), required average 94.5 mM NaOH than that of other RPIs to change the pH by 1 unit. All the samples of 1% dispersion (w/v) showed the lowest buffering capacity near the initial pH. The water‐holding capacities (WHC) of RPIs and casein as controls without pH‐shift were in range of 3.7–4.0 g/g protein, and there were no significant differences (p > 0.05). At pH 2 and 8–12 with pH‐shift, WHC and protein solubility of RPIs were significantly improved compared to those of controls. Foaming capacities of RPI‐1 and RPI‐3 were 141.9% and 128.1%, respectively, but those of RPI‐2 and RPI‐4 were not detected. The oil‐in‐water emulsifying activity index of RPI‐1 and RPI‐3 was 10.0 and 8.3 m2/g protein, which was not statistically different from casein (7.0 m2/g), but lower than that of hemoglobin (19.1 m2/g). Overall, RPIs, casein, and hemoglobin exhibited lower food functionality at pH 4–6 near isoelectric points. Through the pH‐shift treatment, the food functionalities of RPIs were improved over the controls, especially in the pH 2 and pH 8–12 ranges. RPI also showed in vitro antioxidant and antihypertensive activities. Therefore, it has been confirmed that RPI extracted from yellowfin tuna roe has high utility as a protein‐ or food‐functional‐enhancing material or protein substitute resource for noodles, confectionery, baking, and surimi‐based products.

Protein Recovery from Underutilised Marine Bioresources for Product Development with Nutraceutical and Pharmaceutical Bioactivities

“…As functional nutrients, proteins extracted from yellowfin tuna roes have commercial applications for the development of paste-based products. These proteins are also suggested candidates for development of protein-fortified and marine-infused products [27]. In this context, protein hydrolysates produced from green mussel was incorporated in gluten-free breads containing buckwheat flour, rice flour, and chickpea flour to enhance product flavour [29].…”

“…Moreover, PHs contain a large amount of arginine, glutamic acid, glycine, and alanine which are responsible for their savoury taste making these protein products more palatable [ 25 , 26 ]. This, combined with their exceptional richness in essential amino acids, particularly methionine and lysine which are lacking in most cereals, corns, and legumes, make them superior to formulated protein products due to enhanced nutritional quality [ 27 , 28 , 29 , 30 ]. Such products also show promise for the treatment of malnutrition and anorexia [ 31 , 32 , 33 ].…”

Functional proteins through green refining of seafood side streams

“…FPHs from blue whiting have been used for beverage fortification ( 163 ). Proteins from yellow fin tuna roes, extracted by the ISP process, can be additive in noodles, confectionery, baking, and surimi-based products ( 164 ). The synergistic interactions of proteins and polysaccharides in their mixed systems could obtain various colloidal structures that can have promising applications in the food industry ( 147 ).…”

Development of patty meat analogue using anchovy protein isolate (Stolephorus insularis) as a binding agent

“…Research on making protein isolates from various types of fish have been developed. Fish protein isolates are produced from Indian mackerel, salmon, cod, herring by-products, ponyfish, sardines, lanternfish, yellowfin tuna roe, tilapia, anchovy, Baltic herring, and catfish [ [11] , [12] , [13] , [14] , [15] , [16] , [17] , [18] ]. The functional protein isolate is added to food products, stabilizing the emulsion, increasing colour brightness, improving texture, increasing protein content, and reducing cooking loss [ 19 ].…”