Comparative Effect of Cricket Protein Powder and Soy Protein Isolate on Gel Properties of Indian Mackerel Surimi

Abstract

This work comparatively investigated the effects of different levels (0, 1, 3, and 5%, w/w) of cricket protein powder (CP) and soy protein isolate (SPI) on the gel properties of mackerel surimi. Both SPI and CP enhanced the rheological properties of surimi pastes during heating, as indicated by the increase in G′ and G″ and the decrease in tan δ. With increasing SPI content, the proteolytic inhibition, gel properties, water-holding capacity, and textural profiles of surimi gel were markedly enhanced. Molecular driving-force results showed that SPI markedly promoted the hydrophobic interaction, while disulfide bonds were dominant in CP-added gel. However, the whiteness of surimi gels tended to decrease with the increased levels of both additives, in particular CP. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that SPI hindered the polymerization of myosin heavy chain while CP participated in the formation of non-disulfide covalent bonds with actin. Fourier transform infrared (FTIR) spectra indicated that CP and SPI did not influence the secondary structure of proteins in surimi. Scanning electron microscopy (SEM) demonstrated that CP or SPI induced the myofibrillar protein to form smoother and compact gel network structures. Overall acceptability of the mackerel surimi gel can be improved by the incorporation of 5% SPI while CP had a negative impact on several parameters. However, CP showed the remarkable ability to prevent the lipid oxidation of the gel after storage at 4 °C for 7 days. Overall, both SPI and CP demonstrated positive impacts on the gelling characteristics of mackerel surimi; however, SPI was more advantageous than CP in terms of the gel-strengthening effect and sensory qualities. This study offered a potential use for plant and insect proteins as functional and nutritional ingredients for the production of dark-fleshed fish surimi.

Cryoprotective effect of three oligosaccharides on freezing–thawing induced krill mince: with emphasis on physicochemical changes and gelation properties

“…However, the addition of KC, CGO, COS, and AOS increased the ionic strength and hydrogen bonds, with a significant increase for the KC and CGO groups compared to the control sample ( P < 0.05). During the formation of a gel, favourable or unfavourable electrostatic interactions would occur simultaneously in denatured proteins, thus distinct denatured processes of proteins or peptides may be responsible for the variations in ionic bonding (Somjid et al ., 2022). It was also postulated that the hydroxyl groups of oligosaccharides could interact with water molecules via hydrogen bonds, maintaining the content of hydrogen and ionic bonds on the surface of protein molecules and thereby reducing the mechanical injury to MPs (Zhang et al ., 2021).…”

“…The chemical forces between the proteins in the heat‐induced gel were determined according to the method of Somjid et al . (2022) with modifications. About 2.0 g of gel was chopped and precisely weighed, added with 10 mL 0.05 mol/L NaCl solutions (S 0 ), 0.6 mol/L NaCl (S 1 ), 0.6 mol/L NaCl and 1.5 mol/L carbamide (S 2 ), 0.6 mol/L NaCl and 8 mol/L carbamide (S 3 ), 0.6 mol/L NaCl+8 mol/L carbamide + 0.5 mol/L β‐mercaptoethanol (S 4 ), respectively.…”

Recent advance in modification strategies and applications of soy protein gel properties

“…Somjid et al. (2022) found that the myofibrillar protein with addition of SPI could form smooth and compact gel network structures. Xu, Yu, et al.…”

Study on the interaction and gel properties of pork myofibrillar protein with konjac polysaccharides

“…14 And this filled in the spaces between the proteins, enhancing the protein-water interactions. 27 The addition and filling of konjac polysaccharides might obstruct the combination of hydrophobic sites between protein molecules, which could also lead to retention of water in the three-dimensional network structure, thus altering the water loss. 1,12 It has been found that a higher WHC is related to a gel's compact and homogeneous structure.…”

“…Konjac polysaccharides absorbed the surrounding water and filled in the spaces between the proteins, then promoted crosslinking of molecules during gel formation through proteinpolysaccharide interactions and enhanced the gel-forming ability of the gel. 8,27,30 Konjac polysaccharides further promoted the formation of a consecutive gel matrix and contributed to the formation of a robust and compact gel network, thereby increasing strength and hardness. 8,30 This showed that konjac polysaccharides could provide support to the gel network and confer better integrity to the protein gel network.…”