Hairtail Surimi Research Articles

Characteristics of hairtail surimi gels treated with myofibrillar protein-stabilized Pickering emulsions.

Hairtail (Trichiurus haumela) surimi exhibits poor gelation properties and a dark gray appearance, which hinder its utilization in high-quality surimi gel products. The effect of Pickering emulsions stabilized by myofibrillar proteins (MPE) on the gel properties of hairtail surimi has been unclear. In particular, the impact of MPE under NaCl and KCl treatments on the quality of hairtail surimi gels requires further elucidation. Pickering emulsions stabilized by myofibrillar proteins and treated with NaCl or KCl (Na-MPE, K-MPE) were added to hairtail surimi in amounts of 10-70 g kg-1. The addition of 50 g kg-1 Na-MPE and K-MPE improved the gel strength, textural properties, whiteness, and water-holding capacity (WHC) of hairtail surimi. The relative content of β-turn and β-sheet in the surimi gels increased and the relative content of random coils and α-helix decreased with the addition of oil. The addition of Na-MPE and K-MPE did not affect the secondary structure of surimi gels but stimulated the gelation of hairtail surimi gels. Hairtail surimi containing K-MPE demonstrated similar performance in terms of hardness, microstructure, and WHC compared with the addition of Na-MPE. The quality of hairtail surimi gels can be improved by the addition of Na-MPE or K-MPE. The K-MPE proved to be an effective option for enhancing the properties of hairtail surimi gels at 50 g kg-1 to replace Na-MPE. © 2024 Society of Chemical Industry.

Determination of Optimum Processing Condition of High Protein Laver Chip Using Air-Frying and Reaction Flavor Technologies.

This study aimed to develop a high-protein and gluten-free laver chip using air-frying and reaction flavor technologies via response surface methodology (RSM). The optimum processing condition (w/w) was determined with a batter composition of 20% dried laver, 21.3% hair tail surimi, and 58.7% rice flour. Additional ingredients included б-gluconolactone, NaHCO3, soybean oil, corn syrup, table salt, saccharin, and a mixture of distilled water and reaction flavor-inducing solution (RFIS). The laver pellet processed and dried (50 °C, 1-2 h) with air-frying (195 °C, 52.5 s) to process the laver chip. The values of brittleness and puffing ratio of the laver chip were 6.93 ± 0.33 N and 116.19 ± 0.48%, respectively, with an error within 10% of the predicted values of RSM. RFIS was prepared via RSM with the addition of precursor substances (w/v) of methionine 0.54%, threonine 3.30%, glycine 2.40%, glutamic acid 0.90%, and glucose 3% to distilled water and then heating reaction (121 °C, 90 min). The quantitatively descriptive analysis (QDA) of RFIS, baked potato-like and savory odor were 6.00 ± 0.78 and 4.00 ± 0.91, respectively, with an error within 10% of the predicted values. The laver chip exhibited high-protein (24.26 ± 0.10 g%) and low-calorie (371.56 kcal) contents.

Physiochemical Quality, Microbial Diversity, and Volatile Components of Monascus-Fermented Hairtail Surimi.

In order to study the effects and mechanism of Monascus on the quality of hairtail surimi, high-throughput sequencing technology, headspace solid-phase microextraction-gas chromatography-mass spectrometry (HS-SPME-GC/MS), and electronic nose techniques were used to investigate the changes in the quality, microbial diversity, and volatile flavor compounds of Monascus-fermented hairtail surimi (MFHS) during fermentation. The results showed that the total volatile basic nitrogen (TVB-N) index of hairtail surimi fermented by Monascus for 0-5 h met the requirements of the national standard. Among them, the 1 h group showed the best gel quality, which detected a total of 138 volatile substances, including 20 alcohols, 7 aldehydes, 12 olefins, 4 phenols, 12 alkanes, 8 ketones, 15 esters, 6 acids, 16 benzenes, 4 ethers, and 8 amines, as well as 26 other compounds. In addition, the dominant fungal microorganisms in the fermentation process of MFHS were identified, and a Spearman correlation analysis showed that 16 fungal microorganisms were significantly correlated with the decrease in fishy odor substances in the fermented fish and that 8 fungal microorganisms were significantly correlated with the increase in aromatic substances after fermentation. In short, Monascus fermentation can eliminate and reduce the fishy odor substances in hairtail fish, increase and improve the aromatic flavor, and improve the quality of hairtail surimi gel. These findings are helpful for revealing the mechanism of the quality formation of fermented surimi and provide guidance for the screening of starter culture in the future.

Enhancement of surimi gel properties through the synergetic effect of fucoidan and oligochitosan

For the first time, two common marine-derived dietary fibres (MDFs), fucoidan (FU) and oligochitosan (OCS), were introduced as textural and nutritional enhancers in hairtail surimi gels. The MDFs could assist with inhabiting the endogenous proteolytic enzyme activity, unfolding the myosin to expose more reactive domains, inducing favorable protein conformational transition, and thus, promoting gelation. The highly hydrophilic MDFs rich in –OH groups can bind water molecules via strong hydrogen bonds, facilitating water redistribution within the gel network. Driven by the enhanced chemical forces, a stable protein-FU-OCS gel is obtained, which improves the hardness by almost 100% and the water holding capacity from 86.25% to 92.25%. Collectively, this study demonstrates that MDFs are a group of effective additives to improve gel characteristics and nutritional profiles of surimi-based seafood products. The proposed MDF-protein interaction model would guide the application of MDFs as novel additives in the food industry.

Effects of chickpea and peanut protein isolates on the gelling properties of hairtail (Trichiurus haumela) myosin

In order to improve the gel quality of hairtail surimi and clarify the formation mechanism of plant protein-myosin complex gel, the effects of different amounts of chickpea protein isolate (CPI) and peanut protein isolate (PPI) on rheological behavior, gel properties, second structures and molecular driving forces of hairtail (Trichiurus haumela) myosin gel were investigated. The results showed that CPI intensified the gel strength, textural properties, storage modulus, water-holding capacity, and reticular flexibility of the myosin gel markedly (P < 0.05) as its concentration increased from 1% to 8%. In contrast, as PPI concentration increased, the breaking force, immobilized water and elastic characteristics exhibited increased first and then decreased, while whiteness values elevated (P < 0.05). The optimum PPI concentration was 2%. CPI and PPI enhanced the hydrophobic interactions between protein molecules, which could accelerate the formation of gel network structure during heating. The microstructures revealed that CPI and PPI triggered a denser gel structure at a suitable concentration. In conclusion, CPI and PPI have positive effects on the formation of hairtail myosin gels, while CPI exhibited a higher gel strengthening effect than PPI. This study provided a potential application of plant proteins for surimi or minced meat processing.

Effect of Extracts Derived from Brown Algae (Sargassum horneri) on the Gel Property and Moisture Distribution of Hairtail Surimi Gel (Trichiurus haumela).

The cross-linking degree between myosin affected the surimi gel properties in the hairtail. In this study, the effects of phlorotannin extracts (PE) derived from brown algae (Sargassum horneri) with different concentrations (0.05%, 0.3%, 1% w/w) on the hairtail surimi gel-forming properties were investigated in comparison with the commercial phloroglucinol (PG). The breaking forces of surimi gel with 1% PE and 0.05% PG were increased by 14.80% and 2.73%, respectively. The increase in deformation was 9.66% with 1% PE compared with the control added with water, but there was no increase in deformation of surimi gel with 0.05% PG. The improved surimi gel structure with PE as a bridge for the three-dimensional network forming of protein was observed in the microstructure. Moreover, PE could significantly shorten the water relaxation time (p < 0.05), reduce free water content (p < 0.05), and increase the hydrogen proton density of the hairtail surimi according to the results of NMR, dielectric properties, and MRI map, respectively. Our findings suggest that the extracts from the brown algae could be a potential economical gel structure enhancer to improve the myosin network.

Purification and characterization of antioxidant peptides from hairtail surimi hydrolysates and their effects on beef color stability.

The antioxidant peptides extracted from plants or animals have shown great potential in preventing food quality deterioration caused by oxidization. Here, peptide fractions obtained from hairtail surimi hydrolysates (HSH) were investigated for structure and color-protective effect. The results showed the<3kDa fraction obtained from HSH by ultrafiltration could be separated into five major fractions (A-E) by gel chromatography, among which fraction A possessed the highest antioxidant activities. This fraction A could be further separated into two fractions (A1 and A2 ) by the reversed-phase high-performance liquid chromatography, and fraction A2 with lower α-helix content exhibited the higher antioxidant activities. The amino acids sequence of fraction A2 was identified as DLYANTVLSGGTTMYPGIADR (2214.0627Da). The synthetic peptide with this sequence was also found to exhibit obvious antioxidant activity. Moreover, both HSH, fractions A1 and A2 , and synthetic peptide demonstrated color-protective effects during the beef preservation. Taken together, the results obtained showed that the natural antioxidant peptides could be isolated from HSH, which can be used in meat preservation for inhibiting color deterioration. PRACTICAL APPLICATION: This study demonstrated the potential of hairtail surimi hydrolysates (HSH) as a source of antioxidant peptides. Furthermore, these antioxidant peptides purified from HSH exhibited the potential for prevention of beef color deterioration of beef, providing a potential application for meat preservation. Particularly, using the antioxidant peptides sourced from fish surimi for meat preservation may not only ease the safety concerns about artificial preservatives but also create a unique selling proposition, especially in far eastern Asian countries, since consumers in these countries believe "umami" is the combination of "fish" and "meat."

Preparation of antioxidant peptides from hairtail surimi using hydrolysis and evaluation of its antioxidant stability

In this study, antioxidant peptides were prepared from hairtail surimi by hydrolysis. Response surface methodology coupled with a Box-Behnken design was applied to optimize hydrolysis conditions. The optimum conditions were determined as: 12.1 h incubation time, 44.74 °C incubation temperature and enzyme concentration 1858.85 U/g. The amino acid compositions analysis showed most abundant amino acid in hairtail surimi antioxidant peptides (HAP) was Glutamic acid followed by Aspartic acid and Lysine. In addition, the fraction of HAP with a molecular weight less than 3 kDa showed the strongest antioxidant activity among the 4 fractions obtained by ultrafiltration. Furthermore, HAP showed good stability in mild acidic, alkaline, or salt solutions, in in vitro digestive juice, and upon heating. In conclusion, hairtail surimi might be a good source to produce antioxidant peptides, which can be used as a natural antioxidant in food industry.

Chemical interactions and rheological properties of hairtail (Trichiurus haumela) surimi: Effects of chopping and pressure

Hairtail surimi was treated with high hydrostatic pressure (HHP) and heating, and the gel network structure, gel strength and water holding capacity were studied. The best gel properties were observed with HHP at 350 MPa for 8 min (350/8), and HHP after chopping was beneficial to the formation of the gel network. Changes in hydrophobic interactions may be an important factor leading to different gel properties with different processing sequences. The suwari treatment of the 350/8 decreased the thermal stability and elastic modulus of suwari gels, but increased the ability of the surimi gel system to bind water molecules.

Combined Use of Rheology, LF-NMR, and MRI for Characterizing the Gel Properties of Hairtail Surimi with Potato Starch

The effects of potato starch (4%, 8%, 12%, 16%, and 20%) on the gel properties of hairtail surimi were investigated by rheology, low-field nuclear magnetic resonance (LF-NMR), and magnetic resonance imaging (MRI). The results indicated that the addition of potato starch markedly improved the gel properties, including the maximum texture profiles, gel strength, and water holding capacity. The addition of potato starch significantly increased both the storage modulus and loss modulus after the formation of gel rather than changed the type of two curves. Furthermore, there was a positive correlation between heat-induced gel properties and rheological properties in the surimi-starch system. The LF-NMR results indicated that the addition of potato starch had a positive effect toward the shortening of T2 spin-spin relaxation time of gel and water exchange from free water to bound water. Additionally, more uniform water distribution in surimi gel contained potato starch was observed from the result of MRI. The overall results suggested that interactions of starch-protein promoted the most favorable properties of hairtail surimi at the addition of 16% potato starch.

Myofibrillar Protein Structure and Gel Properties of Trichiurus Haumela Surimi Subjected to High Pressure or High Pressure Synergistic Heat

The changes in gel properties and myofibrillar protein structure of Trichiurus haumela surimi subjected to high pressure (300–450 MPa; 5 min) or high pressure synergistic heat (90 °C; 30 min) treatment were investigated. The results showed that high pressure below 400 MPa could improve the gel properties. The water holding capacity of the 350 MPa group increased by 27.40% compared with the control group. Moreover, the gel strength of surimi gel induced by high pressure of 300 MPa and 350 MPa increased by 38.08% and 40.00%, respectively, and continually increased by 17.86% and 21.00% after further heating. Both of high pressure and heating affected the composition of myofibrillar protein and partially degraded the actin and myosin heavy chain. High pressure reduced the contents of α-helix and β-turn, but increased β-sheet and random coil in the myofibrillar protein. Subsequent heat treatment converted the partial β-sheet into the α-helix structure. In addition, in the gels of surimi subjected to high pressure, the secondary structure of myofibrillar protein was significantly correlated with the whiteness, gel strength, and texture characteristics of the gels. Collectively, the results supported an optimum pressure of 300–350 MPa for the induction of hairtail surimi gel.

Changes of water state and gel characteristics of Hairtail (Trichiurus lepturus) surimi during thermal processing.

This study examined the changes of water state and gel characteristics of Hairtail surimi during thermal processing including two steps. The results showed that there were four content of water in Hairtail surimi gels. Water-holding capacity (WHC) and T23 relaxation time of water and gel strength increased from 47.01 to 78.97% and from 64.23 to 51.52 ms, respectively, and whiteness decreased from 63.87 to 55.22 during the entire thermal processing. Meanwhile, the texture properties including hardness, gumminess, and chewiness declined from 402.42 to 130.41 g, from 294.39 to103.70 g, and from 233.68 to 43.60 g, respectively, during the first step, and then increased markedly during the second step from 130.41 to 2,301.87 g, from 103.70 to 1,250.99 g, and from 43.60 to 978.51 g, respectively. Furthermore, the WHC and textural profile had positive correlation, and changes in protein secondary structure were interesting, with the α-helices decreasing significantly from 26.40 to 14.12%, while the β-sheet and the random coil structure increasing significantly from 36.28 to 44.03%, and from 10.89 to 14.31%, respectively, and β-turn structure increasing form 26.44 to 27.98% during the first step and then declining markedly during the second step, moreover β-sheet had a fine positive correlation with WHC hardness and chewiness. Overall, dense, porous and compact three-dimensional network gel structure gradually formed. In a word, during thermal processing. WHC of Hairtail surimi increased, and protein secondary structure of protein became orderly, and a fine, dense gel formed during thermal processing. Water is considered as the highest and most important chemical constituent in surimi products. During surimi gelation, water molecules exist as bulk water and motionally restricted water on the protein surface. In order to gain more insights into the surimi heating-induced gelation processing, and improve the surimi gel properties, and give same advice to manufacturing enterprise, this work was conducted to study the structural changes of protein and water state during surimi gelation processing and performed along with the monitoring of the texture, WHC and other physical characteristics of surimi gel, as well as the microstructure of surimi gel.

Enzymatic Hydrolysis of Hairtail Surimi in an Ultra-High Pressure Bioreactor

Amino acids have been extracted from Hairtail surimi using enzymes in an ultra-high pressure bioreactor. The extraction efficiency of different enzymes including papain, trypsin, and proteases (acid, neutral, alkaline) also has been evaluated, and it has been discovered that neutral protease behaved the best. The amino acids were analyzed using automatic amino acid analyzer, and the enzymatic digestion conditions were optimized. For neutral protease, the optimal condition was 50℃, 250 MPa, pH 7.0. Material to liquid ratio of enzyme is 6%. More than 29 amino acids were detected after 24 hours of hydrolysis; the enzymatic hydrolysis rate can reach 83.29%. The results show that enzymatic digestion under ultra-high-pressure provides a very promising approach to extract amino acids from Hairtail surimi.

γ-PGA and MTGase improve the formation of ε-(γ-glutamyl) lysine cross-links within hairtail (Trichiurus haumela) surimi protein

The present study investigated the mechanism of ε-(γ-glutamyl) lysine cross-links within hairtail (Trichiurus haumela) surimi protein via γ-polyglutamic acid (γ-PGA) and MTGase. The results indicated that the addition of MTGase and γ-PGA markedly improved the gelation properties of hairtail surimi protein, including its maximum breaking force and deformation, water holding capacity and gel strength. The maximum improvements were achieved by adding 0.5units MTGase/g meat paste in combination with 0.06% γ-PGA. SDS-PAGE showed that the band intensity of cross-linked proteins increased, whereas that of myosin heavy chain decreased after treatments. Further scanning electron microscopy (SEM) analysis showed the formation of a denser gel matrix, which was caused by much stronger and more inter- and intra-molecular cross-linking of proteins, via MTGase catalysing ε-(γ-glutamyl) lysine cross-links formed between lysine residues in the gel protein and glutamic residues in the hydrolytic γ-PGA. The results provide reliable guidance for the improvement of hairtail surimi protein gelation properties.

Antioxidant Activity of Enzymatic Hydrolysate Derived From Hairtail Surimi Wash Water Using an Immobilized Chymotrypsin-Trypsin Column Reactor

In this study, a column reactor filled with immobilized chymotrypsin–trypsin (I-CT) was used to prepare antioxidant peptides from hairtail surimi wash water. At the optimum reaction temperature (30C), when residence time is 5 min (flow rate is 3 mL/min), the conversion rate of the I-CT column enzymatic reactor could be maintained above 60%. The half-life of the column reactor was in excess of 6 h. At 30C, when residence time is 15 min (flow rate is 1 mL/min), the antioxidant capacity of the resulting enzymatic hydrolysate was the highest (1.59 mmol/L FeSO4 equivalent) and the product conversion rate was 67.0%. Tricine–sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis showed that the main ingredients of enzymatic hydrolysate were low-molecular-weight peptides (<4 kDa). Practical Applications In order to fully utilized protein resources, it is necessary to develop an effective approach to recover protein in the surimi wash water. To this end, a practical method by using a column reactor filled with immobilized chymotrypsin–trypsin developed in our laboratory was established. The hydrolysates obtained by this method may be used as ingredients of functional foods due to their antioxidant activity.

Effect of electron irradiation and heat on the structure of hairtail surimi

Abstract Hairtail surimi was treated with electron radiation and heat, the chemical interactions, thermal properties and the structural changes were determined. The chemical interaction data indicate that the contribution of disulfide bonds to heat-induced gel formation was decisive. Irradiation promoted the formation of disulfide bonds during the cooking. Differential scanning calorimetry showed that the myosin and actin thermal transitions of irradiated surimi shifted to lower temperatures. And the myosin thermal stability of irradiated surimi was lower than unirradiated surimi. The Fourier transform infrared and Raman results showed the irradiation and heat treatments decreased the α-helix structure content and increased β-sheet structure content. This study may provide useful information for the effect of irradiation on the surimi gel properties.

Rapid discrimination of three marine fish surimi by Tri-step infrared spectroscopy combined with Principle Component Regression

A Tri-step infrared spectroscopy (Fourier transform infrared spectroscopy (FT-IR) integrated with second derivative infrared (SD-IR) spectroscopy and two-dimensional correlation infrared spectroscopy (2DCOS-IR)) combined with Principal Component Regression (PCR) were employed to characterize and discriminate three marine fish surimi (white croaker surimi (WCS), hairtail surimi (HS) and red coat surimi (RCS)). The three surimi had similar IR macro-fingerprints (similarity>0.7) especially for the absorption bands of amide groups. Compared to the other two surimi, however, RCS had a middle strong characteristic peak of lipids at 1745cm−1, indicating that RCS had the highest content of lipids. SD-IR spectra of the three surimi enhanced the spectral resolution and amplified the small differences, especially at about 1682cm−1, 1679cm−1, 1656cm−1 and 1631cm−1, suggesting that the three had different profiles of proteins. Moreover, evident differences were observed in 2DCOS-IR spectra of 1500–1800cm−1. WCS had one strong (1620cm−1) and three weak auto-peaks (1520cm−1, 1552cm−1, 1706cm−1). HS had three strong (1621cm−1, 1648cm−1, 1708cm−1) and two weak auto-peaks (1523cm−1, 1553cm−1), whereas RCS had one strong (1623cm−1) and three weak auto-peaks (1525cm−1, 1709cm−1, 1738cm−1). Furthermore, sixty batches of surimi (twenty for each surimi) were objectively classified by PCR. It was demonstrated that the Tri-step infrared spectroscopy combined with PCR could be applicable for discrimination of precious marine fish surimi in a direct, rapid and holistic manner.

Improving gel properties of hairtail surimi by electron irradiation

Abstract Hairtail surimi was subjected to electron irradiation for doses up to 9 kGy. At 7 kGy highest gel strength was achieved. The irradiation also increased lightness and expressible water amount. Scanning electron micrographs showed that 7 kGy irradiation made the surimi protein gel network more compact. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed the degradation of myosin heavy chain (MHC) as the irradiation dose increased, particularly at the 7 and 9 kGy doses. Radiation processing may become a new effective tool in surimi production.

Twin-Screw Extrusion of Hairtail Surimi and Soy Protein Isolate Blends

In this study, hairtail surimi (HS) and soy protein isolate (SPI) blends were extruded using a co-rotating twin-screw extruder. The effects of feed moisture, screw speed, and barrel temperature on the texture and water-holding capacity of the extrudates were investigated using response surface methodology. HS and SPI were mixed at a ratio of 1:4; the screw speed was tested at three levels between 80 and 120 rpm; the barrel temperature was set between 140°C and 160°C, and the feed moisture was set between 30% and 50%. The digestibility and microstructure of the extrudate produced by optimum condutions were also studied. The results demonstrated that the physical properties were significantly (p < 0.05) affected by the three process variables. Water-holding capacity and extrudate texture were found to mainly depend on barrel temperature and feed moisture, respectively. In vitro protein digestibility of the blends was improved by the extruding process.

Improvement of Hairtail Surimi Gel Properties by NADPH‐Sulfite Reductase, Recombinant Cystatin, and Microbial Transglutaminase

ABSTRACT: Effects of nicotinamide dinucleotide phosphate (NADPH)‐sulfite reductase, recombinant cystatin, and microbial transglutaminase (MTGase) or their combination on hairtail surimi quality were investigated. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) showed that adding NADPH‐sulfite reductase could effectively recover native myosin. Apparent cross‐linking of hairtail myosin during the setting process was observed with added MTGase, while myosin degradation on the heating process was substantially retarded with recombinant chicken cystatin. The combined use of NADPH‐sulfite reductase, recombinant chicken cystatin, and MTGase exhibited a greater effect on improving hairtail surimi quality.