Saurida Wanieso Research Articles

Comparative ontogeny and phylogenetic relationships of eight lizardfish species (Synodontidae) from the Northwest Pacific, with a focus on Trachinocephalus monophyly.

Lizardfish (Aulopiforms: Synodontidae), distributed broadly in temperate to tropical waters, are represented globally by 83 species across four genera, with 10 species in Korea. Despite these numbers, few studies have been conducted on the early life history of lizardfishes compared to their adult counterparts. Thus, we conducted molecular identification of 123 Synodontidae larvae collected from the Northwest Pacific (Korea Strait, Yellow Sea, East China Sea, and East Sea) between June 2017 and July 2021, using mitochondrial DNA COI and 16S rRNA sequences. Significant morphological differences were observed in the larvae and juvenile, including variation in melanophore, count, morphometric characteristics, and body shape. The morphological traits of eight species (Harpadon nehereus, Saurida macrolepis, Saurida wanieso, Saurida sp., Synodus hoshinonis, Synodus kaianus, Synodus macrops, and Trachinocephalus trachinus) served as vital data for interpreting the phylogenetic relationships within the Northwest Pacific Synodontidae. Ultimately, the identification key revealed by this study will enable accurate identification of Synodontid larvae and juveniles, and further facilitate our understanding of the phylogenetic relationships within this family.

Characterization of the antioxidant and angiotensin I-converting enzyme inhibitory activities of lizardfish Saurida wanieso viscera sauce and their correlation with the amino acid profiles

Characterization of the antioxidant and angiotensin I-converting enzyme inhibitory activities of lizardfish Saurida wanieso viscera sauce and their correlation with the amino acid profiles

Comparison of non-volatile taste-active components in fish sauce produced from lizardfish Saurida wanieso viscera under different conditions

Lizardfish is a major ingredient for the manufacture of surimi in Japan, and its viscera are considered a novel source of protease to enhance protein autolysis. We investigated the non-volatile taste components of fish sauce produced from the lizardfish Saurida wanieso viscera in order to clarify the effects of fermentation conditions on the quality of fish sauce. Samples were fermented for 40 days under three sets of conditions: group 1, pH 7.0 and 60 °C; group 2, pH 11.0 and 40 °C; and group 3, uncontrolled pH and ambient temperature. Group 2 showed the highest concentration of umami amino acids (1,195.29 mg/100 ml) and sweet amino acids (2,033.60 mg/100 ml). High levels of lactic acid (1,219.65 mg/100 ml), acetic acid (367.08 mg/100 ml), and pyroglutamic acid (261.66 mg/100 ml) were also found in group 2. In addition, investigation of nucleic acid-related compounds revealed differences in the degree of nucleotide hydrolysis among the three groups during fermentation. Sensory evaluation showed that group 2 had the highest umami and the lowest bitterness, indicating that this group had the most preferable taste. These results reveal that fermentation under conditions optimal for endogenous proteases is beneficial for producing a product with optimal taste qualities.

The effect of mung bean tripsin inhibitor on himodori kamaboko prepared from lizardfish (Saurida wanieso)

The effect of mung bean tripsin inhibitor on himodori kamaboko prepared from lizardfish (<i>Saurida wanieso</i>)

The complete mitochondrial genome of Wanieso lizardfish Saurida wanieso Shindo & Yamada, 1972 (Aulopiformes: Synodontidae)

The complete mitochondrial genome of the Wanieso lizardfish (Saurida wanieso) was determined by using a PCR-based method. The total length of mitochondrial DNA is 16,552 base pairs including 13 protein-coding genes, 2 ribosomal RNA, 22 transfer RNA genes, 1 replication origin region and 1 control region as other Saurida spp. and bony fish. Base composition of the genome is A (25.7%), T (25.2%), C (31.5%), and G (17.6%) with an A + T-rich hallmark as that of other vertebrate mitochondrial genomes.

Effect of Proteolytic Squid Protein Hydrolysate on Textural Quality and Denaturation of Wanieso Lizardfish (Saurida wanieso) Surimi during Frozen Storage

Effect of Proteolytic Squid Protein Hydrolysate on Textural Quality and Denaturation of Wanieso Lizardfish (Saurida wanieso) Surimi during Frozen Storage

Effect of Shrimp Chitin and Shrimp Chitin Hydrolysate on the State of Water and Dehydration-induced Denaturation of Lizard Fish Myofibrillar Protein

To assess the potential utilization of shrimp waste, shrimp chitin (SC) and shrimp chitin hydrolysate (SCH) were prepared from black tiger (Penaeus monodon), endeavour (Metapenaeus endeavouri) and giant freshwater (Macrobrachium rosenbergii) prawns. Effect of SC and SCH on the state of water and denaturation of lizard fish (Saurida wanieso) myofibrillar protein (Mf) at concentrations of 5% (dry weight/wet weight) were assessed based on water activity (Aw) and changes in Mf Ca-ATPase activity during dehydration. The effect was compared with untreated Mf (control) and Mf containing glucose. The Aw of Mf for each SCH was remarkably lower than the Mf with SC and control. The Mf with SCH showed a remarkably high level of inactivated Ca-ATPase activity, followed by Mf with SC and the control. Mf with glucose showed slightly higher inactivated Ca-ATPase activity than SCH, reaching Aw levels of 0.65, before rapidly decreasing. These findings revealed that SCH contributed to the retardation effect on dehydration-induced denaturation of Mf by stabilizing hydrated water molecules surrounding the Mf.

Effect of proteolytic squid protein hydrolysate on the state of water and denaturation of lizardfish ( Saurida wanieso) myofibrillar protein during freezing

The concentration dependent (2.5–10% of dry weight/wet weight) protective effect of squid protein hydrolysate (SPH), extracted from Japanese flying squid and swordtip squid by protease treatment, on the state of water and denaturation of frozen lizardfish ( Saurida wanieso) myofibrillar protein (Mf) were assessed on the basis of the amount of unfrozen water in Mf by differential scanning calorimetry and Mf Ca-ATPase inactivation during freezing at −25 °C for 90 days; the effects were compared with those of sodium glutamate. The Mf showed a higher amount of unfrozen water upon addition of SPH, regardless of level of addition and species differences, resulting in a markedly decreased inactivation of Mf Ca-ATPase throughout the freezing period. The Ca-ATPase activity in the Mf without SPH (control) dropped drastically from the beginning of the freezing. These findings suggest that the functional side chains of the peptides of SPH produce bound water in the Mf structure, which provides a structural alteration of the hydrate water that has a capacity to suppress the freeze-induced denaturation of Mf. An addition of 5.0–7.5% concentration of SPH is found to be suitable to increase the amount of unfrozen water and to prevent the freeze-induced denaturation of Mf.

Concentration Dependent Effect of Enzymatic Fish Protein Hydrolysate on the State of Water and Denaturation of Lizard Fish (Saurida wanieso) Myofibrils during Dehydration

To utilize fishery waste products as functional food material, the fish protein hydrolysate (FPH) was prepared from fish scraps of three marine species by protease treatment. The added-concentration dependent effects of FPH (2.5-12.5%, dry weight/wet weight) on the state of water and denaturation of lizard fish myofibrils were evaluated by desorption isotherm curves, myofibrillar Ca-ATPase activity, and unfrozen water which was determined by differential scanning calorimetry during dehydration. The water activity (Aw) in myofibrils was distinctly decreased with the increasing concentration of FPH from 2.5% up to 10.0%, although the Aw added with 12.5% of FPH was almost equal to that with 10.0% of FPH. The amount of unfrozen water in myofibrils during dehydration was increased by the addition of FPH, and the greatest increase was found at 5.0-10.0%. The FPH suppressed the inactivation of myofibrillar Ca-ATPase activity during dehydration, and a larger effect of suppression was observed at 7.5% addition of FPH. These findings suggest that peptides produced in FPH functioned to stabilize the hydrate water surrounding the myofibrils and suppressed their dehydration-induced denaturation.

Purification and characterization of myofibril-bound serine protease from lizard fish ( Saurida undosquamis) muscle

Myofibril-bound serine protease (MBSP) from lizard fish ( Saurida undosquamis: Synodontidae) skeletal muscle was purified to homogeneity with higher purification (1260-fold) and higher recovery (7%) than our previous report in lizard fish ( Saurida wanieso). The new purification method combines a heat-treatment for dissociation from washed myofibrils, acid-treatment at pH 5.0 before and after lyophilization, and alcohol-treatment, followed by two column chromatographies. The molecular mass of the enzyme was estimated to be 50 kDa under non-reducing conditions and 28 kDa under reducing conditions by SDS-PAGE. The N-terminal amino acid sequence of the MBSP was determined to be 22 residues (IVGGYEXEAYSKPYQVSINLGY) and the sequence showed high homology to carp and other fish trypsins (64–77%), but did not show high homology to carp MBSP (41%). The enzyme activity was inhibited by serine protease inhibitors such as Pefabloc SC, leupeptin, TLCK and native protein inhibitors (soybean trypsin inhibitor, α 1-antitrypsin and aprotinin). The purified enzyme specifically hydrolyzed at the carboxyl side of the arginine residue of synthetic 4-methyl-coumaryl-7-amide substrate. When purified MBSP was stored at −35 °C in the presence of 50% ethylene glycol (V/V), the enzyme activity was entirely preserved over 6 months and stable against freezing and thawing. Activities for both casein and the synthetic substrate were most active at pH 9.0, and the enzyme was most active approximately 55 °C with casein and between 35 and 45 °C for synthetic substrate. When myofibrils were incubated with purified MBSP, myosin heavy chain was mostly degraded approximately 55 °C, but the degradation of actin was very slow.

Effect of Enzymatic Fish Protein Hydrolysate from Fish Scrap on the State of Water and Denaturation of Lizard Fish (Saurida wanieso) Myofibrils during Dehydration

Fish protein hydrolysate (FPH) was prepared from scraps of 5 marine species, in order to utilize by-products effectively by protease treatment. Protein was the major component of the FPH ranging 82–86%. The effects of 5% FPH (dried weight/wet weight) on the state of water and the denaturation of lizard fish Saurida wanieso myofibrils were evaluated by desorption isotherm curves, Ca-ATPase activity, and differential scanning calorimetry (DSC) during dehydration. The myofibrils with FPH showed a decreased water activity (Aw), while they exhibited significantly higher Ca-ATPase activity compared to myofibrils without FPH (control). The myofibrils with FPH had higher amount of unfrozen water than the control. These results suggest that the FPH suppressed dehydration-induced denaturation, which seems to be attributable to the stabilization of the hydrated water surrounding the myofibrils.

Effect of Squid Protein Hydrolysate on Freeze-Induced Denaturation of Lizardfish (Saurida wanieso) Myofibrillar Protein

In order to utilize low-cost squid effectively as a functional material for food processing and preservation, squid protein hydrolysate (SPH) was prepared from 4 species of squid by protease treatment. Peptides are the major components (84–88%) of SPH. The protective effect of 5% SPH (dry weight/wet weight) on the freeze-induced denaturation of lizardfish Saurida wanieso myofibrillar protein (Mf) was evaluated on the basis of Mf Ca-ATPase activity and the amount of unfrozen water in Mf, which was determined by differential scanning calorimetry (DSC); the effect was compared with that of sodium glutamate. Mf with SPH showed markedly higher Ca-ATPase activity than did Mf without SPH (control) during frozen storage. Mf with SPH had a higher amount of unfrozen water than the control. These findings suggest that SPH stabilized water molecules in the hydration sphere of Mf and thus, suppressed freeze-induced denaturation of Mf. The effect by SPH was less than that by sodium glutamate.

Purification of a novel myofibril-bound serine proteinase inhibitor (MBSPI) from the skeletal muscle of lizard fish

A novel myofibril-bound serine proteinase inhibitor (MBSPI) was purified to homogeneity from the skeletal muscle of lizard fish ( Saurida wanieso). Purification was carried out by ammonium sulfate fractionation, followed by column chromatographies on DEAE-Sephacel, SP-Sepharose and Sephadex G-150. MBSPI was purified 7.7-fold starting from the DEAE-Sephacel fraction, with a yield of 0.2%. It is a monomeric protein with the molecular mass of 50 kDa as estimated by SDS-PAGE and gel filtration. MBSPI reveals high inhibition specificity toward a myofibril-bound serine proteinase (MBSP) purified from lizard fish muscle. No inhibition is detected toward bovine trypsin, bovine chymotrypsin, two trypsins from carp hepatopancreas and a serine proteinase isolated from the sarcoplasmic fraction of white croaker muscle. It does not exert any inhibitory activity toward a myofibril-bound serine proteinase from carp muscle.

Purification of a Novel Serine Proteinase Inhibitor from the Skeletal Muscle of White Croaker (Argyrosomus argentatus)

A novel serine proteinase inhibitor has been purified to homogeneity from the skeletal muscle of white croaker (Argyrosomus argentatus). The purification was carried out by ammonium sulfate fractionation, DEAE-Sephacel, heating treatment followed by column chromatographies on SP-Sepharose, Sephadex G-150 and gel-filtration high performance liquid chromatography. The molecular mass of the inhibitor was 55 kDa as estimated by SDS–PAGE and gel filtration. It specifically inhibited a myofibril-bound serine proteinase (MBSP) isolated from the skeletal muscle of lizard fish (Saurida wanieso). No inhibition, however, was detected toward other serine proteinases such as bovine trypsin, bovine chymotrypsin and a myofibril-bound serine proteinase from carp (Cyprinus carpio) muscle. Interestingly, the sequences of tryptic digested peptide fragments of MBSPI revealed high identity to that of porcine phosphoglucose isomerase (PGI) (76%) and other PGIs. Furthermore, purified MBSPI exhibits PGI activity, suggesting the inhibitor is a protein closely related to PGI. When rabbit muscle PGI was investigated, it also specifically suppressed the activity of MBSP. It thus strongly suggests that MBSPI is actually PGI and conversely, PGI is a specific inhibitor toward myofibril-bound serine proteinase(s).

Identification of a myofibril-bound serine proteinase (MBSP) in the skeletal muscle of lizard fish Saurida wanieso which specifically cleaves the arginine site

A myofibril-bound serine proteinase (MBSP) from the skeletal muscle of lizard fish ( Saurida wanieso) was purified to homogeneity by a heating treatment followed by a series of column chromatographies on DEAE-Sephacel, Sephacryl S-200, Q-Sepharose, Hydroxyapatite and Benzamidine-Sepharose 6B, and characterized enzymatically. On SDS-polyacrylamide gel electrophoresis (SDS-PAGE), the purified enzyme showed a band with molecular mass of ≈29 kDa under reducing conditions, while 60 kDa under non-reducing conditions. The optimum temperature of the enzyme was 50°C using t-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide (Boc-Phe-Ser-Arg-MCA) as a substrate. Substrate specificity analysis both using MCA-substrates and peptides showed that MBSP specifically cleaved at the carboxyl side of the arginine residue. Inhibitor susceptibility analysis revealed that MBSP was inhibited effectively by Pefabloc SC, soybean trypsin inhibitor (STI) and aprotinin, indicating the characteristic of a serine proteinase. When myofibril was incubated with the enzyme, it optically degraded myosin heavy chain at 55–60°C, while α-actinin and actin were not at all hydrolyzed as detected by immunoblotting. The N-terminal amino acid sequence of MBSP was partially determined as IVGGAEXVPY- and was very homologous to other serine proteases.

The Gel-Forming Characteristics of Lizardfish.

The gel-forming characteristics of unwashed and washed meat from three lizardfish species (maeso Saurida undosquamis, wanieso Saurida wanieso, and tokageeso Saurida elongata) were investigated at various heating temperatures from 30 to 80°C for 20 minutes and 2hours. Judging from evaluation of gel strength by tensiometer and a folding test accompanied by degradation of myosin heavy chain (MHC) by SDS-PAGE analysis, the gel degradation of unwashed meat gels occurred at 40, 60, and 70°C in tokageeso, while it occurred at 60 and 70°C in maeso and at 60°C in wanieso. Washing of meat did not improve the gel strength or MHC degradation of meat gel at 40°C in tokageeso or at 60°C in maeso. Moreover, washing of meat showed an enhancing effect on MHC degradation of maeso and wanieso meat gels at 40°C. These findings indicate that the gel-degrading factors (GDFs) which existed in these species were not only sarcoplasmic (Sp) and myofibrillar (Mf) type active at 60°C but also Mf type active at 40°C and Sp type active at 70°C.