Search

Sea urchin Mesocentrotus nudus, Glyptocidaris crenularis, and Strongylocentrotus intermedius gonad protein isolates (mnGPIs, gcGPIs, and siGPIs) were extracted by isoelectric solubilization/precipitation (ISP) from the defatted gonads, and their functional properties were compared. Sodium dodecyl sulfate polyacrylamide gel electrophoresis results showed the similar protein pattern between each protein isolate and defatted gonad, indicating the high efficiency of ISP processing for protein recovery. Amino acid profileconfirmed that the mnGPIs and siGPIs could be potential sources of essential amino acid in nature. As regard to functional properties, mnGPIs showed higher water- and oil- holding capacities followed bysiGPIs and gcGPIs and all protein isolates presented great foaming property. As for emulsifying activity index (EAI), mnGPIs, gcGPIs, and siGPIs showed the minimum solubility and EAI at pH 5, 3, and 4, respectively, and behaved a pH-dependent manner. The gcGPIs revealed the highest EAI from pH 6 to 8 among the samples. In addition, circular dichroism showed increased content of β-sheet at the expense of α-helix and β-turn, suggesting the structure denaturation of the protein isolates. Indeed, no statistical difference was observed between secondary structure of mnGPIs and siGPIs. Moreover, ISP processing increased free sulfhydryl content of sea urchin protein isolates, but no difference was observed among the samples. Furthermore, siGPIs revealed the highest amount of total sulfhydryl and disulfide bonds, whereas both defatted gonads and protein isolates from G. crenularis presented the maximum surface hydrophobicity. These results suggest that gonad protein isolates from three species of sea urchin possess various functionalities and therefore can be potentially applied in food system. PRACTICAL APPLICATION: Sea urchin M. nudus, G. crenularis, and S. intermedius gonads are edible, whereas the functional properties of protein isolates from sea urchin gonad remain unknown. In this case, the extraction and comparison of three species of sea urchin gonad protein isolates will not only confirm functional properties but also screen food ingredients with suitable functions. In this study, functionalities of protein isolates derived from M. nudus, G. crenularis, and S. intermedius gonads would provide potential application in bakery food and meat products or as emulsifier candidates in food system., (© 2020 Institute of Food Technologists®.)

Protein isolates were recovered from scallop (Patinopecten yessoensis) gonads to develop a novel functional matrix by investigating their physiochemical and functional properties. Scallop gonad protein isolates (SGPIs) were prepared from degreased scallop gonads (DSGs) by an alkali extraction and isoelectric solubilization/precipitation (ISP) process. The protein compositions of the SGPIs were mainly vitellogenin and beta-actin with molecular weights of 266 and 42 kDa, respectively, as determined using Nano-liquid chromatography-mass/mass (Nano-LC-MS/MS). After the ISP process, the protein solubility of the SGPIs was significantly improved, and the surface hydrophobicity of SGPIs intensely increased by 1.1-fold, which were attributed to the exposure of aromatic residues such as phenylalanine, tyrosine, and tryptophan. However, the content of total/reactive sulfhydryl in SGPIs was decreased compared with that of DSGs. Meanwhile, the ISP process caused partial protein unfolding, as indicated by circular dichroism analysis, which exhibited a remarkable rise in the β-sheet content with a parallel decline in the α-helix and random coil contents (P < 0.05). SGPIs exhibited a better oil absorption capacity and foaming property than both DSGs and soybean protein isolates (SPIs). Moreover, the emulsifying capacity of SGPIs was greatly enhanced by the ISP process, which was superior to the effect of commercial SPIs and was ascribed to its favorable solubility as well as surface characteristics. PRACTICAL APPLICATION: During the processing of scallop (Patinopecten yessoensis) adductors, scallop gonad, a high-protein part, is usually discarded as processing by-products despite its edibility. In recent years, scallop gonads are regarded as good sources to develop protein matrices due to their high protein content and numerous nutrients. In this study, scallop gonad protein isolates (SGPIs) were isolated by isoelectric solubilization/precipitation (ISP) process. The preferable solubility, foaming property coupled with high emulsifying property of SGPIs indicated that the SGPIs could be potentially utilized as a good protein emulsifier and additives in production of kamaboko gels, hamburger patties, sausages, and pet foods., (© 2019 Institute of Food Technologists®.)

The objective of this study was to investigate the properties of ternary composite gel of scallop (Patinopecten yessoensis) protein hydrolysates (SMGHs)/κ‐carrageenan (KC)/xanthan gum (XG). The rheological properties, moisture‐distribution, molecular structure, and microstructure of SMGNs/KC/XG gels were analyzed. The results showed that the G′ value, melting temperature, and water holding capacity of SMGHs/KC/XG were higher than those of SMGHs, SMGHs/KC, and SMGHs/XG. FTIR spectrum showed the generation of hydrogen bonds between SMGHs and KC/XG, and the carboxylic acid group of XG interacts with SMGHs. Moreover, the cryo‐SEM results showed that SMGHs/KC/XG exhibited a tighter, smoother, and more aggregated microstructure than those of SMGHs, SMGHs/KC, and SMGHs/XG. These results indicate that the gel and microstructural properties of SMGHs are significantly improved by addition of KC and XG, and SMGHs/KC/XG has potential to be used as functional hydrogels for food, pharmaceutical, and biomedical applications. Practical Application: Scallop (Patinopecten yessoensis) male gonads are rich in protein and usually regarded as byproducts during adductor processing. Because of its gelation properties, scallop male gonads have potential to be used as functional hydrogels for food. The SMGHs/KC/XG ternary composite gel showed excellent gel properties, which would be potentially applied in delivery system in food and biological fields. Further study is undergoing to apply SMGHs/KC/XG to embed bioactive compounds, such as curcumin and β‐carotene. [ABSTRACT FROM AUTHOR]

Roes are the main byproducts during the processing of large yellow croaker (Pseudosciaena crocea) and have not been well utilized. Heat-induced gels were prepared by using P. crocea roe protein isolates (pcRPI), and the influence of pH on the gel properties was also investigated. pcRPI could not form a gel at pH 4–6 but showed gelation behaviors at pH 7–9. The pcRPI gels prepared at pH 8 had a lower gel point (84 °C), and their G ′ reached 535.4 Pa. Moreover, pcRPI gels formed at pH 8–9 had a more continuous network structure with a shorter T 2 relaxation time than those at other pH conditions. Additionally, vitellogenin and vitellogenin B and C in pcRPI easily formed protein complexes during heating. The hydrophobic interactions, which were the main force between protein molecules during heating, as shown by molecular dynamics simulation, also contributed to gel formation. pcRPI has the potential to be used as a novel hydrogel product in food and other fields. • The optimum pH of P. crocea roe protein isolates (pcRPI) to form gels was pH 8. • The water holding ability of pcRPI gels was enhanced as pH increased. • The pcRPI gels had smoother surface and continuous network structure at pH 8–9. • Hydrophobic interactions were the main forces in the formation of pcRPI gels. [ABSTRACT FROM AUTHOR]

• Gellan gum (GG) improved gel formation of protein isolate from P. crocea roe (pcRPI). • GG improved the rheological properties and water holding ability of pcRPI gels. • The pcRPI-GG binary gels showed denser, more aggregated network structure. • GG improved the protective effects of curcumin by pcRPI gels with control release. The aim of this study was to investigate the effect of gellan gum (GG) on the cold gelation of large yellow croaker roe protein isolate (pcRPI). The water-holding ability and storage modulus of the pcRPI-GG binary gels increased with the GG concentration, where the storage modulus of the pcRPI-0.2% GG gel was approximately 30.7 times that of the pure pcRPI gel. Compare to the other binary gels, pcRPI-0.2% GG gels exhibited a lower lacunarity and higher junction density, with a denser, more aggregated microstructure. Consequently, curcumin was embedded in pcRPI-0.2% GG gels, and simulated gastrointestinal digestion test results showed that GG addition effectively protected and slowed curcumin release in the gastrointestinal environment. These findings may contribute to elucidating the interaction of pcRPI with GG and demonstrate the potential of binary gels for the embedding and delivery of active substances. [ABSTRACT FROM AUTHOR]

In this study, cold-set large yellow croaker (Pseudosciaena crocea) roe protein isolate (pcRPI) gels were prepared by glucono-δ-lactone (GDL) at different concentrations. The 0.1% and 0.2% GDL induced pcRPI at 50 mg/mL to form cold-set gels, while pcRPI suspension with 0.4% GDL addition still showed a fluid state. The pcRPI gel induced by 0.2% GDL showed better rheological properties and its G' value was about 5.1 times than that of 0.1% GDL. In addition, pcRPI gels induced by 0.1% and 0.2% GDL showed similar water holding capacity, and 0.2% GDL-induced pcRPI gels showed a special T 2 peak in 2249.0 ms which might represent free water on the surface of the gel. Furthermore, the higher total number of junctions, vessels percentage area, and lower lacunarity indicated a denser three-dimensional network structure in pcRPI gels induced by 0.1% and 0.2% GDL. Particle size tests and AFM results further confirmed that GDL induced pcRPI to form cold-set gels by promoting the formation of protein aggregates. Therefore, 0.1–0.2% GDL are suitable to prepare pcRPI cold-set gels. These results may deepen the understanding on cold-set pcRPI gels induced by GDL. • Pseudosciaena crocea roe protein isolates (pcRPI) had potential to form cold-set gels. • 0.2% glucono-δ-lactone (GDL)-induced pcRPI gels showed good rheological properties. • The 0.1–0.2% GDL induced pcRPI gels had a dense three-dimensional network structure. • GDL-induced pcRPI gels were promoted by the formation of protein aggregates. [ABSTRACT FROM AUTHOR]

• Protein isolates (pcRPIs) and lipids (pcRLs) of large yellow croaker roes were extracted simultaneously. • The purity of pcRPIs was greater than 70% with vitellogenin, vitellogenin B and vitellogenin C as main proteins. • pcRLs were mainly composed of triglyceride with high level of EPA and DHA content. • pcRPIs exhibited better physicochemical and functional properties than pcR. • pcRPIs had the better oil holding capacity and emulsifying abilities than soy protein isolate. The objective of this study was to simultaneously obtain protein isolates and lipids from the dried powder of large yellow croaker (Pseudosciaena crocea) roes (pcRs) to achieve high-value utilization. Protein isolates and lipids were extracted simultaneously from pcRs by saline and acidic solutions. The purity of the protein isolates from the pcRs (pcRPIs) was greater than 70%, with vitellogenin, vitellogenin B and vitellogenin C as the main proteins. The lipids from pcRs (pcRLs) were mainly composed of triglycerides with high levels of EPA and DHA. The pcRPIs exhibited a higher surface hydrophobicity, water/oil holding capacity and emulsifying ability than those of the pcRs. Moreover, pcRPIs had a better oil holding capacity and emulsifying ability than soy protein isolate. These results suggest that protein isolates and lipids can be simultaneously extracted by saline and acidic solutions, and pcRPIs and pcRLs can be used as functional materials in the food industry. [ABSTRACT FROM AUTHOR]

Protein isolate of sea cucumber guts (SCGPI) was extracted from defatted power of sea cucumber guts (SCGs) by alkaline extraction and acid precipitation method. The physicochemical and functional properties of SCGPI were evaluated in comparison with those of SCGs. It was found that the SCGPI showed higher whiteness, and contained 39.5% of the essential amino acids with higher protein efficiency ratio. The functionalities of SCGPI, including solubility, water/oil holding capacity (WHC/OHC), foaming capacity (FC), and emulsifying abilities (EAI), were significantly higher than those of SCGs. SCGPI exhibited higher total sulfhydryl group, disulfide bond, β‐turns, and random coil, while less surface hydrophobicity and α‐helix than SCGs. The thermal denaturation temperature of SCGPI was 46.55°C and the microstructure of SCGPI was flaky. Moreover, OHC, FC, and EAI of SCGPI were significantly better than those of SPI. These results suggest SCGPI can be used as functional bases in the food industry. Practical applications: Sea cucumber (Stichopus japonicus) guts are the main byproducts in the sea cucumber processing, which are rich in protein. In this study, we prepared protein isolate from sea cucumber guts (SCGPI) by alkaline extraction and acid precipitation method. The results showed that SCGPI exhibited great solubility, water/oil holding capacity, foaming capacity, and emulsifying abilities. The present study demonstrates that SCGPI can be used as a functional base in the food industry. [ABSTRACT FROM AUTHOR]