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Amino acid compositions (%) of isolate processed waters (IPW-3) produced from the protein isolates preparation of fish roes by ISP process

Amino acid compositions (%) of isolate processed waters (IPW-3) produced from the protein isolates preparation of fish roes by ISP process

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Article
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This study evaluated the protein recovery, functional properties and biological activity of isolate processed water (IPW) generated in the preparation of protein isolates from fish roes (BH, bastard halibut Paralichthys olivaceus; ST, skipjack tuna Katsuwonus pelamis; YT, yellowfin tuna Thunnus albacares) by an isoelectric solubilization and precip...

Citations

... 10 (Kang et al., 2007;Lee et al., 2017;Yoon et al., 2017). ...
... legumes (Horax et al., 2004), oilseeds (Horax et al., 2011), cereals (Agboola et al., 2005;Paraman et al., 2007) ( Azadian et al., 2012) . (Heu et al., 2006;Kang et al., 2015;Lee et al., 2016bLee et al., , 2017Yoon et al., 2017). ...
Article
Four roe protein isolates (RPIs) from olive flounder Paralichthys olivaceus roes (OFR) were recovered by isoelectric solubilization (pH 11 and 12) and precipitation (pH 4.5 and 5.5) and investigated for their food characteristics. RPIs contained 4.5–9.6% moisture, 64.1-69.5% protein, 16.1-19.8% lipid, and 1.0-3.9% ash. The protein yields of RPIs ranged from 50.1 to 56.8%, which was significantly different depending on the recovery conditions. A difference was observed in the SDS-PAGE protein band (25–100 kDa) between the alkaline solubilization at pH 11 (RPI-1 and 2) and pH 12 (RPI-3 and 4). The major amino acids of RPIs were Leu, Lys, Asp, Glu and Ala and major mineral components were sulfur, sodium, phosphorus, and magnesium, which were significantly different from OFR (P<0.05). Additionally, the lead and cadmium content was below the chemical hazard standard of the Korean food standards code. The Hunter color and whiteness of RPIs also showed significant differences according to the treatment conditions of the ISP process (P<0.05). This suggests that protein isolates recovered from olive flounder roes have high potential as nutritional supplements.
... , (130-180 μg/mL; Yoon et al., 2020), (82 μg/ mL; Yoon et al., 2018d) (103 μg/ mL; Cha et al., 2020), (160-170 μg/mL; Kim et al., 2016) , (33-97 μg/ml, Lee et al., 2017), (28-45 μg/mL) (55-110 μg/ml, Yoon et al., 2017) . , peptide , peptide , , (Wu et al., 2003). ...
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Boil-dried concentrate (BDC) and steam-dried concentrate (SDC) were prepared from olive flounder Paralichthys olivaceus roe using the cook-dried process, and their food functionality and in vitro bioactivity were examined. The buffer capacity of BDC and SDC was found to be stronger in the alkaline region than in the acidic region, and the buffer capacity of SDC was superior to that of BDC. The water holding capacities of these concentrates were 7.6 and 7.4 g/g protein, respectively, both of which were significantly lower than that of freeze-dried concentrate (FDC). The solubility of BDC (13.4%) and SDC (12.7%), foaming capacity of BDC (107.7%) and SDC (110.6%), and oil-in-water emulsifying activity index of BDC (7.7 m2/g) and SDC (9.7 m2/g) were all significantly lower than the corresponding values for FDC (P<0.05). The lower food functionality of BDC and SDC compared with FDC can be attributed to the high-temperature denaturation of proteins during the cook-dried process. The 2,2′-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid radical scavenging activities (IC50) of SDC (2.5 mg protein/mL) was 60.4 μg/mL, and the angiotensin I converting enzyme inhibitory activity was 80.9%. Olive flounder roe concentrates have good antioxidant and antihypertensive activities, and can be used as materials or ingredients in the processing of seafood and other foods to enhance protein contents and food functionality.
... En cambio, las proteínas recuperadas al vapor mostraron actividad antihipertensiva medida por la capacidad inhibidora de la enzima convertidora de angiotensina I (ECA), siendo mayor dicha actividad en el lenguado japonés con un IC50 de 1.04 mg/mL. Usando estos mismos efluentes, pero sometidos a un proceso de precipitación y solubilización isoeléctrica,Lee et al., (2017) obtuvieron la mejor actividad inhibidora de ECA en bonito (IC50 = 1.52 mg/ml) y un mayor poder reductor y actividad de tipo superóxido dismutasa para lenguado japonés. Por su parte, Mahdabi y Shekarabi (2018) evaluaron las características funcionales y propiedades antioxidantes de hidrolizados proteicos de harina y agua de cola de anchoveta (Clupeonella sp.). ...
Chapter
La industria procesadora de productos pesqueros, derivado de sus actividades productivas, genera una importante cantidad de residuos líquidos, los cuales son comúnmente conocidos como efluentes pesqueros. Muchos de estos efluentes, son descargados al medio ambiente sin recibir algún tratamiento, generando un impacto negativo en los cuerpos de agua y zonas costeras donde son vertidos. Por otro lado, estudios han determinado que estos efluentes poseen concentraciones importantes de materia sólida, principalmente proteínas. Dicha proteína es de alta calidad considerando su perfil de aminoácidos, por lo cual es de interés emplear tecnologías para poder concentrarlas y recuperarlas. Una vez recuperada la fracción proteica de los efluentes pesqueros, a partir de esta se pueden obtener productos con alto valor agregado (p.ej. hidrolizados proteicos y péptidos bioactivos) aplicando tecnología enzimática. Las aplicaciones de estos nuevos productos en la industria alimentaria (humana o animal), pueden ser amplias y de importante valor económico. En esta revisión, se discutirá lo relacionado a alternativas de aprovechamiento de los efluentes generados en la industria pesquera, enfocándose en la recuperación y la utilización de fracciones proteicas. Se incluyen algunas técnicas empleadas para su obtención, mencionando sus ventajas y requerimientos; así como las propiedades tecno-funcionales y biológicas de las proteínas o sus hidrolizados proteicos obtenidos a partir de los efluentes pesqueros, y finalmente, se discutirá los usos y aplicaciones de efluentes pesqueros y sus hidrolizados como reemplazo de harina de pescado para la formulación de alimentos acuícolas, lo cual acarrea ventajas sobre el desempeño productivo y/o sobre distintos indicadores de la salud de los organismos.
... Vitellogenin and vitellogenin derivatives derived from tuna roe have been reported as considerable functional proteins (Yoon et al., 2018). Isolated proteins from there different fish roes, including halibut, skipjack tuna, and yellowfin tuna treated by ISP processing have been demonstrated to have good emulsifying activity (Lee et al., 2017). Moreover, the comparison of functional properties of protein isolates from catfish (Batrachocephalus mino), Indian mackerel (Rastrelliger kanagurta), ponyfish (Aurigequula fasciata), and sardine (Sardinella brachysoma) and protein isolates from salmon, cod, and herring by-products have also been reported by Kumarakuru, Reddy, and Haripriya (2018) and Abdollahi and Undeland (2019), respectively. ...
... Both sea urchin and fish are aquatic animals, and sea urchin gonads as well as fish roes have similar biological function. Lee et al. (2017) have studied foaming properties of protein isolates from bastard halibut, skipjack tuna, and yellowfin tuna roe, which exhibited similar FC values but lower FS values in comparison to those of protein isolates from sea urchin. Moreover, the protein isolates from sea urchins also had higher FC and FS than those of Channa striatus and Lates calcarifer roe protein concentrates (Galla, Karakala, Akula, & Pamidighantam, 2012). ...
Article
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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.
... FRCs (0.082 mg/mL; Yoon et al., 2108a) (0.103 mg/mL; Cha et al., 2020), (0.16-0.17 mg/mL; Kim et al., 2016), (0.033-0.16 mg/mL; Lee et al., 2017), (0.028-0.045 mg/mL) (0.055-0.11 mg/mL; Yoon et al., 2017) . ...
Article
The purpose of this study was to evaluate the food functional properties and in vitro bioactivity of vacuum freezedried fish roe concentrates (FRCs) prepared from Alaska pollock Theragra chalcogramma (AP), bastard halibut Paralichthys olivaceus (BH) and skipjack tuna Katsuwonus pelamis (ST). All three species showed better buffering capacity on the alkaline side (pH 10-12) than on the acidic side. The water-holding capacities of the FRCs were 3.5, 8.5 and 4.2 g/g protein for AP, BH and ST, respectively, and were significantly higher than that of commercial egg white. The protein solubilities of the FRCs were 42.5% (AP), 50.0% (BH) and 13.9% (ST). The foaming capacities of the FRCs were not significantly different among the species (128.0% for AP, 128.3% for BH, and 143.3% for ST; P>0.05), and their foam stability was maintained at 53.0-74.2% for 60 minutes. The oil-in-water emulsifying activity indexes of AP and BH (19.5 and 20.2 m2/g protein, respectively) were significantly superior to that of ST (P<0.05). The 2,2-diphenyl-1-picrylhydrazyl and 2,2′-azino-bis-3-ethylbenzothia-zoline-6-sulfonic acid radical-scavenging activities (IC50, mg/mL) of the FRCs were in the ranges of 1.05-3.26 and 0.13-0.18 mg/mL, respectively, and the angiotensin I converting enzyme inhibitory activity was in the range of 0.97-1.89 mg/mL.
... Lipid (13.8 ± 2.5-15.6 ± 1.0%) and ash content (1.8 ± 0.6-3.6 ± 0.1%) in the RPIs were lower than those in FDSTR (p < .05). This reduction in lipid and mineral content occurred because of mineral and fat migration into the processed water during ISP (Lee et al., 2017;. The protein content of RPI-2 and RPI-4 precipitated at pH 5.5 after alkaline solubilization was significantly higher than that of RPI-1 and RPI-3 precipitated at pH 4.5 (p < .05). ...
... Acid precipitation at pH 4.5 during ISP was found to be effective for removing minerals (potassium, sodium, sulfur, and phosphorus) except for iron. Therefore, most minerals in FDSTR migrated into the processed water during ISP (Lee et al., 2017;. ...
Article
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Four roe protein isolates (RPIs) from skipjack tuna were prepared using isoelectric solubilization (pH 11 and 12) and precipitation (pH 4.5 and 5.5) (ISP) at different pH points to evaluate their physicochemical and functional properties and in vitro bioactivities. Moisture (<6.3%) and protein (71%–77%) content were maintained. Sulfur, sodium, phosphorus, and potassium were the major elements, and glutamic acid and leucine were the prevalent amino acids (12.2–12.8 and 9.6–9.8 g/100 g protein, respectively) in RPIs. RPI-1 showed the highest buffering capacity at pH 7–12. RPIs and casein showed similar water-holding capacities. At pH 12, RPI-1(pH 11/4.5) showed the highest solubility, followed by RPI-3(pH 12/4.5), RPI-2(pH 11/5.5), and RPI-4(pH 12/5.5) (p < .05). Oil-in-water emulsifying activity indices of RPI-1 and RPI-3 significantly differed. At pH 2 and 7–12, pH-shift treatment improved the food functionality of RPIs, which was superior to positive controls (casein and hemoglobin). RPI-1 showed ABTS+ radical scavenging (102.7 μg/ml) and angiotensin-converting enzyme inhibitory activities (44.0%).
... The global demand for proteins is increasing, and more food proteins are needed from the source of conventional proteins as well as the new source of protein. If we accept that all proteins will have nutritional value, the value in the food industry for both conventional and new protein sources is required to have enough food functional properties to allow the protein to be accepted as a food ingredient (Azadian, Nasab, & Abedi, 2012;Horax, Hettiarachchy, Kannan, & Chen, 2011;Lee et al., 2017). Among fish by-products, fish roes are highly nutritious material rich in essential fatty acids, minerals, and amino acids (Heu et al., 2006;Park et al., 2016). ...
... dispersion was 82.9 μg/ml and showed better scavenging activity than that (160-170 μg/ml) of enzyme hydrolysates from shrimp processing by-products (Kim, Yoon, Shim, & Lim, 2016). It also exhibited similar or slightly weaker scavenging activity than those of isolate processed water (33-97 μg/ml, Lee et al., 2017), extracts (28-45 μg/ ml), and cooking drips (55-110 μg/ml, Yoon et al., 2017) of fish roe. ...
... Current research on natural ACE inhibition peptides has extended to seafood protein sources, particularly seafood by-products. Lee et al. (2017) and Yoon et al. (2017) showed that the 50% ACE inhibitory activity concentration of processed waters recovered from fish roes ranged from 1.2 to 2.0 mg/ml, and these processed waters recovered through heat or alkali/acid treatment showed no difference according to treatment method in ACE inhibitory activity. On the other hand, the enzyme hydrolysates of skate skin gelatin (Ngo, Ryu, & Kim, 2014), yellow sole frame , skipjack roe (Intarasirisawat, Benjakul, Wu, & Visessanguan, 2013), and Pacific cod skin (Himaya, Ngo, Ryu, & Kim, 2012) showed 35%-86% ACE inhibitory activity and similar or superior to the results of this experiment. ...
Article
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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.
... 서 론 (Food and Agriculture Organization of the United Nations, FAO) , 2015 2 (FAO, 2015), 10 , 327 (MOF, 2017). , , frame, , , 30-60% (Narsing Rao et al., 2014;Klomklao and Benjakul, 2016), 10 ( Lee et al., 2017;Yoon et al., 2017). , , . ...
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This study investigated the potential of collagenous protein fractions (CPFs) as functional foods. The specific CPFs studied were recovered from the roe of bastard halibut (BH), Paralichthys olivaceus; skipjack tuna (ST), Katsuwonus pelamis; and yellowfin tuna (YT), Thunnus albacares through the alkaline solubilization process at pH 11 and 12. The buffer capacity, water-holding capacity and solubility of CPFs with pH-shift treatment were significantly better at alkaline pH (10-12) than at acidic pH (2.0). At pH-shift treatment (pH 2 and 12), the foaming capacities of CPFs from ST and YT were improved compared to those of controls, but they were unstable compared to BH CPFs. The emulsi-fying activity index (EAI, m 2 /g protein) of CPFs (controls) was 16.0-21.1 for BH, 20.1-23.9 for ST and 9.3-13.7 for YT (P<0.05). CPFs adjusted to pH 12 showed improved EAI and YT CPFs showed significantly greater emulsifying ability than those from BH and ST. CPFs recovered from fish roe are not only protein sources but also have a wide range of food functionalities, confirming the high availability of fish sausage and surimi-based products as protein or reinforcing materials for functional foods and alternative raw materials.
Article
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In the present study, protein hydrolysates were prepared from olive flounder Paralichthys olivaceus roe concentrate using different commercial proteases, and their functional properties and bioactivities were examined. Protamex (PR; 21.6%) showed the highest degree of hydrolysis, followed by alcalase (AL; 21.1%) and aroase AP-10 (AA; 20.2%). With regard to foaming activity, trypsin, chymotrypsin (CH), and bromelain (BR) had values ranging 181–188%, followed by neutrase (152%) and AA (141%). CH (36%) and BR (70%) maintained foam stability for up to 15 min. The oil-in-water emulsifying activity index of CH (10.6 m2/g) was the highest among all the hydrolysates. Notably, the 2,2′-azino-bis-3-ethylbenzo-thiazoline-6-sulfonic acid (ABTS+) radical scavenging activities (IC50) were significantly higher in pantidase NP-2 (68.1 μg/mL) and flavourzyme (FL, 69.8 μg/mL) than in other hydrolysates. The tyrosinase inhibitory activities of FL, PR, and AA were inhibited by 12.5–19.8%. Aangiotensin I converting enzyme inhibitory activity of the control was 80.9%, and that of the hydrolysates of CH, AA, PR, and AL, which exhibited higher inhibitory activity, ranged 87.6–90.7%. CH, BR, and AA AP-10 hydrolysates exhibited superior bioactivity and functional properties. Therefore, these hydrolysates can be used as food ingredients in novel types of functional food-enhancing seafood and food processing industries.
Article
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We investigated the functional properties and in vitro bioactivity of protein isolates (RPIs) recovered from olive floun�der Paralichthys olivaceus roes by isoelectric solubilization/precipitation process, according to pH-shift treatments. The buffer capacity of RPIs was shown to be stronger in alkaline pH than in acidic pH. Water holding capacity of RPIs was in range of 4.5–5.2 g/g protein with no significant differences (P>0.05). The foaming capacity and emulsifying activ�ity index of RPIs did not show any significant differences between RPI-1 (pH 11/4.5) and 3 (pH 12/4.5), however they were superior to RPI-2 (pH 11/5.5) and 4 (pH 12/5.5). The 2,2′-azino-bis-3-ethylbenzo-thiazoline-6-sulfonic acid radical scavenging activity of RPI-3 (2.5 mg protein/mL) was 102.4 μg/mL, and the angiotensin I converting enzyme inhibitory activity was 30.8%. Among the RPIs, RPI-3 was relatively superior in protein functional properties such as buffer capacity, foaming capacity, emulsification, and anti-oxidative activity. Therefore, we suggest that RPI prepared from olive flounder roes could serve as a potential food resource.