Sung Hwan Park’s research while affiliated with Gyeongsang National University and other places

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Publications (13)


Fig. 1. pH values (A) and buffer capacity (B) of roe protein concentrates (RPCs) from yellowfin tuna prepared by cook-dried process. Data are mean±standard deviation of triplicate determinations. Values with different letter within samples are significantly different at p<0.05 by Duncan's multiple range test.  
Fig. 3. Foam stability of roe protein concentrates (FDC, BDC, and SDC) prepared from yellowfin tuna by cook-dried process at various pH (2-12). Data represent the mean±SD of n=3.  
Foaming capacity (%) of yellowfin tuna roe concentrates (FDC, BDC, and SDC) prepared by cook-dried process
Emulsifying activity index (EAI, m 2 /g of protein) of yellowfin tuna roe concentrates (FDC, BDC, and SDC) prepared by cook-dried process
Protein functionality of concentrates prepared from yellowfin tuna (Thunnus albacares) roe by cook-dried process
  • Article
  • Full-text available

December 2016

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285 Reads

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24 Citations

Food Science and Biotechnology

Sung Hwan Park

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Hyun Ji Lee

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In Seong Yoon

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[...]

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Three kinds of roe protein concentrates (RPCs: boil-dried concentrate, BDC; steam-dried concentrate, SDC; freeze-dried concentrate, FDC) were prepared from yellowfin tuna to produce value added products for food applications. The buffer capacities of the RPCs were higher under alkaline than under acidic conditions. The water holding capacities of the RPCs were in range 4.5–4.7 g/g protein at pH 6.0. The protein solubility of the FDC (14.2%) was higher than those of the BDC (5.4%) and SDC (5.5%) at pH 6.0. The foaming capacity of the FDC (156.8%) was higher than those of the BDC (109.7%) and SDC (109.4%); the FDC foam was stable for 60 min. The oil-in-water emulsifying activity index of the FDC (12.2m2/g protein) exceeded those of the BDC and SDC (2.2m2/g protein). Protein concentrates from yellowfin tuna roe may be useful as a potential protein source and as a high-value food ingredient.

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Recovery of serine protease inhibitor from fish roes by polyethylene glycol precipitation

July 2016

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190 Reads

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4 Citations

Fisheries and Aquatic Sciences

The fractionation of serine protease inhibitor (SPI) from fish roe extracts was carried out using polyethylene glycol-4000(PEG4000) precipitation. The protease inhibitory activity of extracts and PEG fractions from Alaska pollock (AP), bastardhalibut (BH), skipjack tuna (ST), and yellowfin tuna (YT) roes were determined against target proteases. All of the roeextracts showed inhibitory activity toward bromelain (BR), chymotrypsin (CH), trypsin (TR), papain-EDTA (PED), andalcalase (AL) as target proteases. PEG fractions, which have positive inhibitory activity and high recovery (%), were thePEG1 fraction (0–5%,w/v) against cysteine proteases (BR and PA) and the PEG4 fraction (20–40 %,w/v) against serineproteases (CH and TR). The strongest specific inhibitory activity toward CH and TR of PEG4 fractions was AP (9278 and1170 U/mg) followed by ST (6687 and 2064 U/mg), YT (3951 and 1536 U/mg), and BH (538 and 98 U/mg). Theinhibitory activity of serine protease in extracts and PEG fractions from fish roe was stronger than that of cysteineprotease toward common casein substrate. Therefore, SPI is mainly distributed in fish roe and PEG fractionationeffectively isolated the SPI from fish roes. Recovery of serine protease inhibitor from fish roes by polyethylene glycol precipitation. Available from: https://www.researchgate.net/publication/305637522_Recovery_of_serine_protease_inhibitor_from_fish_roes_by_polyethylene_glycol_precipitation [accessed Jul 26, 2016].


Characterization of Calcium Lactate Prepared from Butter Clam Saxidomus purpuratus Shell Powder

June 2016

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562 Reads

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5 Citations

Korean Journal of Fisheries and Aquatic Sciences

To facilitate the effective use of butter clam shell as a natural calcium resource, we determined the optimal conditions for calcium lactate (BCCL) preparation with high solubility using response surface methodology (RSM). The polynomial models developed by RSM for pH, solubility and yield were highly effective in describing the relationships between factors (P<0.05). Increased molar ratios of calcined powder (BCCP) from butter clam shell led to reduced solubility, yield, color values and overall quality. The critical values of multiple response optimization to independent variables were 1.75 M and 0.94 M for lactic acid and BCCP, respectively. The actual values (pH 7.23, 97.42% for solubility and 423.22% for yield) under optimization conditions were similar to the predicted values. White indices of BCCLs were in the range of 86.70–90.86. Therefore, organic acid treatment improved color value. The buffer-ing capacity of BCCLs was strong, at pH 2.82 to 3.80, upon the addition of less than 2 mL of 1 N HCl. The calcium content and solubility of BCCLs were 6.2–16.7 g/100 g and 93.6-98.5%, respectively. Fourier transform analysis of infrared spectroscopy data identified BCCL as calcium lactate pentahydrate, and the analysis of microstructure by field emission scanning electron microscopy revealed an irregular form.


Preparation and characterization of protein isolate from Yellowfin tuna Thunnus albacares roe by isoelectric solubilization/precipitation process

May 2016

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647 Reads

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38 Citations

Fisheries and Aquatic Sciences

Isoelectric solubilization/precipitation (ISP) processing allows selective, pH-induced water solubility of proteinswith concurrent separation of lipids and removal of materials not intended for human consumption such asbone, scales, skin, etc. Recovered proteins retain functional properties and nutritional value. Four roe proteinisolates (RPIs) from yellowfin tuna roe were prepared under different solubilization and precipitation condition(pH 11/4.5, pH 11/5.5, pH 12/4.5 and pH 12/5.5). RPIs contained 2.3–5.0 % moisture, 79.1–87.8 % protein, 5.6–7.4%lipidand3.0–3.8 % ash. Protein content of RPI-1 and RPI-2 precipitated at pH 4.5 and 5.5 after alkalinesolubilization at pH 11, was higher than those of RPI-3 and RPI-4 after alkaline solubilization at pH 12 (P< 0.05).Lipid content (5.6–7.4 %) of RPIs was lower than that of freeze-dried concentrate (10.6 %). And leucine and lysineof RPIs were the most abundant amino acids (8.8–9.4 and 8.5–8.9 g/100 g protein, respectively). S, Na, P, K asminerals were the major elements in RPIs. SDS-PAGE of RPIs showed bands at 100, 45, 25 and 15 K. Moisture andprotein contents of process water as a 2’nd byproduct were 98.9–99.0 and 1.3–1.8 %, respectively. Therefore,yellowfin tuna roe isolate could be a promising source of valuable nutrients for human food and animal feeds.


Chemical composition of protein concentrate prepared from Yellowfin tuna Thunnus albacares roe by cook-dried process

May 2016

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925 Reads

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34 Citations

Fisheries and Aquatic Sciences

Roe is the term used to describe fish eggs (oocytes) gathered in skeins and is one of the most valuable food products from fishery sources. Thus, means of processing are required to convert the underutilized yellowfin tuna roes (YTR) into more marketable and acceptable forms as protein concentrate. Roe protein concentrates (RPCs) were prepared by cooking condition (boil-dried concentrate, BDC and steam-dried concentrate, SDC, respectively) and un-cooking condition (freeze-dried concentrate, FDC) from yellowfin tuna roe. The yield of RPCs was in the range from 22.2 to 25.3 g/100 g of roe. RPCs contained protein (72.3–77.3 %), moisture (4.3–5.6 %), lipid (10.6–11.3 %) and ash (4.3–5.7 %) as the major constituents. The prominent amino acids of RPCs were aspartic acid, 8.7–9.2, glutamic acid, 13.1–13.2, and leucine, 8.5–8.6 g/100 g of protein. Major differences were not observed in each of the amino acid. K, S, Na, and P as minerals were the major elements in RPCs. No difference noted in sodium dodecyl sulfate polyacrylamide gel electrophoresis protein band (15–100 K) possibly representing partial hydrolysis of myosin. Therefore, RPCs from YTR could be use potential protein ingredient for human food and animal feeds.


Table 3 . Response surface model for acetic acid treated calcium from littleneck clam calcined powder
Table 4 . Optimal conditions of multiple responses for preparation of calcium acetate from littleneck clam calcined powder using MINITAB program
Table 6 . Hunter's color values and white index of calcium acetate from littleneck clam calcined powder
Optimization of Calcium Acetate Preparation from Littleneck Clam (Ruditapes philippinarum) Shell Powder and Its Properties

June 2015

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380 Reads

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11 Citations

Korean Journal of Food Science and Technology

The optimal condition for preparation of powdered calcium acetate (LCCA) which has high solubility, from calcined powder (LCCP) of the littleneck clam shell by response surface methodology (RSM) was examined. Increased molar ratio of LCCP led to reduced solubility, yield, color values, and overall quality. The critical values of multiple response optimization of independent variables were 2.57 M of acetic acid and 1.57 M of LCCP. The actual values (pH 7.0, 96.1% for solubility, and 220.9% for yield) under the optimized condition were similar to the predicted values. LCCA showed strong buffering capacity between pH 4.89 and 4.92 on addition of ~2 mL of 1 N HCl. The calcium content and solubility of LCCA were 21.9-23.0 g/100 g and 96.1-100.1%, respectively. The FT-IR and XRD patterns of LCCA were identified as calcium acetate monohydrate, and FESEM images revealed an irregular and rod-like microstructure.


Fig. 2. Comparison of calcium solubility of calcium acetate from butter clam calcined powder.
Table 3 . Optimal conditions of multiple responses for preparation of calcium acetate from butter clam calcined powder using MINITAB program
Table 5 . Hunter's color values and white index of calcium ace- tate from butter clam calcined powder
Characteristics and Preparation of Calcium Acetate from Butter Clam (Saxidomus purpuratus) Shell Powder by Response Surface Methodology

June 2015

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366 Reads

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4 Citations

Journal of the Korean Society of Food Science and Nutrition

For effective utilization of butter clam shell as a natural calcium resource, the optimal conditions for preparation of calcium acetate (BCCA) with high solubility were determined using response surface methodology (RSM). The polynomial models developed by RSM for pH, solubility, and yield were highly effective in describing the relationships between factors (P<0.05). Increased molar ratio of calcined powder (BCCP) from butter clam shell led to reduction of solubility, yield, color values, and overall quality. Critical values of multiple response optimization to independent variables were 2.70 M and 1.05 M for acetic acid and BCCP, respectively. The actual values (pH 7.04, 93.0% for solubility and 267.5% for yield) under optimization conditions were similar to predicted values. White indices of BCCAs were in the range of 89.7∼93.3. Therefore, color value was improved by calcination and organic acid treatment. Buffering capacity of BCCAs was strong at pH 4.88 to 4.92 upon addition of ∼2 mL of 1 N HCl. Calcium content and solubility of BCCAs were 20.7∼22.8 g/100 g and 97.2∼99.6%, respectively. The patterns of fourier transform infrared spectrometer and X-ray diffractometer analyses from BCCA were identified as calcium acetate monohydrate, and microstructure by field emission scanning electron microscope showed an irregular form.


Fig. 3. Native-PAGE of fractions obtained from roe extracts of bas tard halibut Paralichthys olivaceus by fractionation methods base on the protein solubility (A1-4), net charge (D1-4) and molecular mass (S1-4). 
Trypsin inhibitory activities of fractions obtained from the roe extracts of bastard halibut Paralichthys olivaceus by chromatographic methods base on net charge toward casein and BAPNA as substrate
Trypsin inhibitory activities of fractions obtained from the roe extracts of bastard halibut Paralichthys olivaceus by chromatographic methods base on the molecular mass toward casein and BAPNA as substrate
Recovery and Fractionation of Serine Protease Inhibitors from Bastard Halibut Paralichthys olivaceus Roe

April 2015

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91 Reads

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4 Citations

Korean Journal of Fisheries and Aquatic Sciences

Protease inhibitors (PI) of trypsin and papain as target proteases from the roe of bastard halibut Paralichthys olivaceus were fractionated out using ammonium sulfate precipitation (A), DEAE 650M anion exchange chromatography (D), and Sephacryl S-300 gel filtration (S). The recovery percentages of the fractions with the strongest inhibitory activity for each fractionation method were 13% for the A4 fraction, 21.2% for the D3 fraction, and 21.3% for the S2 fraction, with specific inhibitory activities of the fractions toward trypsin and casein of 168, 139, and 218 U/mg, respectively, while no inhibition of papain was observed. The IC50 for the trypsin-specific substrate Nα-benzoyl-l-arginine-p-nitroanilide (BAPNA) was 0.65, 1.55, 2.26, and 2.85 mg/mL for the A4, S2, A3, and D3 fractions, respectively. These results suggest that chromatographic fractionation methods (D and S) based on the molecular mass and charge of the protein were more effective at fractionating PI than was ammonium sulfate precipitation based on protein solubility, and that the bastard halibut roe extract acts as a serine protease inhibitor. Therefore, the PI fraction from fish roe might be useful for inhibiting proteases in foodstuffs, and could constitute an alternative food-grade inhibitor for the surimi industry.


Table 1 . General information of butter clam Saxidomus purpuratus and littleneck clam Ruditapes philippinarum sampled from Geoje island 
Fig. 4. FT-IR spectra of shell and calcined powder from butter clam Saxidomus purpuratus and littleneck clam Ruditapes philippinarum. BCSP, butter clam shell powder; LCSP, littleneck clam shell powder; BCCP, butter clam calcined powder; LCCP, littleneck clam calcined powder. 
Fig. 5. XRD analyses of shell and calcined powder from butter clam Saxidomus purpuratus and littleneck clam Ruditapes philippinarum. BCSP, butter clam shell powder; LCSP, littleneck clam shell powder; BCCP, butter clam calcined powder; LCCP, littleneck clam calcined powder. 
Hunter's color values and white index of shell and cal- cined powder from butter clam Saxidomus purpuratus and little- neck clam Ruditapes philippinarum 
Characteristics of the Shells and Calcined Powders from the Butter Clam Saxidomus purpuratus and Littleneck Clam Ruditapes philippinarum as a Natural Calcium Resource

April 2015

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632 Reads

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6 Citations

Korean Journal of Fisheries and Aquatic Sciences

Shell waste from the butter clam Saxidomus purpuratus and littleneck clam Ruditapes philippinarum is a large by-product of shellfish aquaculture, and it is desirable to convert it into value-added products for industrial applications. In this study, calcium carbonate (CaC) polymorphs from butter clam (BCSP) and littleneck clam (LCSP) shell powders and commercial CaC were characterized using Fourier transmission infrared spectroscopy (FT-IR), X-ray diffraction (XRD), and scanning electron microscopy (SEM). The results revealed that the optimal calcination conditions to eliminate organic substances and improve solubility for both BCSP and LCSP were 800°C for 8 h in an electrical furnace. Calcination improved the white index of the butter clam (BCCP) and littleneck clam (LCCP) calcined powder compared with shell powders. The calcium content in BCCP (51.1%) was higher than that of LCCP (44.9%) or commercial calcium oxide (CaO, 44.7%). The XRD patterns of BCCP and LCCP were similar to that of CaO. Cubic-like crystals of CaC and irregular crystals of BCCP and LCCP were observed by SEM. The FT-IR and XRD analyses revealed the presence of calcite and aragonite in the BCSP and aragonite in the LCSP, whereas the CaC contained calcite. These results indicate that butter and littleneck clam shells are potential biomass resources for calcium carbonate and calcium oxide.


Fig. 2. Hydrolysis pattern and bitterness of tryptic casein hydrolysates incubated with GF-I fraction from the T. pacificus hepatopancreas crude extract during hydrolysis time. Numerical in parentheses represent the number of panel felt similar bitterness to 0.5-2% Gly-phe. Different letters on the symbol indicate a significant difference at p<0.05.
Fig. 3. Reverse-phase HPLC chromatograms of tryptic casein hydrolysates treated with GF-I fraction. CH: tryptic casein hydrolysate before GF-I fraction treatment, CH08: tryptic casein hydrolysate after 8 h of treatment with GF-I fraction, CH24: tryptic casein hydrolysate after 24 h of treatment with GF-I fraction.
Fig. 4. Hydrolysis of tryptic casein hydrolysates treated with GFI fraction as affected by enzyme concentration and hydrolysis time. Different letters of the different symbol indicate a significant difference at p<0.05.
Table 4 . Change in major peak area (%) from HPLC chromatograms of tryptic casein hydrolysates treated with GF-I as affected by enzyme concentration and hydrolysis time (Area %)
Bitterness evaluation of tryptic casein hydrolysates treated with active fractions obtained from the T. pacificus hepatopancreas crude extract by different fractionation methods for hydrolysis time
Lowering the Bitterness of Enzymatic Hydrolysate Using Aminopeptidase-active Fractions from the Common Squid (Todarodes pacificus) Hepatopancreas

December 2014

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132 Reads

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6 Citations

Korean Journal of Food Science and Technology

Aminopeptidase-active fractions from crude extract of the hepatopancreas of a common squid (Todarodes pacificus) were obtained using acetone (AC; 30-40%) and ammonium sulfate precipitation (AS; 60-70% saturation), anion exchange (AE-II; 0.2 M NaCl) and gel filtration chromatography (GF-I; 30-50 kDa), respectively. The debittering capacity of GF-I fraction based on the aminopeptidase activity (89.2 U/mg), recovery (56.6%) and sensory evaluation (1.0) was better than that of other fractions. Release of amino acids increased as incubation time was increased, and the bitterness of the enzyme reaction mixtures decreased. Incubation with the GF-I fraction for 24 h resulted in the hydrolysis of several peptides, as revealed by reverse-phase HPLC profiles. Peaks 3, 5 and 6 showed the decreased area (%), whereas peaks 1, 2 and 4 showed the increased area. The GF-I fractions were found to be suitable for reducing bitterness in protein hydrolysates by catalyzing the hydrolysis of bitter peptides. Lowering the Bitterness of Enzymatic Hydrolysate Using Aminopeptidase-active Fractions from the Common Squid (Todarodes pacificus) Hepatopancreas.


Citations (13)


... 1.5-10% , (11%), (75%) (13%) vitellogenin vitellogenin derivatives (Sikorski, 1994;Heu et al., 2006;Park et al., 2016;Kwon et al., 2022;Yoon et al., 2023) Mahmoud et al., 2008;Intarasirisawat et al., 2011) . ...

Reference:

Food Functionalities of Various Enzyme Hydrolysates Prepared from Olive Flounder Paralichthys olivaceus Steam-dried Roe Concentrate
Protein functionality of concentrates prepared from yellowfin tuna (Thunnus albacares) roe by cook-dried process

Food Science and Biotechnology

... (Heu et al., 2006;Kang et al., 2007;Kang et al., 2015;Kim et al., 2015;Lee et al., 2016b;Yoon et al., 2017). ( Lee et al., 2016a), (Heu et al., 2010;Lee et al., 2016b), Yoon et al., 2017) , (Lee et al., 2016a;Binsi et al., 2017;Yoon et al., 2018b), (Lee et al., 2016c), (Noh et al., 2013;Intarasirisawat et al., 2014) (Park et al., 2016;Binsi et al., 2017;Yoon et al., 2018b), (Heu et al., 2009;Intarasirisawat et al., 2014) . Lee et al., 2016b), (Binsi et al., 2017), (Lee et al., 2016;Yoon et al., 2018b), (Kim et al., 2012;Kim et al., 2014), / (Kristinsson et al., 2005;Lee et al., 2016c) . ...

Recovery of serine protease inhibitor from fish roes by polyethylene glycol precipitation

Fisheries and Aquatic Sciences

... 2,18 Calcium lactate is composed of two lactate (CH 3 CHOHCO 2 − ) anions and one calcium (Ca 2+ ) cation. Two crystal forms, namely, calcium lactate pentahydrate (Ca(CH 3 CHOHCOO) 2 ·5H 2 O) 19,20 and calcium lactate monohydrate (Ca(CH 3 CHOHCOO) 2 ·H 2 O), 21 were previously reported in the literature. Calcium lactates have been employed as an antidote for soluble fluoride ingestion, 22 for hypocalcemia, 23 for prevention of tetany, as an anti-tartar agent in some mouthwashes and toothpaste, as an antacid, 24 and as a calcium source for treating calcium deficiencies. ...

Characterization of Calcium Lactate Prepared from Butter Clam Saxidomus purpuratus Shell Powder

Korean Journal of Fisheries and Aquatic Sciences

... tuna fish (5.7±0.54%), and carp (4.88±0.21% db) (Lee et al., 2016;Shaviklo et al., 2017;Tian et al., 2017). The CPI had low lipid content due to the defatting process in CF. ...

Preparation and characterization of protein isolate from Yellowfin tuna Thunnus albacares roe by isoelectric solubilization/precipitation process

Fisheries and Aquatic Sciences

... OFR -(steam-dried concentrates, SDC) Lee et al. (2016) Kwon et al. (2022) . , tea bag 300 g OFR 6 80 C 20 min , ...

Chemical composition of protein concentrate prepared from Yellowfin tuna Thunnus albacares roe by cook-dried process

Fisheries and Aquatic Sciences

... 바지락 패각분말(shell powder, SP) 및 소성분말 (calcined powder, CP)의 제조 (littleneck clam, LC)SP CP Kim et al. (2015) . Lee et al. (2015) . 20 mL 1 g LCCLs , 2,000 g 15 , (10 mL) 1 N HCl 0.1 mL pH . ...

Characteristics and Preparation of Calcium Acetate from Butter Clam (Saxidomus purpuratus) Shell Powder by Response Surface Methodology

Journal of the Korean Society of Food Science and Nutrition

... . This anhydrous form could be prepared from the thermal decomposition of Ca(CH 3 COO) 2 ·H 2 O. Calcium acetate can be synthesized by the reaction between vinegar (or acetic acid, CH 3 COOH) and CaCO 3 , which is derived from different calcium sources of non-living things such as carbonate rocks, limestone, and marble [22]. In addition, it could also be synthesized by using some components of living things as the starting materials, such as eggshells [24], black snails [25], and littleneck clams [26]. Calcium acetate has been employed as an adsorbent to adsorb the greenhouse CO 2 gas [27], as an important controller to reduce the emissions of toxic gasses in the coal combustion process such as nitrogen oxide, sulfur dioxide, and other toxic gasses [28], and as an alternative deicer ...

Optimization of Calcium Acetate Preparation from Littleneck Clam (Ruditapes philippinarum) Shell Powder and Its Properties

Korean Journal of Food Science and Technology

... , , . (Heu et al., 2006;Kang et al., 2007;Kang et al., 2015;Kim et al., 2015;Lee et al., 2016b;Yoon et al., 2017). ( Lee et al., 2016a), (Heu et al., 2010;Lee et al., 2016b), Yoon et al., 2017) , (Lee et al., 2016a;Binsi et al., 2017;Yoon et al., 2018b), (Lee et al., 2016c), (Noh et al., 2013;Intarasirisawat et al., 2014) (Park et al., 2016;Binsi et al., 2017;Yoon et al., 2018b), (Heu et al., 2009;Intarasirisawat et al., 2014) . ...

Recovery and Fractionation of Serine Protease Inhibitors from Bastard Halibut Paralichthys olivaceus Roe

Korean Journal of Fisheries and Aquatic Sciences

... Calcined shell powder is generated through washing, drying, calcining, and sieving of raw waste seashells. Organic matter in waste shells is removed by calcination (Kim, Jung, Soo Jang, Lee, Park, Kim, & Heu, 2015). The temperature of calcination is critical. ...

Characteristics of the Shells and Calcined Powders from the Butter Clam Saxidomus purpuratus and Littleneck Clam Ruditapes philippinarum as a Natural Calcium Resource

Korean Journal of Fisheries and Aquatic Sciences

... A previous study analyzes endoprotease and exopeptidase fractions (Kim et al., 2008;Kim et al., 2012b), and their hydrolysis bitter-taste improvement (Kim et al., 2014a;Kim et al., 2014b). Additionally, the recovery, bitterness improvement, and enzyme characteristics of the aminopeptidase active-fraction have been investigated by the filtration method, considering its economic and industrial utilization (Kim et al., 2020). ...

Lowering the Bitterness of Enzymatic Hydrolysate Using Aminopeptidase-active Fractions from the Common Squid (Todarodes pacificus) Hepatopancreas

Korean Journal of Food Science and Technology