• Animal Bioscience
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• v.37 no.6
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• pp.1096-1109
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• 2024

Objective: This research aims to explore the nutritional and bioactive peptide properties of goat meat taken from various primal cuts, including the breast, shoulder, rib, loin, and leg, to produce these bioactive peptides during in vitro gastrointestinal (GI) digestion and absorption. Methods: The goat meat from various primal cuts was obtained from Boer goats with an average carcass weight of 30±2 kg. The meat was collected within 3 h after slaughter and was stored at -80℃ until analysis. A comprehensive assessment encompassed various aspects, including the chemical composition, cooking properties, in vitro GI digestion, bioactive characteristics, and the bioavailability of the resulting peptides. Results: The findings indicate that the loin muscles contain the highest protein and essential amino acid composition. When the meats were cooked at 70℃ for 30 min, they exhibited distinct protein compositions and quantities in the sodium dodecyl sulfate-polyacrylamide gel electrophoresis profile, suggesting they served as different protein substrates during GI digestion. Subsequent in vitro simulated GI digestion revealed that the cooked shoulder and loin underwent the most significant hydrolysis during the intestinal phase, resulting in the strongest angiotensin-converting enzyme (ACE) and dipeptidyl peptidase-IV (DPP-IV) inhibition. Following in vitro GI peptide absorption using a Caco-2 cell monolayer, the GI peptide derived from the cooked loin demonstrated greater bioavailability and a higher degree of ACE and DPP-IV inhibition than the shoulder peptide. Conclusion: This study highlights the potential of goat meat, particularly cooked loin, as a functional meat source for protein, essential amino acids, and bioactive peptides during GI digestion and absorption. These peptides promise to play a role in preventing and treating metabolic diseases due to their dual inhibitory effects on ACE and DPP-IV.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.50 no.5
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• pp.506-519
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• 2017

This study evaluated the protein recovery and functional properties and biological activity of boiled and steamed process water (BPW and SPW, respectively) generated from the preparation of concentrated roe of bastard halibut (BH; Paralichthys olivaceus), skipjack tuna (ST; Katsuwonus pelamis), and yellowfin tuna (YT; Thunnus albacares) using the cook-dry process. The protein loss from the water extracts (EXT) of 100 g of roe protein was 15.05-19.71% and was significantly (P<0.05) higher than that of BPW (5.47-10.34%) and SPW (3.88-8.18%). The foam capacity of BPW (166-203%) and SPW (15-194%) was better than that of EXT. The emulsifying activity index of the original samples was lower than those ($15.40-107.86m^2/g$) of diluted protein samples. The 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity and the reducing power of BPW and SPW were stronger than those of EXT. The 2,2'-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid ($ABTS^+$) radical scavenging activity of EXT (0.028-0.045mg/mL) was significantly higher those of BPW and SPW. The angiotensin I-converting enzyme (ACE) inhibitory activity of SPW was the highest for BH (1.04 mg/mL), followed by YT and ST. The predominant amino acids in SPW were Glu, Ala, Leu, and His. These results demonstrate that processing water containing diluted organic components, including protein, can be consumed directly by humans as a functional reinforcing material after appropriate concentration processes.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.54 no.6
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• pp.849-860
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• 2021

This study investigated the preparation of seasoned anchovy sauce (SAS) and its functional characteristics by using aminopeptidase active fractions (AAFs) derived from squid Todarodes pacificus hepatopancreas as a bitter taste improver. As the base of the SAS, a hydrolysate (AAAH) prepared by continuously treating raw anchovies with Alcalase-AAF was used. The high-performance liquid chromatography profile of the AAAH suggested that the action of AAFs decreased the hydrophobicity of the N-terminal peptide related to bitterness in the protein hydrolysates. SAS was prepared by blending with the AAAH and other ingredients. The crude protein (2.5%), carbohydrates (18.4%), amino acid-nitrogen (1,325.1 mg/100 mL), and total free and released amino acids (FRAAs, 700.2 mg/100 mL) of SAS were higher than those of commercial anchovy sauce (CAS). Sensory evaluation revealed that SAS was superior to CAS in flavor, color, and taste. The main FRAAs of SAS were glycine (16.8%), alanine (13.2%), glutamic acid (7.8%), and leucine (7.3%). The amino acids that had a major influence on the taste according to the SAS taste values were glutamic acid, aspartic acid, alanine, and histidine. The angiotensin-converting enzyme inhibitory (2.21 mg/mL) and antioxidant activities (3.58 mg/mL) of SAS were superior to those of CAS.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.56 no.1
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• pp.7-20
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• 2023

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 ㎍/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.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.50 no.6
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• pp.694-706
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• 2017

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 precipitation process. The IPWs contained 2.7-5.4 mg/mL of protein, and the protein losses were 8-21% (P<0.05). The form capacity of IPW-3 for BH and ST, and IPW-4 for YT was 155, 194, and 164%, respectively. The emulsifying activity index ($27-43m^2/g$) of the YT-IPWs was the strongest, followed by ST ($7-29m^2/g$) and BH ($10-19m^2/g$). The 2,2-diphenyl-1-picrylhydrazyl scavenging activities of IPW-1 and -3 were higher than those of IPW-2 and -4. The 2,2'-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid scavenging activity ($IC_{50}$, mg/mL) of IPW-2 and -4 was 0.03 mg/mL for BH, 0.04-0.08 mg/mL for ST, and 0.04-0.07 mg/mL for YT. BH IPW-3 had the strongest reducing power (0.41 mg/mL) and superoxide dismutase-like activity (1.68 mg/mL). The angiotensin-I converting enzyme inhibitory activity of IPW-3 was the highest for ST (1.52 mg/mL), followed by BH and YT. The common predominant amino acids in the IPWs were the essential amino acids Val, Leu, Lys, and Arg and the non-essential amino acids Ser, Glu, and Ala.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.46 no.1
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• pp.37-45
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• 2013

This study was conducted to improve the yield of extracts from Alaska pollock Theragra chalcogramma head and sea tangle Laminaria japonica byproducts using various commercial enzymes, such as Alcalase, Flavourzyme, Neutrase (NH), and Protamex. Among the enzymatic hydrolysates, the yield was highest in hydrolysate incubated with NH for 4 h. NH-treated hydrolysates (NHH) also improved functional properties, such as angiotensin-I converting enzyme (ACE) inhibitory activity and 2,2-diphenyl-1-picryldrazyl (DPPH) radical scavenging activity, as compared to extracts from Alaska pollock head and sea tangle byproducts. Total free amino acid and taste values of NHH were 379.7 mg/100 mL and 24.03, respectively, after digestion for 4 h. These values are 2.2-fold and 1.9-fold higher compared with those of water soluble fractions extracted from Alaska pollock head and non-forming sea tangle, respectively. According to the taste value results, the major taste-active compounds among free amino acids of NHH were glutamic acid and aspartic acid. These results suggest that NHH can be used as an ingredient for natural seasoning preparation.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.53 no.3
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• pp.403-416
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• 2020

The purpose of this study was to evaluate the food functional properties and in vitro bioactivity of vacuum freeze-dried 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 ㎡/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.

• Food Science and Preservation
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• v.13 no.5
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• pp.596-602
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• 2006

This study was conducted to investigate the changes of major components and bioactivities of tea produce. The tea produce were made by various methods, with different degree of fermentation during manufacturing process. Except green tea, degrees of fermentation in Wizo Tea, Ilsoae Tea, and Hwang Tea were $5{\sim}10%,\;50{\sim}60%$ and $70{\sim}80%$ respectively. The result are as follows : The general component(moisture, crude ash, crude lipid, and crude protein) and the content of total polyphenol in tea products were not shown significant difference during the fermentation process. The content of caffeine in tea extracts decreased sharply as degree of fermentation of tea. In comparison of hunter values in tea extract, lightness was decreased as fermentation redness (a) was all (-), and yellowness(b) was increased sharpy with degree of fermentation. Radical scavenging activity using DPPH of tow kinds of tea was potent and decreased generally with degree of feimentation. Inhibitory effects of tea extracts against angiotensin I converting enzyme were also potent.

• Food Science and Preservation
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• v.14 no.4
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• pp.425-430
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• 2007

To investigate the potential therapeutic value of a plant extract against amyloid ${\beta}-peptide-induced$ cell damage, we first screened extracts of 250 herbs, and finally selected a water extract of Spinacia oleracea for further study. This extractshowed the potential to inhibit the reactions of oxidants. We measured the angiotensin-converting-enzyme (ACE) inhibitory activity of the extract, and assessed the ability of the extract to protect neuronal cells from chemical-induced cell death. SH-SY5Y neuroblastoma cells were used in this assay. The extract exerted protective effects on $H_2O_2-induced$ cell death, when $H_2O_2$ was used at 100 M, 200 M, and 500 M (protection of 87%, 73%, and 58%, respectively). When 50 M of amyloid ${\beta}-peptide$ was added to the test cells, however, the extract had no protective effect on cell death. The extract inhibited ACE activity in a dose-dependent manner, and exhibited potent protection against the deleterious effects of $H_2O_2$. In sum, these results suggest that a water extract of Spinacia oleracea has the potential to afford protection against chemical-induced neuronal cell death, and the extract may be useful in the treatment of neurodegenerative diseases. The precise molecular mechanism of neuroprotection is under investigation.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.57 no.1
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• pp.1-14
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• 2024

We investigated the functional properties and in vitro bioactivity of protein isolates (RPIs) recovered from olive flounder 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 activity 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 ㎍/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.