• Journal of the Korean Society of Food Science and Nutrition
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• v.44 no.11
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• pp.1645-1652
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• 2015

We investigated the anti-wrinkle efficacy of hydrolysate from oyster protein by Protamex and Neutrase for the purpose of finding materials to assist skin health originating from marine organisms. There were about 7.9% free amino acids in the oyster hydrolysate, and contents of urea, taurine, alanine, and glycine were high. Oyster hydrolysate also showed collagenase inhibitory activity and was not toxic to CCD986sk human fibroblast cells. Yield of the fractions according to the molecular weight of oyster hydrolysate was 40% for less than 1,000 Da and 60.4% for less than 5,000 Da, respectively. Antioxidative effect, procollagen production, and matrix metalloproteinase-1 inhibitory activity were highest in 1,000~3,000 Da fractions. We observed that oyster hydrolysate and its less than 5,000 Da fraction are potential functional compounds for skin health and for improving wrinkles.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.33 no.3
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• pp.198-204
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• 2000

In order to utilize by-products which would normally be discarded in marine processing plants, cod teiset protein was hydrolyzed and antioxidative actiTity of the hydrolysate was investigated. AntioxidatiTe peptide was isolated using ultrafiltration membrane, ion-exchange chromatography on a SP-Sephadex C-25 column, gel filtration on a Sephadex G-15 column, high performance liquid chromatography on an ODS column, and capillary electrophoresis chromatography. Antioxidative activities of the cod teiset hydrolysate were compared with ${\alpha}-tocopherol$, one of the commercial antioxidant. The hydrolysate passed through a membrane with molecular weight cut-off (MWCO) 1 kDa was shown the strongest antioxidative activity, and the activity was higher $10{\%}$ as compared with ${\alpha}-tocopherol$. In addition, the peptide isolated by ion-exchange chromatography, gel filtration, and HPLC, respectively, was higher $53{\%}$ as compared with ${\alpha}-tocopherol$, and the amino acid sequence was Ser-Asn-Pro-Glu-Trp-Ser-Trp-Asn.

• Applied Biological Chemistry
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• v.42 no.1
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• pp.49-57
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• 1999

Enzymatic hydrolysis with tuna pyloric caeca crude enzyme(TPCCE) was performed to recover a protein hydrolysate from hoki frame, fish processing by-product. Optimum hydrolytic conditions were pH 10.0, temperature $50^{\circ}C$, and incubation time 12 hrs, and then the degree of hydrolysis was about 60%. The yield of the hydrolysate from hoki frame by enzymatic hydrolysis was approximately 77% on a dry weight basis. The prepared protein hydrolysates were also fractionated through a series of 30, 10, 5 and 1 kDa molecular weight cut-off (MWCO) membranes in order to investigate the effect of their functionalities according to the difference of their molecular size. As the result of studying functionalities of the hydrolysates, 1 K hydrolysate showed the highest solubility over all pHs, and 30 and 10 K hydrolysate showed more excellent emulsifying property and whippability than the other hydrolysates.

• 한국생물공학회:학술대회논문집
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• 2003.10a
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• pp.541-541
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• 2003

• Applied Biological Chemistry
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• v.42 no.2
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• pp.128-133
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• 1999

To enhance functional properties of 4 different hoki frame protein hydrolysates (30K, 10K, 5K and 1K hydrolysate) fractionated through a series of 30, 10, 5 and 1 kDa molecular weight cut-off membranes in order to decrease pore size, all hydrolysates were phosphorylated with sodium trimetaphosphate and altered phosphorylated 30K, 10K, 5K and 1K (P-30K, P-10K, P-5K and P-1K), respectively. The covalent attachment of anionic phosphate groups to polypeptide chains improved the functional properties, such as solubility, emulsifying properties and foaming properties, of hoki frame protein hydrolysates. Especially, P-30K hydrolysate with the highest molecular weight fraction possessed the most excellent functional properties among 4 different phosphorylated hydrolysates.

• Food Science and Preservation
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• v.24 no.4
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• pp.550-558
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• 2017

The purpose of current study is to investigate the beneficial effect of enzyme (Alcalase) hydrolysates of silk protein in rat. Alcalase-treated silk protein hydrolysate (ATSH) itself did not show any cytotoxicity on the hepatic tissues and blood biochemistry, similar to the normal condition. ATSH played a protective role in tert-butyl hydroperoxide (t-BHP)-induced hepatotoxicity and liver damage. The values of AST (aspartate aminotransferase) and ALT (alanine aminotransferase), which are the indicators of the liver function, were effectively alleviated with the ATSH treatment in a dose dependent manner. The level of Lactate dehydrogenase (LDH) and Malondialdehyde (MDA), which were increased with t-BHP treatment, were significantly reduced by ATSH. High dose of ATSH (2 g/kg) reduced the t-BHP-induced LDH release by 48%. Antioxidant and antioxidant enzymes in liver cells were significantly increased by ATSH treatment in their level and activities. ATSH (2 g/kg) increased glutathione (GSH), an intracelluar antioxidant, by 2.5-fold compared with the t-BHP treated group. The activities of glutathione-s-transferase (GST), superoxide dismutase (SOD), and catalase were also elevated by 38%, 60%, and 45%, respectively, with ATSH (2 g/kg) treatment. The antioxidative effect of ATSH was recapitulated to the protection from t-BHP induced liver damages in hematoxylin and eosin (H&E) staining. Thus, ATSH might be used as a hepatoprotective agent.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.35 no.1
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• pp.97-104
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• 2002

Protein hydrolysate was prepared as a natural flavor stock from the sharp toothed eel (Muraenesox cinereus) mince using com-mercially available proteolytic enzymes, Alcalase, Neutrase, Protamex, and Flavourzyme. A 6 hr hydrolysis of mince, to which water of the equal weight of the mince was added, with $2\%$ (w/w, protein weight) Elavourzyme at $50^{\circ}$ yielded a hydrolysate of the highest acceptability. Removing the access lipid in liquified hydrolysate (not dehydrated) after enzyme hydrolysis, five times repetitive extraction using n-hexane (liquified hydrolysate : n-hexane=4 : 1, v/v) was effective, resulting in less than $1\%$ lipid content of the dehydrated-hydrolysate. The amino acid composition of the hydrolysate (prepared with Flavourzyme) was similar to that of the starting material. Hydrolysis led to an increase in concentration of not only total free amino acid but also free amino acid such as serine, glutamic acid, alanine, and methionine responsible for umami taste, especially up to about 40 times for methionine. Major free amino acids in amount were leucine, phenylalanine, valine, alanine, and isoleucine and they comprised about half of the total free amino acids, Moisture adsorption, fat adsorption, emulsifying capacity, and foaming capacity of the hydrolysate were 870.1 $\pm$ $7.9\%$, 352.0$\pm$ $5.3\%$, 50.3 $\pm$ $1.2\%$, and $87.5\pm$ $2.5\%$, respectively, and solubility was 83$\~$$84\%$ at acid pH range of 2$\~$4.

• Journal of the Korean Society of Food Science and Nutrition
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• v.42 no.12
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• pp.1940-1948
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• 2013

This study is conducted to investigate the antioxidative effect of oyster hydrolysates in the serum and liver of SD-rats through the determination of lipid content, production of free radicals and antioxidant enzyme activities. Two different hydrolysates, Protamex-treated and Neutrase-treated hydrolysate with the cross-linking of protein by transglutaminase (TGPN group) and without (PN group), were fed for 6 weeks. TGPN hydrolysate in serum and liver significantly decreased the total cholesterol in the range of 26.1% to 28.9%, and triglyceride in the liver of up to 6.3%. Superoxide radical in the serum and lipid peroxide radical in the liver were significantly decreased in SD-rats fed 200 mg TGPN hydrolysate. Superoxide dismutase activity was significantly decreased in the liver of SD-rats. These results indicate that TGPN hydrolysate could scavenge the superoxide and hydroxyl radicals, and reduce the superoxide dismutase and catalase activities. The TGPN is also protected the oxidation of protein by the free radicals.

• Fisheries and Aquatic Sciences
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• v.26 no.6
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• pp.367-379
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• 2023

The rapid expansion of shrimp production requires a huge amount of protein sources from soybeans and wild-caught fishmeal; both are becoming a shortage. Meanwhile, catfish production and processing is a giant industry in Vietnam, which produce hundred thousand tonnes of protein- and lipid-rich by-products, annually. Using catfish by-products to gradually replace the traditional protein sources in shrimp aquaculture may bring triple benefits: 1) reducing pressure on wild fish exploitation for fishmeal, 2) reducing the environmental impacts of catfish by-products, and 3) increasing the value and sustainability of aquaculture production. In this study, we used catfish by-products to produce fish protein hydrolysate (FPH) and nano-hydroxyapatite (HA) as additives in feed for Pacific white shrimp (Litopenaeus vannamei). The supplement mixture of FPH and HA was added into the commercial diet (Charoen Pokphand Group [CP], 38% protein, and 6.5% lipid) to reach 38%, 38.5%, 40%, 43%, and 44% of the crude protein content. The survival and growth of shrimps were weekly assessed to day 55. The results showed that the shrimp growth was highest at 43% crude protein content in the feed as indicated by an increase of 124% and 112% in shrimp weight and length, respectively, compared to the commercial reference diet. No negative effects of adding the mixture of FPH and HA on the water quality were observed. Vibrio density was lower than 6.5 × 10³ CFU/mL, which is the lowest Vibrio density negatively affecting the shrimp growth and development. These findings indicate that the mixture of FPH and HA are promising additive components in feed for post-larval shrimp L. vannamei diets.

• Korean Journal of Food Science and Technology
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• v.31 no.5
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• pp.1363-1370
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• 1999

This study was performed to investigate the average molecular weight range of chitosan hydrolysates showing maximum effect in macrophage activation. Nitrite production by continuous macrophage cell line J774A.1 was the highest at $10\;{\mu}g/ml$ concentration of intact chitosan. Hydrogen peroxide production by J774A.1 showed the high value of $894\;{\mu}M/mg$ macrophage protein at $1,000\;{\mu}g/ml$ concentration of chitosan hydrolysate fraction 5 and $1,044\;{\mu}M/mg$ macrophage protein at $100\;{\mu}g/ml$ concentration of the fraction 6. Chitsan hydrolysate fraction 4, fraction 6 and intact chitosan enhanced $IL-1{\alpha}$ production, while the others did not. The production of tumor necrosis factor showed the high value at $1,000\;{\mu}g/ml$ concentration of chitosan hydrolysate fraction 4, $100\;{\mu}g/ml$ concentration of the fraction 5 and fraction 6, and $10\;{\mu}g/ml$ concentration of intact chitosan. In conclusion, fractions 4, 5 and 6 of the chitosan hydrolysatets with average molecular weight of $24,000{\sim}64,000$ calculated by HPLC analysis are the most effective in macrophage activation tested in this study.