• Title/Summary/Keyword: fish protein hydrolysate

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Isolation and Charaterization of Bioactive Peptides from Hwangtae (yellowish dried Alaska pollack) Protein Hydrolysate

  • Cho, San-Soon;Lee, Hyo-Ku;Yu, Chang-Yeon;Kim, Myong-Jo;Seong, Eun-Soo;Ghimire, Bimal Kumar;Son, Eun-Hwa;Choung, Myoung-Gun;Lim, Jung-Dae
    • Preventive Nutrition and Food Science
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    • v.13 no.3
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    • pp.196-203
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    • 2008
  • Hwangtae, dried Alaska pollack, is a major storage product in the fish processing industry. Hwangtae is prepared by removing the internal organs and drying outdoors during the cold witner months by allowing it to thaw during the daytime and re-freeze at night under sub-zero ($-10^{\circ}C$) conditions and gradually dry from December until the next April for around 5 months from Myungtae. In this study, ground Hwangtae was hydrolyzed using two proteolytic enzymes (pepsin and alcalase) which produced five soluble active peptides from Hwangtae (yellowish dried Pollack, Theragra chalcogramma) protein. Two different peptides with strong antioxidative activity were isolated from the hydrolysate using consecutive chromatographic methods of Sephadex G-25 gel, ion-exchange chromatography on a Sepharose-Sephadex C-25 gel, and high-performance liquid chromatography. The isolated peptides, APO1 and APO2, were composed of 16 and 13 amino acid residues, respectively. Both peptides contained a Gly residue at the C-terminus and the repeating motif Gly-Pro-Hyp. The peptide with a molecular weight less than 1,000 Daltons (APACE) obtained from enzymatic hydrolysates of Hwangtae exhibited the highest ACE inhibitory activity. The APACE peptides was composed of 4 amino acid residues (Gly-Leu-Leu-Pro). These results suggest that Hwangtae hydrolysates could be a good source of peptides with ACE inhibitory activity. Biochemical analysis indicated that two 70 kDa peptides (APG1 and APG2) isolated from the hydrolysate had gelatinoytic activity, which was shown to be a calcium dependent protease type as showed by gelatin SDS PAGE.

Salt reduction in foods using protein hydrolysates (단백질 가수분해물을 이용한 식품 내 소금 저감화)

  • Shin, Jung-Kue
    • Food Science and Industry
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    • v.51 no.4
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    • pp.313-324
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    • 2018
  • As excessive intake of salt is regarded as a reason for health problems, the tendency of people to attempt to reduce intake of salt in their everyday lives is on the rise. In Korea, where many people have a higher intake of salt compared to those in other countries, there have been diverse efforts to improve on this eating habit. Protein hydrolysates are chemically, physically hydrolyzed protein that have been widely utilized as a material for not only regular food but health functional food due to have diverse biological effects such as anti-oxidation, anti-inflammation, prevention of diabetes, and regulation of blood pressure. Various amino acids such as glutamic acid, arginine and arginine dipeptides, which exist in the components of protein hydrolysates, have also been recently recognized as being helpful in decreasing the use of salt in foods as they can greatly enhance salty taste when used concurrently with salt due to having both salty and palatable flavors. In the case of protein hydrolysates that decompose soy protein or fish protein such as anchovy, they could reduce consumption of salt by as much as 50% without affecting people's food preferences when applied to food as they boost salty taste by approximately 10% to 70%. Although there are only a few studies on protein hydrolysates as a salty taste enhancer or salt substitute, the results of several studies are indicative of the potential of protein hydrolysates as a salty taste enhancing ingredient.

A study on the Rapid Processing of Hydrolyzed Anchovy Paste and Its Quality Stability (효소분해법에 의한 페이스트형 속성 멸치젓의 제조 및 품질에 관한 연구)

  • HAN Bong-Ho;KIM Sang-Ho;CHO Hyun-Duk;CHO Man-Gi;BAE Tae-Jin
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.30 no.1
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    • pp.79-87
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    • 1997
  • A study on the processing method of anchovy hydrolysate paste (AHP) was carried out to improve the sensory quality of salted and fermented fish. Homogenized whole anchovy was hydrolyzed using commercial pretenses, Complex enzyme-2000 (CE, Pacific Chem. Co.) and Alcalase (AL, Novo), in a cylindrical vessel with 4 baffle plates and 6-bladed turbine impeller. Optimal pH, temperature, and enzyme concentration for the hydrolysis with CE and AL were $7.0,\;52^{\circ}C,\;7\%$, and $8.0,\;60^{\circ}C,\;6\%$, respectively. The rational amount of water for homogenization, agitation speed, and hydrolyzing time were $100\%\;(w/w)$, 100 rpm, and 210 min, respectively. To make the hydrolysate to paste type, it was effective to mix the additives, such as starch, soybean protein, agar, and carrageenan gum to the hydrolysate 5 min before the end of boiling at $100^{\circ}C$ for 30 min. Minimal NaCl concentration for long-term preservation was $15\%$, and this could be reduced to $12\%$ by adding $5\%$ of KCl. yield of the AHP based on the total nitrogen content was $94.6\~97.0\%,\;and\;86.0\~89.2\%$, of the nitrogen was amino nitrogen. Salinity, pH and histamine content of the AHP prepared with $12\%$ NaCl and $5\%$ KCl were $9.3\~9.9\%,\;6.1\~6.2$, and below 13 mg/100 g, respectively. The AHP was stable at $26{\pm}3^{\circ}C$ for 60 days on bacterial growth, and addition of $0.05\%$ of rosemary (Herbalox) extract was effective to inhibit the lipid oxidation of the AHP during storage.

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Partial Purification of Antioxidative Peptides from Gelatin Hydrolysates of Alaska Pollock Surimi Refiner Discharge

  • Heu, Min-Soo;Park, Chan-Ho;Kim, Hyung-Jun;Park, Jae-W.;Kim, Jin-Soo
    • Fisheries and Aquatic Sciences
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    • v.12 no.4
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    • pp.249-257
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    • 2009
  • This study is conducted to partially purify an antioxidative peptide in a two-step gelatin hydrolysate from Alaska pollock surimi refiner discharge, which was obtained by sequential treatment with Pronase E and Flavourzyme. The two-step gelatin hydrolysate was fractionated using chromatographic methods. Based on the same protein concentration of each fraction, the antioxidative activities (85.1-95.4%) of positive fractions fractionated by ion-exchange chromatography were higher than those (27.2-87.8%) from gel filtration. Then, further purification of the positive fractions was performed. Among them, the partially purified A1C1L2G1 and A1C1L2G2 fractions showed 96.2% and 85.1% inhibition, respectively, of linoleic acid peroxidation. The A1C1L2G1 fraction was composed of 15 kinds of amino acids and the predominant amino acids were proline, glycine and alanine. The results obtained in this study suggested that the fraction partially purified through chromatographic methods from the two-step gelatin hydrolysate of Alaska pollock surimi refiner discharge could be useful as a supplementary source for improving health functionality.

Qualify and Stability of Fish Sauce during Storage (어장유의 품질과 저장안정성)

  • KIM Byeong-Sam;PARK Sang-Min;CHOI Soo-Il;KIM Chang-Yang;HAN Bong-Ho
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.19 no.1
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    • pp.20-26
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    • 1986
  • Very little information is available in the literature on storage of fish sauce. Therefore, microbiological and chemical chracteristics during storage and quality of fish sauce were investigated and discussed to present data about the optimum storage condition. The chopped sardine meat was mixed with equal amount of water and $9\%$(w/w) of $75\%$ vital wheat gluten and then hydrolyzed by addition of commercial proteolytic enzymes such as bromelain, papaya protease, ficin and a enzyme mixture (Pacific Chem. Co.) for 4 hours at $52.5^{\circ}C$. The reaction mixture was heated for 30 min at $100^{\circ}C$ for enzyme inactivation, pasteurization and color development and then centrifuged for 20 min at 4,000 rpm. Table salt and benzoic acid were added for bacteriostatic effect and stored for 80 days at $15{\pm}1^{\circ}C$ and $30{\pm}1^{\circ}C$. The results were summarized as follows: 1. The amount of amino-nitrogen and pH of fish sauce were almost unchanged during storage. 2. Mininum concentration of salt for bacteriostatic activity was $9\%$(w/w) regardless of addition of benzoic acid. 3. the yields of amino-nitrogen were $63.1\%$ for the hydrolysate prepared without enzyme, $79.7\%$ for that with bromelain, $69.9\%$ with ficin, $74.3\%$ with papaya pretense, and $78.1\%$ with enzyme mixture, respectively. 4. The contents of amino-nitrogen were $4510.0mg\%$ on the dry basis for the product prepared by autolysis, $5483.2mg\%$ for that prepared with bromelain, $5305.7mg\%$ with ficin, $4994.1mg\%$ with papaya protease and $5582.3mg\%$ with the enzyme mixture, respectively. 5. The contents of crude protein were $51.35\%$ on the dry basis for the product prepared by autolysis and 55 to $59\%$ for prepared with commercial enzymes. 6. The hydrolysate prepared with the enzyme mixture revealed a little stronger meaty taste than any other products. 7. The level of crude protein in residues was still high ($69.5{\sim}77.2\%$ on the dry basis) and might be originated from the added vital wheat gluten.

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Synthesis and Functional Properties of Plastein from the Enzymatic Hydrolysates of Filefish Protein 2. General Properties and IR Spectrum of Plasteins (말쥐치육 단백질의 효소적 가수분해물을 이용한 Plastein의 합성 및 그 물성 2. Plastein의 일반적 성상과 IR Spectrum)

  • KIM Se-Kwon;LEE Eung-Ho
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.20 no.5
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    • pp.431-440
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    • 1987
  • In order to develop a new type of food source for the effective utilization of fish protein, plastein reaction was applied to improve the functional properties of filefish protein. Plasteins were synthesized from a peptic filefish protein hydrolysate by papain, pepsin, $\alpha-chymotrypsin$ and protease(from Streptomyces griceus) under the optimum conditions of previous paper). Also, L-glutamic acid diethylester and L-leucine ethylester were incorporated into plastein during the plastein reaction by papain. And, General composition, yield, molecular weight, amino acid composition, color and IR spectrum of plasteins were measured. The protein, ash and lipid content of the plasteins were $72\~78\%,\;7.4\~11.8\%\;and\;0.3\~0.9\%$ respectively. The yield of plasteins were papain $55.0\%,\;pepsin\;47.6\%,\;\alpha-chymotrypsin\;38.3\%,\;protease\;23.6\%$, glutamic acid-incorporated plastein (Glu-Plastein) $35.0\%$, and leucine-incorporated plastein (Leu-plastein) $45.7\%$. The glutamic acid and leucine content in Glu-plastein and Leu-plastein were $38.7\%,\;41,7\%$, respectively, while the contents in the peptic filefish protein hydrolysate were $16.01\%\;and\;8.16\%$, respectively. The amino acid compositions were similar to that of the original filefish muscle protein. The major molecular weights of the peptic hydrolysate estimated by gel filteration were 2,000 and 310, and those of plasteihs were 21,000 and 4,900 for papain, 24,000 for pepsin, 18,500 for $\alpha-chymotrypsin$ 6,700 for protease, 24,000 for Glu-plastein and 17,000 for Leu-plastein. The structural changes in freeze-dried filefish meat, the FPC and hydrolysate were not observed on the IR spectrum. But plasteins showed amide I band in $1,600\~l,700cm^{-1}$ range and resulted in a strong band in $800\~850\;cm^{-1},\;700\~750\;cm^{-1}\;and\;650\~700\;cm^{-1}$. The amide I band of Glu-plastein was wider than those of other plasteins and had also a small band at $1,440\;cm^{-1}$.

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Studies on the Improvements of Functional Properties of Sardine Protein by Plastein Reaction -1. Synthetic Conditions of Plasteins from the Enzymatic Hydrolysate of Sardine Protein- (Plastein반응을 이용한 정어리 단백질의 기능성 개선에 관한 연구 -1. 정어리 분말단백질의 pepsin가수분해물을 이용한 plastein의 합성조건-)

  • Kim, Se-Kwon;Kwak, Dong-Chae;Cho, Duck-Jae
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.17 no.3
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    • pp.233-241
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    • 1988
  • In order to develop a new type of food source for the effective utilization of fish protein, plastein reaction was applied to improve the functional properties of sardine protein. Conditions necessary for optimal plastein productivity from sardine protein using pepsin, ${\alpha}-chymotrypsin$, protease(from Aspergillus saitoi) and papain were established. Sardine protein concentrate was hydrolyzed with pepsin yielding an approximate degree of hydrolysis of 78.4%. Enzyme induced plastein was optimized at : pH 4 for pepsin, pH 7 for ${\alpha}-chymotrypsin$, pH 5 for pretense and pH 6 for papain : Substrate concentrate 40% for pepsin and ${\alpha}-chymotrypsin$, 50% for pretense and papain : the time of incubation, 24hr : enzyme/substrate ratio, 1 : 100(w/v) incubation temperature, $50^{\circ}C$.

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Improvement on the Functional Properties of Gomtang-like Product from Salmon Frame Using Commercial Enzymes (상업적 효소를 이용한 연어 Frame 유래 곰탕 유사 제품의 기능성 개선)

  • Heu, Min-Soo;Park, Shin-Ho;Kim, Hye-Suk;Jee, Seung-Joon;Lee, Jae-Hyoung;Kim, Hyung-Jun;Han, Byung-Wook;Kim, Jin-Soo
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.36 no.12
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    • pp.1596-1603
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    • 2007
  • This study was conducted to improve functional properties of salmon frame extracts using various commercial enzymes (Alkalase 2.4 L FG, Flavourzyme 500 MG, Neutrase 0.8 L and Protamex 1.5 MG). The ACE (angiotensin I converting enzyme) inhibitory activity was the highest ($IC_{50}=0.67mg/mL$) in the product incubated with Neutrase for 4 hrs (N4-treated hydrolysates) among the various extracts incubated with commercial enzymes for different times. However, antioxidant activities of all salmon frame extracts were less than 15%. There were no significant differences in the proximate composition and sensory evaluation of the fish odor and taste. However, N4-treated hydrolysate was improved in the extractive-nitrogen content and transmission compared to the other enzymatic hydrolysates. When compared to commercial Gomtang products, N4-treated hydrolysate was also high in protein, extractive-nitrogen, total amino acid, and calcium contents, while low in taste sensory score. There were no differences in transmission and sensory score on the fish odor between N4-treated hydrolysates and commercial Gomtang.

Antioxidant Activity of Pepsin Hydrolysate Derived from Edible Hippocampus abdominalis in vitro and in Zebrafish Models (빅벨리 해마(Hippocampus abdominalis) 유래 펩신 가수분해물의 In vitro와 In vivo에서의 항산화 효능)

  • Kim, Hyun-Soo;Shin, Byeung-Ok;Kim, Seo-Young;Wang, Lei;Lee, WonWoo;Kim, Yoon Taek;Rho, Sum;Cho, Moonjae;Jeon, You-Jin
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.49 no.4
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    • pp.445-453
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    • 2016
  • Seahorse Hippocampus abdominalis a marine teleost fish, has long been used as one of the essential materials in traditional Chinese medicine. However, the uses of seahorse have been limited due to its high cost, despite its beneficial biological activities. Seahorse has not been widely explored for its biofunctional properties and active components. In the present study, the enzymatic hydrolysates of seahorse were prepared by using two digestive enzymes (trypsin and pepsin) and five food grade enzymes (neutrase, protamex, alcalase, kojizyme, and flavourzyme). The enzymatic hydrolysates indicated higher hydrolysis yields than its water extract. Among them, the distilled water-pepsin hydrolysate (DP) which was obtained by distilled water extraction followed by pepsin hydrolysis, showed the highest yield and protein content as well as the highest alkyl radical scavenging activity. Also, it provided protective effects against oxidative stress induced by AAPH in vero cell and zebrafish. Further fractionation based on the molecular weight was carried out to identify it’s active components, and < 5 kDa (less than 5 kDa) molecular weight fraction was confirmed to have the highest antioxidant activity. In conclusion, this study suggests that DP of seahorse has antioxidant properties, and might be a novel and useful material from the marine origin for healthy functional foods and cosmetics.

Cryoprotective Effect and Mechanism of Corn Starch Enzyme Hydrolysates on Fish Protein 1. Cryoprotective Effect of Corn Starch Enzyme Hydrolysates on Fish Protein (전분가수분해물의 어육단백질 동결변성 방지효과 및 작용기구 1. 옥수수전분가수분해물의 어육단백질에 대한 동결변성 방지효과)

  • LEE Kang-Ho;JUNG Byung-Chun;HONG Byung-Il
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.31 no.6
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    • pp.823-828
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    • 1998
  • The objective of this study is to investigate cryoprotective effects of corn starch enzyme hydrolysates of nonsweet and low-calories on denaturation of frozen fish protein. The cryoprotective effects of were examined in Alaska pollack actomyosin solution by changes in SDS-PAGE pattern, solubility, and $Ca^{2+}$-ATPase activity. When samples stored for 0 and 30 days were compared on SDS-PAGE patterns, severe changes in all bands were shown on the control sample regardless of storage temperature, especially in myosin heavy chain (MHC). Not much difference no appeared the electrophoretic pattern in case of the samples containing sucrose at any storage temperature during 30 days of storage. The cryoprotective effect of the hydrolysates were markedly dependant on storage temperature and no MHC band was found in the samples stored at $-5^{\circ}C$. The SDS-PAGE patterns of sample stored at $-20^{\circ}C$, however, completely maintained after 30 days or storage. When the samples were stored at $-5^{\circ}C$, the solubility of the sample containing sucrose was retained at $90\%$ after 30 days of storage, whereas dramatically decreased in other samples. The samples including sucrose, D.E. 10, 15, and 20 revealed $90\%$ in solubility when stored at $-20^{\circ}C$. The tendency of remaining $Ca^{2+}$-ATPase activity was almost shown the same as that of solubility.

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