말쥐치육의 사후경과에 따른 단백질조성의 변화

변재형,남택정 한국수산학회 1981 한국수산과학회지 Vol.14 No.1

Protein compositions of filefish (Navodon modestus) skeletal muscle and their changes in postmortem with reference to freshness kept at 0�� were investigated. The muscle protein was approximately composed of 31% sarcoplasmic, 55% myofibrillar, 10% residual intracellular, and 4% stroma protein. The sarcoplasmic and myofibrillar protein decreased while the residual intracellular protein increased with the decline of freshness during post-mortem lapse. In the analysis of electrophoretograms and its densitograms, the myofibrillar protein resembled to other fishes in protein composition: 70% actin and myosin, 20% regulatory proteins, and 10% unknown proteins. And most of the residual intracellular protein was estimated as myofibrillar protein. Troponin T, troponin C and myosin light chain 2 of the myofibrillar protein constituents were decreased during storage. Amino acid composition of the protein from the at-death muscle was similar to those of other fishes except that tryptophan and whereas leucine, isoleucine and phenylalanine were slightly increased in the protein from the muscle lapsed of 18 days. In free amino acid composition, alanine, glycine, lysine, nd especially taurine were rich in the at-death muscle. The muscle lapsed of 18 days showed an increase of taurine, histodine, valine and methionine, and a decrease of lyasine, arginine, aspartic acid, threonine, leucine, and isoleucine.

방어 보통육과 혈합육 근원섬유단백질의 열안정성 Ⅰ

변재형 부산수산대학교 1984 부산수산대학교 연구보고(자연과학편) Vol.24 No.2

The Proteinase Distributed in the Intestinal Organs of Fish-1

변재형 부경대학교 부설 수산식품연구소 1986 水産食品硏究所報告 Vol.7 No.-

어류의 조직중에 분포하는 알카리성 단백질분해효소의 활성조건

변재형,남택정 한국수산학회 1983 한국수산과학회지 Vol.16 No.2

Quality changes of the precooked frozen sardine(Sardinops melanosticta) during frozen storage were investigated by measuring extractable protein, expressible drip, available lysine and lipid oxidation as peroxide value. Fresh sardine was dressed, washed in chilled water, cooked in boiling water to have 55℃ and 70℃ at the center of the body, frozen at -40℃, and finally stored at -20℃ for 84 days. The quality factor mentioned above were determined in both ordinary and dark muscle at 14 day intervals through the period of storage. When cooked at 70℃, the changes in expressible drip were less than that of raw and the one cooked at 55℃. In observation of the extractability of muscle protein, no great change in extractable sarcoplasmic protein was observed, the extractable myofibrillar protein, however, showed a tendency to decrease during the period of frozen storage, accompanying the increase of the alkali-soluble protein. That was more excessive in ordinary muscle than dark muscle. Lipid oxidation of dark muscle was faster than that of ordinary muscle. Acid value was not changed, and peroxide value of the samples cooked at 70℃ and 55℃ was higher than that of raw at the early stage of the storage, after 40-50 day storage, it became lower than that of raw muscle.

방어 보통육과 혈합육 근원섬유단백질의 열안정성-1

변재형 釜山水産大學 水産食品硏究所 1984 水産食品硏究所報告 Vol.5 No.-

알긴산이 3T3 - L1 세포의 분화에 미치는 영향

변재형,황혜정,남택정 한국수산학회 2000 한국수산과학회지 Vol.33 No.6

알길산은 3T3-Ll 세포의 분화를 억제하였다. 3T3-Ll 세포의 분화를 촉진시키는 인자로 밝혀진 IGF-I과 insulin을 이용하여 알긴산의 분화에 미치는 영향을 검토한 결과, 알긴산은 insulin의 분화촉진작용을 특이적으로 억제하였다. 본 연구는 알긴산을 이용하여 알긴산의 지질 감소효과를 세포의 수준에서 검증하고자 하였다는 점에서 그 의의가 있으며, 이에 알긴산의 분화억제효과가 일어나는 메카니즘에 관한 연구가 있어야 할 것으로 생각된다. This study examines the effects of alginic acid, a source of dietary fiber, in a glucose-derived media. In particular, we examined how the presence or absence of alginic acid affected the differentiation and triglyceride densities of 3T3-Ll cells. We established that the addition of insulin-like growth factor-I (IGF-I) to 3T3-Ll cells results in acceleration of differentiation. We sought to determine the role of alginic acid in the production of fat, by adding alginic acid to 3T3-Ll cells and examining its ability to limit or potentiate this stimulatory effects of IGF-I and IGF binding proteins. We have determined that alginic arid restricts 3T3-Ll cell differentiation and the creation of triglycerides, effectively attenuating 3T3-L1 cell metablolism and growth.

먹장어의 근육단백질에 관한 영양생화학적 연구 1

변재형 부산수산대학교 1974 부산수산대학교 연구보고(자연과학편) Vol.14 No.2

멸치 젓갈 숙성중의 dimethylamine 의 생성

변재형,정보영,황금소 한국수산학회 1976 한국수산과학회지 Vol.9 No.4

魚類加工品中에 分布하는 2級 amine의 生成 原因을 究明하기 위한 硏究의 一部로서, 멸치를 22%의 食鹽을 添加하여 17℃와 27℃의 溫度別로 熟成시키면서 熟成 日程別로 蛋白質과 TMAO의 分解生成物을 分析하여 2級 amino의 生成과 關係있는 몇가지 實驗結果를 얻었기에 報告한다. 蛋白熊 窒素는 17℃와 27℃에서 熟成시켰을때, 全熟成期間을 通하여 一律的으로 減少하는 傾向을 보였으나, 아미노態 窒素는 蛋白態 窒素의 減少에 反比例하여 增加하였으며, 이 때 아미노態 窒素의 增加速度는 27℃에서 熟成한 것이 17℃에서 熟成한 것에 比하여 훨씬 빨랐다. TMA는 TMAO의 減少와 더불어 增加하여 갔으며 熟成 69日까지는 繼續 增加하다가 以後 徐徐히 減少하는 傾向을 보였다. 이때 溫度에 의한 差異는 보이지 않았다. DMA는 17℃에서 熟成시켰을 때는 熟成 69日까지 繼續 增加하다가 以後 微微한 變化를 보였으며, 27℃에서 熟成시킨 것은 熟成 59日까지는 繼續 增加하다가 그 以後는 微微한 變化를 보였다. DMA는 TMAO의 量的變化에 비추어, 17℃에서 熟成시켰을 때는 相關係數 r=-0.811, 그리고 27℃에서 熟成시켰을 때는 相關係數 r=-0.865로서 各各 負의 相關關係를 보였다. 멸치 젓갈 熟成中의 DMA의 生成原因은 그 寄與率이 17℃일 때 r²≒0.66, 27℃일 때는 r²≒0.75로서 TMAO의 分解와 密接한 關連이 있는 것으로 判斷되었다. Dimethylamine(DMA) is known as an origin compound of dimethylnitrosamine which is responsible for carcinogenesis. It has been also reported that relatively large amount of DMA is distributed in fish muscle, particularly in salted and fermented fish. In this experiment, the degradation products of protein and trimethylaminoxide(TMAO) by the temperature conditions of 17℃ and 27℃ in the course of anchovy fermentation with 22% of salt were analysed, and the formation of DMA was discussed. Protein-N decreased through the whole formentation period in the conditions of 17℃ and 27℃ whereas amino-N increased proportionally to the decrease of protein-N, and the increasing rate of amino-N was remarkably faster at 27℃ than at 17℃. Trimethylamine(TMA) gradually increased with the decrease of TMAO till 69th day of fermentation, hereafter tended to slightly decrease. It seemed that the difference in fermentation temperature affects on the formation of DMA and obviously on the variation of TMAO. Both DMA and TMA content were inversely varied with the TMAO content. Correlation coefficient of DMA to TMAO in quantitative variation was shown -0.811 at 17℃ and -0.865 at 27℃ of fermentation temperature respectively. The results suggested that the formation of DMA during fermentation of anchovy was attributed to the degradation of TMAO showing contributorial ratio of 0.66 at 17℃ and 0.75 at 27℃ respectively.

말쥐치 근원섬유단백질의 열안정성과 몇 가지 첨가제의 영향

변재형,최영준 한국수산학회 1985 한국수산과학회지 Vol.18 No.5

魚具類中에 分布하는 蛋白質分解酵素의 分離 및 精製에 關한 硏究

張東錫,金亨洛,趙鶴來,卞在亨 釜山水産大學校 1986 釜山水産大學 硏究報告 Vol.26 No.1-2

水産無脊椎動物중 낙지, 전복, 소라, 군소, 해삼, 개불과 水産脊椎動物인 말쥐치, 두툽상어, 먹장어, 고등어 그리고 정어리의 消化管 및 肉과 臟器組織을 區分하여 組織中에 分布하는 蛋白質分解組酵素를 抽出하여 그 活性을 比較·檢討하였다. 그리고 强한 活性을 보인 고등어 幽門垂에서 抽出한 粗酵素는 鹽析, DEAE-Sephadex A-50 column chromatography 및 Sephades G-100 겔여과에 의하여 3種類의 알칼리性 蛋白質分解酵素를 分離·精製하였으며 各 精製酵素에 대하여 活性最適條件, 基質親和度, 化學藥劑에 의한 影響 및 分子量 등을 究明하였다. 그리고 試料動物의 內臟에서 分離한 細菌中에서 가장 强한 蛋白質分解酵素를 生産하는 菌株를 選別하고 그 菌이 生産한 酵素를 精製하여 特性을 調査한 結果를 要約하면 다음과 같다. 1. 各 試料의 組織에서 抽出한 粗酵素中 活性이 强한 것으로는 정어리의 膵臟에서 抽出한 것이 活性最適條件인 pH 9.8, 45℃에서 固有活性은 360 이었고, 고등어 幽門??에서 抽出한 것은 pH 9.4, 45~50℃에서 固有活性은 275였다. 2. 고등어 幽門垂에서 抽出한 粗酵素에서는 3種의 알칼리性 蛋白質分解酵素가 分離·精製되었는데, 이 세 酵素를 SDS-PAG 電氣泳動法과 Se-phadex G-100겔 여과법에 의하여 分析·檢討한 結果 이들 酵素는 모두 monomeric polypeptide로서 구성되고, 分子量은 Enz. A가 27,500, Enz. B가 20,500, 그리고 Enz. C가 15,250 정도였다. 3. 酵素의 基質親和度를 測定한 結果 Km値는 casein 基質에 대하여 Enz. A는 5.0×??, Enz.B는 1.0×?? 그리고 Enz. C는 3.3×??였다. 4. 各 精製酵素는 soybean trypsin inhibitor에 의하여 活性이 沮害를 되었으며 Enz. A는 p-chloromercuribenzoate에 의해서도 沮害를 받았는데 Enz. B와 C는 serine系 蛋白質分解酵素로 判斷되었다. 5. 分離細菌中에서 제일 강한 蛋白質分解酵素를 生産하는 細菌은 Pseudomonas SPP. 였으며 酵素의 生産은 pH 7.0, 溫度 25℃, 食鹽 0.5% 염화칼슘 0.2%를 添加했을 때 제일 양호하였으며, 이 酵素는 分子量이 약 29,000되는 metal chelator sensitive neutral proteinase로 추정되었다. 6. 結論的으로 漁具類의 組織酵素는 계속적인 原料供給이 어려우므로 酵素의 産業的 利用을 위해서는 細菌이 生産한 菌體外 蛋白質分解酵素의 活用이 보다 有益할 것으로 생각된다. Proteolytic actvity of the tissue extracts from the octopus(Octopus variabilis), abalone (Haliotis discus hannai), top shell(Turbo cornutus), sea hare(Aplysia kurodai), sea cucumber(Stichopus japonicus), echiurid(Urechis unicinctus), file fish(Navodon modestus), cat shark(Scillion hinus tarazame), hag fish(Eptatretus burgeri), mackerel(Scomber japonicus) and sardine(Sardinops melanosticta) was compared to develope as an useful enzyme. The strongest proteolyticbacterium was selected among the isolated strains from the samples submitted, then the proteolytic exoenzyme produced by this strain was also characterized. Among the tissue enzyme extracts, the proteolytic enzymes from the pyloric caeca of mackerel and pancreas of sardine were estimated as strong alkaline proteinases. The optimum pH and temperature of the crude enzyme extracted with 1% NaCl from the pyloric caeca of mackerel and pancreas of sardine were pH 0.4, 50℃ and pH 9.8, 45℃, respectively. Specific activity of the former enzyme was 275 nM-Tyr. eq/mg-protein/min and that of latter one was 360 nM-Tyr. eq/mg-protein/min. Three kinds of alkaline proteinases were isolated from the pyloric caeca of mackerel, we named those as enzyme A, B and C. Molecular weight of enzyme A, B and C determined by SDS-polyacrylamide gel electrophoresis and Sephadex G-100 gel filtration method was to be 27,500, 20,500 and 15,250, respectively. Km value of enzyme A, B and C by the method of Lineweaver and Burk was determined to be 5.0×10??%, 1.0×10??% and 3.3×10??%, respectively, for 2% casein solution as a substrate. According to the analytical results, these enzymes were observed to be composed of monomeric polypeptide. The enzyme B and C were supposed to be a serine protease because these enzymes were remarkbly inhibited by soybean trypsin inhibitor. Pseudomonas spp. (named Pseudomonas FU 101) was identified as the strongest proteolytic bacterium among the isolated strains, which grew best at 25℃, pH 7.5. It is observed that the addition of 0.2% CaCl₂ and 0.5% NaCl in the culture medium was benefitted for the production of proteinase by Pseudomonas FU 101. The extracellular proteinase produced by the strain was supposed to be kind of metal chelator sensitive neutral protease, and it showed maximum activity at 35℃, pH 7.0. Molecular weight was estimated to be 29,000 by gel filtration. As a conclusion, both proteinases produced by Pseudomonas FU 101 and extracted from tissue of mackerel were pretty good in enzyme activity, but bacterial enzyme was more benefit for industrial use than the enzyme of mackerel tissue, because it is very difficult to supply continuously lots of pyloric caeca of mackerel as raw material for enzyme extraction.