• Journal of the Korean Society of Food Science and Nutrition
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• v.37 no.8
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• pp.1009-1017
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• 2008

For the effective use of exopeptidase from squid viscera as food processing aids, the viscera of Argentina shortfin squid (Illex argentinus) were fractionated by various methods such as acetone treatment, ammonium sulfate treatment, anion exchange chromatography, and gel filtration. The positive exopeptidase fractions were obtained from the fraction II treated by cold acetone ($30{\sim}40%$, w/w), the fraction V by ammonium sulfate ($60{\sim}70%$ saturation), the fraction II (0.2 M NaCl) by anion exchange chromatography, and the fraction I ($30{\sim}50\;kDa$) by gel filtration. The specific activities of positive fractions from viscera of I llex argentinus against substrates were higher to LeuPNA than to ArgPNA. Total activity and recovery against LeuPNA of positive fraction by gel filtration were 1,867 U and 30.69%, respectively, which were the highest among those of positive fraction. The results suggested that the gel filtration chromatography method was the most efficient method for the fractionation of exopeptidase from viscera of Illex argentinus.

• Korean Journal of Veterinary Research
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• v.8 no.1
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• pp.6-10
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• 1968

순화(純化)된 뉴켓슬병(病) 바이러스를 얻기 위(爲)한 기초적(基礎的)인 실험(實驗)으로 바이러스 재료(材料)를 완형액(緩衡液)의 종류(種類) 및 수소(水素)이온 농도(濃度), 한천농도(寒天濃度)를 달리한 한천(寒天)겔칼럼에 통과(通過)시켰다. 그러고 바이러스 재료(材料)의 혈구응집력가(血球凝集力價)와 총질소량(總窒素量)을 비교(比較) 측정(測定)하여 다음과 같은 결과(結果)를 얻었다. 1. 한천(寒天)겔 응과법(凝過法)을 뉴켓슬병(病) 바이러스의 순화(純化)에 간단(簡單)히 이용(利用) 할수 있다. 2. pH 7.0 이상(以上)의 인산식염(燐酸食鹽) 완형액(緩衡液)과 5~8%의 한천농도(寒天濃度) 입자(粒子)를 이용(使用)할때 가장 좋은 결과(結果)를 얻을 수 있었다. 3. 매시(每時) 5~10ml의 유출속도(流出速度)일때 55ml 부터 80ml의 유출액중(流出液中)에서 고농도(高濃度)의 바이러스를 얻을 수 있었다.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.24 no.5
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• pp.273-288
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• 1991

To elucidate the physiological and biochemical differences between chondrichthyes and osteichthyes, the properties of the specific digestive enzymes in cat-shark, Cephaloscyllium umbratile, and mackerel, Scomber japonicus, were studied. Homogenous trypsin proved through the disc-electrophoresis, SDS-PAG electrophoresis and gel filtration was obtained from the pancreas of cat-shark by $50-70\%$ saturated ammonium sulphate fractionation, DEAE-Sephadex A-50 column chromatography, benzamidine-Sepharose 6B affinity chromatography and Sephadex G-75-120 gel filtration. Two types of trypsins were also obtained from the pyloric caeca of mackerel by $30-70\%$ saturated ammonium sulphate fractionation and the slightly modified procedure from the method adopted in the purification of cat-shark trypsin. The two trypsins, designated trypsin A and B, were proved their homogeneity by disc- and SDS-PAG electrophoresis and gel filtration. The molecular weights of the trypsins were estimated to be 31,700 for cat-shark trypsin, 30,000 for mackerel trypsin A and 29,000 for mackerel trypsin B by SDS-PAG electrophoresis, but those were estimated to be 21,500 for cat-shark trypsin, 23,700 for mackerel trypsin A and 21,500 for mackerel trypsin B by gel filtration. The trypsins exhibited their optimum conditions at pH 9.0 and on temperature ranged from $45^{\circ}C\;to\;50^{\circ}C$ for cat-shark, and at pH 8.0 and a temperature of $50^{\circ}C$ for mackerel trypsin A and B, respectively. The cat-shark trypsin was stable at pH 10.0 and the temperature below $10^{\circ}C$, whereas the mackerel trypsin A and B, were stable in the range over pH 7.0 to pH 9.0 below $10^{\circ}C$ and at pH 8.0 below $35^{\circ}C$, respectively. The mackerel trypsins were severely inhibited by some heavy metal ions such as $Ag^{2+},\;Cu^{2+}\;and\;Hg^{2+}$ compared to cat-shark trypsin. All of the enzymes were also inhibited by antipain, leupeptin, TLCK(tosyllysine chloromethyl ketone) and SBTI(soybean trypsin inhibitor) remarkably. The inhibitory effects of PMSF(phenylmethane sulphonylfluoride), DFP(diisopropyl fluorophosphate) and benzamidine were indicated that these enzymes belong to serine-proteases.

• Korean journal of applied entomology
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• v.37 no.1
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• pp.59-64
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• 1998

A juvenile hormone binding protein (JHBP) has been isolated from the whole body homogenate of Galleria rnellonella final instar larvae by gel filtration. The isolated protein is homogenous as judged by column chromatography and gel electrophoresis in the presence and absence of denaturing agent. The JHBP has a relative molecular weight of 32 k by denaturing gel electrophresis and 28 k by gel filtration. The protein exhibits a dissociation constant of 3.9 x M for JH 111.

• Proceedings of the Membrane Society of Korea Conference
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• 1994.04a
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• pp.58-58
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• 1994

슬립캐스팅법으로 제조한 튜브형 $\alpha$-알루미나 담체 (평균기공크기 = $0.1 \mum$)에 졸-겔 침지코팅(dipcoating) 또는 가압코팅 (pressurized coating) 법에 의하여 극미세입자 $\gamma$-AlOOH, $TiO_2, SiO_2$, 및 aluminosilicate diphasic 졸을 코팅한 후 300 ~ 500$\circ$C 에서 열처리하여 세라믹 복합막을 제조하였다. 복합막 전체에 대한 균열유무는 $N_2$ 기체투과율의 평균압력에 대한 의존성으로부터 평가하였으며, 한외여과 (ultrafiltration)에의 응용성을 규명하기 위하여 막의 재질 및 제조조건에 따른 polyethylene glycol (PEG) 수용액의 분획분자량 변화를 측정하였다. 합성 세라믹 복합막의 분획분자량 측정 결과 $SiO_2$의 경우 2,000 정도로 매우 우수하였으며 $\gamma-Al_2O_3, TiO_2$, 그리고 aluminosilcate 막들은 6,000 ~ 10,000 범위 값을 갖고 있었다. 또한 막의 기공크기 및 분획분자량을 제어하기 위한 방법으로서 $TiO_2$ 복합막을 300 ~ 700$\circ$C 에서 열처리하였으며 이들에 대한 분획분자량 변화를 비교 분석하였다.

• Journal of the Korean Society of Food Science and Nutrition
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• v.17 no.4
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• pp.371-375
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• 1988

Tubular ultrafiltration membranes were used to investigated mass transfer characteristics of waste cheese whey. The effects of bulk concentration and flow velocity on permeat flux, mass transfer coefficient and apparent rejection coefficient were measured. Mass transfer coefficient was increased linearly with increasing flow velocity, and following relationship between mass transfer coefficient(k) and linear velocity(u) was obtained. $k=0.87{\times}10^{-5}u^{1-1}$ It is interjecting to note that plots for all linear velocity tend to converge to the same point for zero permeating flux, and the maximum bulk concentration that can be achieved with cheese whey extracts was 38(w/v %). In general, membrane rejection coefficient increased with increasing flow velocity and the rejection coefficients of cheese whey solution and that of lactose in cheese whey solution were obtained $0.40{\sim}0.65$, $0.15{\sim}0.30$, respectively.

• Journal of Life Science
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• v.6 no.4
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• pp.241-249
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• 1996

A collagenase was isolated from the culture filtrate of Vibrio mimicus (ATCC 33658). The enzyme was purified to homogeneity by ammonium sulfate precipitation and DEAE-Sephadex A-50 chromatography, which an activity recovery of 22%. The molecular weight of the purified enzyme was estimated to be 42 kDa by SDS-polyacrylamide gel electrophoresis and gel filtration, indication a monomer structure. The optimum pH and temperature od the enzyme for insoluble collagen (Type I) were around 7.75 and 28$\circ$C, respectively. Some chelating agents and serine protease inhibitor inactivated the enzyme, but L-cysteine and histidine did not affect the activity. The amino acid composition indicated that the collagenase contained high amounts of amino acid residues of glycine and alanine. The K$_{m}$ and R$_{cat}$/K$_{m}$ values for the collagenase, using insoluble collagen (type I) as substrate, were 2.86 mg/ml and 972.28 U/mg-protein, respectively.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.33 no.1
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• pp.70-74
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• 2000

Agar for microbiological medium was prepared with pilot-scale for industrial application by the process of microfiltration ($0.4 {\mu}m\;pore size$) in $40{\~}50{\circ}C$, washing with sot water, and treatment with $0.25\;N NaOH\;at\;70{\circ}C$. Transparency, gel strength, viscosity, sulfate content, and syneresis ratio of agar prepared from Gelidium amansii was compared with commercial agar for microbiological medium. Gel strength and transparency were increased with processing, however, it's viscosity, sulfate content, and syneresis ratio were reduced. The final agar product was superior to commercial agar for microbiological medium.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.23 no.1
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• pp.12-24
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• 1990

Two trypsin-like enzymes, designated trypsin A and 3, purified from the intestine of menhaden by $(NH_4)_2SO_4$ fractionation, Benzamidine-Sepharose 6B affinity chromatography, DEAE-Sephacel ion exchange chromatography and Sephadex G-75 gel filtration chromatography. The two trypsins were subjected to compare the enzymatic properties of the trypsin-like enzymes from the other dark fleshed fishes. Both trypsins catalysed the hydrolysis of N$\alpha$-benzoyl-DL-arginine-p-nitroanilide and they were remarkably inhibited by several well known trypsin-inhibitors, tosyllysyl chloromethyl ketone, soybean trypsin inhibitor, be-nzamidine, leupeptin and antipain, etc. Therefore, it was ascertained that the two enzymes are serine-type trypsins. The molecular weights of these enzymes were about 25,000 and 26,200, respectively, ;Is determined by SDS-PAG electrophoresis and by Sephadex G-100 gel filtration, and the molecular weights of these two enzymes are somewhat fewer than those from the other dark fleshed fishes. Both enzymes had less basic amino acids such as arginine and Iysine, whereas they had slightly high contents of neutral amino acids, glycine, alanine and tryptophane. The enzymes showed a pH optimum of $8\~11$ at $60^{\circ}C$ against the $N\alpha$-benzoyl-DL-argi-nine-p-nitroanilide substrate and they were quite unstable above $40^{\circ}C$ and under the atidic pH region. The Km constant of the two enzymes against the $N\alpha$-benzoyl-DL-arginine-p-nitroanilide was $1.4\times10^{-4}M$ for trypsin A and $4.3\times10^{-5}M$ for trypsin B, respectively.

• 한국해양학회지
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• v.24 no.2
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• pp.79-83
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• 1989

Attempts were made to analyze the toxin composition of the toxic mussel Mytilus edulis galloprovincialis which were collected from aquaculture pond in Apr. 1988 in Hachung, Koje, southern Korea. The toxins were partially purified from the ethanolic extract of the mussel digestive glands by activated charcoal and Bio Gel P-2 column chromatography. HPLC analysis demonstrated that the toxin consisted mainly of gonyautoxin 1-4 (GTX 1-4), along with trace amounts of saxitoxin (STX) and protogonyautoxin 1-2 (PX 1-2).