• 제목/요약/키워드: The recovered protein fraction

검색결과 25건 처리시간 0.192초

수산가공공장폐액의 등전점이동 응집처리에 의한 유용성분재회수이용;4. 회수단백질의 어분 대체 사료로서의 이용 (Recovery and Utilization of Proteins and Lipids from the Washing Wastewater in Marine Manufacture by Isoelectric Point Shifting Precipitation Method;4. Utilization of the Recovered Protein Fractions as the Alternative Feed of Fish Meal.)

  • 김광우;김가현;어명희;김옥선;조순영
    • 생명과학회지
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    • 제18권6호
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    • pp.832-838
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    • 2008
  • 수산가공공장폐액의 주성분은 수용성단백질이며 일부 지방이 함유되어 있는 특성이 있으므로 그 수용성 단백질을 등전점 침전처리에 의해 침전회수하여 어분 대체 사료로서의 이용을 시도하였다. 1차 이스라엘잉어 사육 실험에서는 지방 산화가 진행된 고등어가공공장폐액으로 제조 된 고등어가공공장폐액 회수단백질 어분의 첨가량이 증가할수록 사료효율이 떨어지는 결과를 보였으나, 이 산화된 고등어가공폐액 회수단백질의 산화된 지방성분을 제거한 후 다시 2차 이스라엘 잉어 사육 실험을 한 결과에서는 고등어가공폐액 회수단백질의 첨가량이 증가할수록 사료효율이 좋음을 확인하였다. 따라서, 지금까지 버려지는 고등어가공공장폐액 중 수용성단백질을 등전점이동 응집처리법으로 회수하여 어분 대체 단백질원으로 활용할 수 있음을 실제 field에서의 이스라엘 잉어 사육 실험으로 확인할 수 있었다.

인삼사포닌 분획이 단백부족 마우스의 면역체계에 미치는 영향 (Studies on the Effects of the Saponin Fraction of Panax Ginseng on the Immune System of the Mouse Fed with Protein Malnutritive Diet)

  • 이나경;김영중
    • 약학회지
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    • 제30권4호
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    • pp.174-179
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    • 1986
  • The thymus weight of the mouse was 54.1% in protein malnutritive diet group and 39.2% in group treated with saponin fraction of Panax ginseng in comparison to normal diet group. This decreasing effects of protein malnutritive diet and saponin fraction on the thymus weight practically disappeared after four weeks. The saponin fraction showed no effect on the spleen weight of the mouse. The supplement of the saponin fraction enhanced total peritoneal exudate cells, content of total serum protein and albumin content of the mouse, each 45, 8 and 10% respectively in comparision to that of normal diet group. And these values in protein malnutritive diet group were 61.2, 83.6 and 87.0% respectively in comparision to that of normal diet group, and recovered to the level of normal diet group by the supplement of the saponin fraction. The electrophoregram of the serum protein of the mouse fed with protein malnutritive diet was different from that of the mouse fed with normal diet, but this difference practically disappeared by the supplement of the saponin fraction.

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알칼리 처리하여 회수한 냉동깡치 어육 단백질의 Lysinoalanine 함량 (Lysinoalanine in Protein Recovered from Frozen Belanger's Croaker, Johnius grypotus, Using Alkaline Processing)

  • 김건배;이근우;허성익;최영준
    • 한국수산과학회지
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    • 제40권6호
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    • pp.337-342
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    • 2007
  • The formation of lysinoalanine (LAL) in protein recovered from the belanger's croaker, Johnius grypotus, using a pH shifting process was measured by amino acid analysis. The LAL peak was detected at 49.24 min, between phenylalanine and histidine peaks in the amino acid analyzer. LAL was not detected in the fish muscle or in protein recovered using the alkaline pH shifting process. LAL was not formed in protein recovered after storage for up to 9 hrs at pH 11, but was detected in the soluble protein fraction at pH 11, followed heating at $90\;^{\circ}C$. The myosin heavy chain decreased with storage time at pH 11. The results suggest that the alkaline shifting process for recovering fish muscle protein is safe, and that no LAL forms.

Canavanine에 의한 보리 무배부 종자의 Amylase 활성과 단백질 함량의 변화 (Canavanine Effects on the Amylase Activity and Protein Content in Barley Half Seeds)

  • 전방욱
    • Journal of Plant Biology
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    • 제26권4호
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    • pp.173-180
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    • 1983
  • L-canavanine was added to GAs treated barley seeds, and induced amylase activity, soluble protein content, and arginine content were mesured. Canavanine, added at the beginning of the incubation period, inhibited amylase activity and protein accumulation. Amylase activity decreased markedly by addition of canavanine at 6 hr after incubation, where soluble protein content was not affected. The addition of canavanine after 12 hr incubation did not show serioud inhibited effect on the amylase activity and protein accumulation. GAs incubation caused decrement in arginine content per mg protein, but it was somewhat recovered by canavanine treatment. The longer the time between GAs and canavanine addition was, the less the recovery ration was. Arginine content in the $\alpha$-amylase fraction (ammonium sulfate 20~50% saturation) was lower than in 0~20% fraction, but higher than in 50~80% fraction. These results and control expreiments, using cordycepin and cycloheximide, support the idea that canavanine might incorporate into protein.

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소 정자의 운동성에 영향을 미치는 난포액 성분에 관한 연구 (Study on Components of Bovine Follicular Fluid Affecting on Sperm Movement)

  • 박영식
    • 한국수정란이식학회지
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    • 제12권2호
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    • pp.219-226
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    • 1997
  • Follicular fluid influxed into the oviduct during ovulation may affect movement of sperm for fertilization Thus, in this study, the effect of follicular fluid, obtained from follicles of l0mm in diameter, on number and quality of sperm recovered by swim-up separation was investigated and sperm-movement stimulating components extracted from follicular fluid with methanol and isooctane were separated by gel filtration with Sepadex G-1O, G-25 and G-1OO gels, and were isolated by electrophoresis with SDS-PAGE mini gel. The results obtained were as follows; 1. Diluted follicular fluid stimulated sperm movement. 2. Sperm-movement stimulating factors were in methanol extract. 3. Sperm-movement stimulating effect of methanol extract appeared in fraction I among fractions recovered after gel filtration. And the fraction I contained proteins indicating 4 major bands as about 47, 43, 25 and 14 kilodaldons and 5 minor bands as about 67, 58, 23, 22 and 21 kilodaldons. 4. The fraction I recovered from G-100 gel showed significantly low percentage of motile sperm and had no protein indicating the band of 67 kilodaldons among the minor bands.

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쥐 간에서의 Ginsenoside의 세포내 분포와 대사 (Cellular Distribution and Metabolism of Ginsenosides in Rat Liver)

  • 윤수희;이희봉
    • Journal of Ginseng Research
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    • 제17권2호
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    • pp.114-122
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    • 1993
  • 0.5 mg of natural ginsenoside mixture and 0.8 $\mu$Ci of synthesized 14C-ginsenosides were administered orally to a rat and killed at one hour after the ginsenoside administration and the liver was fractionated into nuclear fraction, mitrochondria microsomes and cytosol fraction. Radioactivity distribu lion in subcellular fractions of the liver showed that 32o1c of total radioactivity absorbed in the liver was in cytosol fraction but a significant portion of the radioactivity was also found in mitochondria (26.6%) and microsomal fraction (18.l%). 5.8% of the total radioactivity was recovered from the nuclear fraction as well. This suggested that ginsenosides might be distributed into all subcellular fractions. Activities of mitochondrial aldehyde dehydrogenase, lactate dehydrogenase and malate dehydrogenase of the liver of rat at two hours after the ginsenoside administraion were found appreciably stimulated, suggesting that the ginsenoside concentration in the liver might be around 10-5%, since optimum concentrations for most enzyme catalyzed reactions in vitro were known to be 10-6% 10-4%. A significant portion of the radioactivity recovered from subcellular fractions of the liver was found in protein fractions, suggesting that proteins might interact with ginsenosides. Examination of protein-ginsenoside interation by gel filtration, equilibrium dialysis and amonium sulfate precipitation technique suggesting that proteins and ginsenosides do not bound covalently but weakl\ulcorner combined. When purified ginsenoside Rbl and Rgl were incubated with rat liver cytosolic enzymes for 20 min, the above ginsenosides were hydrolyzed quickly, suggesting that ginsenosides might be rapidly hydrolyzed and metabolized in the liver. It was also observed in vitro that the ginsenosides such as Rbl and Rgl were easily hydrolyzed by rat liver cytosol preparation suggesting that absorbed ginsenosides might be quickly hydrolyzed and metabolized in the liver.

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Inclusion Body를 형성한 $\beta$-Glucosidase의 Chaperonin에 의한 활성 향상 (Improvement of Insoluble $\beta$-Glucosidase Activity by Molecular Chaperonin GroEL/ES)

  • 김종덕;;;하순덕;공재열
    • KSBB Journal
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    • 제14권4호
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    • pp.429-433
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    • 1999
  • $\beta$-Glucosidaes from Cellvibrio gilvus(CG) was successfully overproduced in soluble form in E. coli with the coexpression of GroEL/ES/. Without the GroEL/ES protein, the $\beta$-glucosidase overexpressed in E. coli constituted a huge amount(80%) of total cellular protein, but was localized in the insoluble fraction, and little activity was detected in the soluble fraction. Coexpression of the E. coli GroEL/ES had a drastic impact on the proper folding of the $\beta$-glucosidase; 20% of the overexpressed enzyme was recovered in the soluble fraction in active form. Similar effects of GroEL/ES were also observed on the overexpressed $\beta$-glucosidase from Agrobacterium tumefaciens(AT). And pET28(a)-RGRAR, partially deleted mutant lacking 5-amino acid residues at carboxy teminus also could be folded into an active form when expressed with the molecular chaperonin GroEL/ES, and its activity was higher than that of the without GroEL/ES system, In addition, the synergistic effect of GroEL/ES and the low induction temperature were important factors for solubilization of the inclusion body from overproduced $\beta$-glucosidases.

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Production of human insulin analogue using recombinant Escherichia coli

  • Lee, Ji-Seon;Park, Jin-Guk;Cho, Jung-Woo;Park, Sun-Ho;Nam, Doo-Hyun
    • 한국생물공학회:학술대회논문집
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    • 한국생물공학회 2003년도 생물공학의 동향(XII)
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    • pp.34-38
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    • 2003
  • For the production of $B^{30}-homoserine$ insulin analog as a novel anti-diabetic drug, the fermentative study was attempted for the maximal gene expression of HTS-fused $B^{30}-homoserine$ insulin precursor in the recombinant Escherichia coli cells. In a batch fermentation, the maximal production of insulin precursor as much as 38.95 mg/L-h, which occupied more than 12.8% of total cell protein. was achieved when the gene expression was induced by 0.5 mM IPTG at the middle logarithmic growth phase. The HTS-fused $B^{30}-homoserine$ insulin precursor was recovered from a batch culture through the processes of cell harvest, collection of insoluble fraction after sonication and purification by nickel affinity column chromatography. The isolated insulin precursor was 14 mg/L with a recovery yield of 35.9% of expressed gene product. The insulin A and B chain mixture was recovered after the insulin precursor was subjected to CNBr cleavage and purified by nickel affinity column chromatography. The isolated insulin chains were then sulfitolyzed with sodium thiosulfat and sodium tetrathionate, and reconstituted to insulin analog with ${\beta}-mercaptoethanol$, followed by purification with CM-Sepharose C-25 column chromatography.

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Optimization of Whey-Based Medium for Growth and ACE-Inhibitory Activity of Lactobacillus brevis

  • Ahn, Jae-Eun;Park, Seung-Yong;Lee, Byong-H.
    • Journal of Dairy Science and Biotechnology
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    • 제25권1호
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    • pp.1-7
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    • 2007
  • 유청을 기초로 하는 배지를 제조하여 Lactobacillus brevis를 배양하면서 유청 단백질로부터 기능성 펩타이드 생성을 알아보고자 하였다. Lb. brevis의 적정생장에 필요한 배지성분의 농도는 2% 유청 분말, 1%의 포도당 및 0.5%의 효모추출물이었다. Lb. brevis의 생장은 효모 추출물의 보충이 포도당의 보충보다 더 효과적이었다. 이 유청 배지에서 Lb. brevis의 생장은 2.0 ${\times}$ 10$^8$CFU/mL에 달하였다. 생장 후의 유청 배지를 10,000 ${\times}$ g에서 10분간 원심분리하여 그 여액으로부터 얻은 유청단백분해물은 ACE 효소 억제 효과가 나타났다. 분자량 8,000Da 이하로 부분 정제한 분획의 ACE에 대한 억제효과는 유청단백분해물의 64.7 ${\pm}$ 3.6%, IC$_{50}$은 38.8 ${\pm}$ 2.2 mg/mL로 나타났다. 따라서 유청을 기초로 한 배지는 젖산균으로부터 유청 단백질을 발효하여 ACE 억제 효과를 주는 펩타이드 생산에 적합한 배지임을 알 수 있었다.

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넙치(Paralichthys olivaceus) 및 가다랑어(Katsuwonus pelamis) 알로부터 알칼리 가용화과정을 통해 회수한 알칼리 불용성획분의 이화학적 성분특성 (Physicochemical Properties of Alkaline-insoluble Fractions Recovered from Bastard Halibut Paralichthys olivaceus and Skipjack Tuna Katsuwonus pelamis roes by Alkaline Solubilization)

  • 윤인성;강상인;박선영;차장우;김도엽;김진수;허민수
    • 한국수산과학회지
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    • 제51권3호
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    • pp.230-237
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    • 2018
  • This study investigated the food and nutritional characteristics of alkaline-insoluble fractions (AIFs) recovered from bastard halibut Paralichthys olivaceus (BH) and skipjack tuna Katsuwonus pelamis (ST) roes using the alkaline solubilization. The moisture content of AIFs ranged from 4.8% to 12.8%, and ST provided significantly better yields (9.5 for STAIF-11 and 7.1 g/100 g roe for STAIF-12) than did BH (P<0.05). The protein content of AIFs ranged from 71.7% to 79.2%, with the highest level yielded by STAIF-11 (6.8 g/100 g roe). The crude fat content of AIFs was 10.9-14.3% and the mineral content was 0.7-3.4%. The major mineral components of AIFs were sulfur, sodium, potassium, and phosphorus. Color values showed that BHAIFs were significantly brighter than STAIFs. Total contents of essential amino acids were significantly higher in STAIFs (47.5-49.5%) than in BHAIFs. The major essential amino acids found in AIFs from both sources were Val, Leu, Lys, and Arg. Therefore, AIFs were significantly superior to whole BH roe in terms of physicochemical and nutritional status, and we identified species-specific differences between BH and ST. Protein is a major component of AIFs recovered from fish roes, which suggests that they have potential for use as a protein source.