• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.28 no.2
• /
• pp.157-162
• /
• 1995

When fish meat is washed for the processing of surimi, about 50ff of lipid in the fish meat is removed from the fish meat to the effluent. The removed lipid was easily recovered by centrifugation or filteration of wastewater washed fish meat. Then, the recovered lipid was utilized as a material of mayonnaise sauce processing. The major fatty acids in the recovered lipids are $C_{16:0},\;C_{18:0},\;C_{16:1},\;C_{20:5},\;and\;C_{22:6}$ Polyenoic fatty acids were composed of $33.6\%$ to total fatty acids. When the recovered lipid was substituted for soybean oil in processing of mayonnaise sauce, the maximum percentage of substitution ratio presumed to be $30\%$ according to viscosity, color difference, and emulsion stability evalution for the substituted ones.

• Korean Journal of Food Science and Technology
• /
• v.31 no.4
• /
• pp.1077-1083
• /
• 1999

This study was aimed to evaluate the effectiveness of hydrophilic, lipophilic antioxidants and emulsifiers by HLB (hydrophilic lipophilic balance) in different oil systems. Lipophilic antioxidant (${\delta}-tocopherol$), hydrophilic antioxidant (gallic acid) and emulsifier(lecithin, tween 20, span 60) were evaluated in relation to oil stability in bulk oil system (soybean oil) and emulsified with Tween 80 at $60^{\circ}C$. In the storage test ($60^{\circ}C$), gallic acid was more effective on the stability of oil oxidation than ${\delta}-tocopherol$ in bulk and emulsion system. Lecithin as a hydrophilic emulsifier was more effective than tween 20 on the stability of oil oxidation in bulk and emulsion system. Also span 60, a lipophilic emulsifier, was more effective than tween 20, a hydrophilic emulsifier, in bulk and emulsion systems.

• Food Science of Animal Resources
• /
• v.20 no.2
• /
• pp.101-106
• /
• 2000

Effects of Ph on the activity of lipase isolated from milk fat globules were investigated, using coconut oil and homogenized milk as substrate. With buttermilk as an enzyme source for coconut oil and homogenized milk substrates bell-shaped curve was observed at $37^{\circ}C$, having the highest activity at pH 9.5. However, lipase activity at $0^{\circ}C$ continuously increased up to pH 10.0. With the purified lipase for homogenized milk substrate, the bell -shaped curve and the highest activity were observed at $37^{\circ}C$ and pH 9.0, respectively. Lipase activity at $0^{\circ}C$ increased up to pH 10.0. The addition of bovine serum albumin to the coconut oil shifted the optimum pH to pH 9.5 and the activity remarkably declined at pH 10.0. The effect of pH on the stability of purified lipase was depending on the temperature. Wehn the lipase kept at $37^{\circ}C$ for 20 minutes, it's activity remarkably declined as pH increased: the activity at pH 10.0 was declined by 13% of that pH 8.5. However, when the lipase kept at $4^{\circ}C$ for 60minutes, the activity was stable within the range of pH 7.5 to 10.0.

• Korean Journal of Food Science and Technology
• /
• v.19 no.1
• /
• pp.23-28
• /
• 1987

The effects of phosphatidyl choline (PC), phosphatidyl ethanolamine (PE), phosphatidyl inositol (PI), phosphatidic acid (PA), phosphatidyl glycerol (PG), and cardiolipin (CL) on the flavor stability of purified soybean oil were studied. Purified soybean oil obtained from soybean oil by silicic acid chromatography does not contain measurable iron, tocopherols and phospholipids. Three hundred ppm of PC, PE, PI, PA, PG, or CL was added to the purified soybean oil, with and without 1ppm ferrous iron added. The flavor stability of sample, which was stored at $60^{\circ}C$ for 10 days in dark oven, was determined by a combination of volatile compounds formation and molecular oxygen disappearence in the headspace of air-tightly sealed serum bottle every 48 hrs. Results showed that, in general, phospholipids worked as prooxidant in the pufified soybean oil without ferrous iron added, and worked as antioxidant in the oil, when added 1ppm ferrous iron. The results also suggest that phospholipids work as prooxidant by increasing the solubility of oxygen on the surface of oil, and work as antioxidant in the oil containing 1 ppm ferrous iron by chelating iron. The results showed that PE and PA are better antioxidants than PC and PG. CL and PI showed the lest antioxidant activities in the oil will 1ppm ferrous iron added.

• Journal of Life Science
• /
• v.12 no.4
• /
• pp.483-489
• /
• 2002

We investigated the biochemical properties of insect defensin expressed and secreted from Saccharomyces corevisiae. The defensin showed extremely high resistance to boiling for up to 30 min and to pH values tested from 2.0 to 12.0. The treatment of defensin with various proteases abolished antibacterial activity. However, amylases, cellulase, lipase and catalase had no effect on the activity. The defensin was purified to homogeneity through ammonium sulfate concentration of culture supernatant, SP-Sepharose column chromatography and RP-HPLC. Tricin-SDS-PAGE analysis revealed that the molecular weight of the defensin was about 4.0 kDa. The antibacterial activity of the purified defensin was verified by renaturation of stained gel and gel pouring assay using Micrococcus luteus as a test organism.

• Proceedings of the Korean Society of Broadcast Engineers Conference
• /
• 2004.11a
• /
• pp.233-236
• /
• 2004

다양한 처리능력을 가진 단말기들은 복잡한 네트워크, 환경의 호환성을 제공하기 위해서, 전송 네트워크 채널이 허용하는 범위내로 부호화 된 비디오의 비트 율을 적응적으로 맞춰 주어야 한다 트랜스코더는 특정 비트율로 부호화되어 있는 비디오를 원하는 비트율의 다시 변환하기 위해서 복호화 만 후 다시 부호와의 과정을 거쳐야 하기 때문에 이에 따른 계산량의 증가와 더불어 전송시간에 문제가 발생한다. 이를 해결하기 위한 한 가지 방법으로 제안된 것이 프레임 건너뜀 기법 즉 시간적 해상도 변환 트랜스코딩이다. 비디오를 부호화하는 과정에서 계산량을 가장 많이 차지하는 움직임 추정과정의 계산량을 줄임으로써 트랜스코딩을 수행하는데 소모되는 시간과 노력을 크게 줄이고, 건너뛰지 않고 남아있는 프레임에 더 많은 비트를 할당하여 요구되는 화질을 유지할 수 있다. 본 논문에서는 움직임 벡터의 방향성을 고려한 움직임 벡터 재추정 기법과 정제 기법을 제안한다 제안된 기법인 E-FDVS(Efficient-Forward Dominant Vector Selection)는 움직임 벡터의 방향성을 고려하여 매크로블록과 움직임 벡터의 차이를 이용하여 움직임 벡터를 재추정한다. 그리고 제안한 기법인 DOS(Direction Oriented Search)를 사용하여 재추정 된 움직임 벡터의 방향으로 강한 움직임 벡터 정제를 함으로써 기존의 기법에 비해 우수한 화질을 제공한다.

• Korean Journal of Food Science and Technology
• /
• v.40 no.1
• /
• pp.70-75
• /
• 2008

Two extracellular amylase isozymes were purified and characterized from alkalophilic Pseudomonas sp. KFCC 10818 for the production of maltooligosaccharides. The molecular weights of the homogeneous proteins were 50 kDa and 75 kDa, respectively. The 50 and 75 kDa amylases showed optimum temperatures at 35 and $40^{\circ}C$, respectively. The optimum pH of the enzymes ranged from pH 6-8, and the enzymes were resistant to an alkaline condition of pH 12. Via the enzyme's actions, the final products from maltooligosaccharides or soluble starch were maltose and maltotriose. Calcium was a potent activator of the 50 kDa amylase. Finally, the N-terminal amino acid sequences of the 50 and 75 kDa amylases were QTVPKTTFV and DTVPGNAFQ, respectively.

• Microbiology and Biotechnology Letters
• /
• v.19 no.3
• /
• pp.209-214
• /
• 1991

Purification of the bacteriocin from Lactococcus sp. 1112-1 was achieved by successive column chromatography on CM-Sephadex C-25 and Sephadex G-50, starting from cell disruption broth. 16.2% of the initial activity was recovered after this purification step and it was shown 123-fold increase in purification. Purified bacteriocin was shown a single band on SDS-polyacrylamide gel electrophoresis. This substance was rather stable at heat treatment and alkaline pH relatively. The residual antimicrobial activity was 38% when the bacteriocin was treated by heat at $100^{\circ}C$ for 60 min. And 23% of the activity remained at pH 8.0 after standing for 48 hr. The amino acid composition of purified bacteriocin was made up 26 residues.

• The Journal of Natural Sciences
• /
• v.14 no.2
• /
• pp.55-65
• /
• 2004

A thiol-specific antioxidant(TSA) protein was purified from Earthworm, Lumbricus terrestris by DEAE-Cellulose, Phenl sepharose, Sephacryl S-200 gel filtration and HPLC S-300 Column Chromatography. This protein showed a thiol-specific antioxidant activity against inactivation of glutamine synthetase by a metal-catalysed oxidation system capable of generation reaction oxygen species. The molecular mass of the protein was determinated to be 51-kDa by SDS-polyacrylamide gel electrophores. Taken together, the purified TSA protein could be a new member of TSA family.

• The Journal of Natural Sciences
• /
• v.4
• /
• pp.59-68
• /
• 1991

$\beta$-Galactosidase(EC 3.2.1.23) from pathogenic Neisseria lactamica 2118 was purified by p-aminopheny1-$\beta$-D-thiogalactopyranoside agarose affinity chromatography. Then some properties of the purified $\beta$-galactosidase were investigated.$\beta$-Galactosidase form Neisseria lactamica 2118 was constitutive enzyme, not induced by lactose and IPTG. Optimal activity was observed at $35^{\circ}C$ and pH 7.5 and the enzyme was stable at the range of pH 6.0-9.0 and at temperature below $50^{\circ}C$. The enzyme activity was inhibited by cations such as $Hg^(2+)$ and $Co^(2+)$.