• 한국미생물·생명공학회지
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• 제19권5호
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• pp.456-463
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• 1991

Bif. longum KCTC 3215에 의한 Beta-galactosidase의 최적생성조건은 탄소원으로 lactose 1.0, 초기 pH 7.0, 배양온도 $37^{\circ}C$ 및 배양시간 17시간 후였다. 이 효소는 protamine sulfate, ammonium sulfate, DEAE-Sephadex A-50 ion exchange chromatography 및 Sephadex G-150 gel filtration 등 4단계 정제과정을 거쳐 9.25배 정제되었다.

• 한국응용과학기술학회지
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• 제33권3호
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• pp.599-605
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• 2016

Serratia marcescens (S. marcescens)는 Gram-음성 박테리아로 soytone과 에탄올이 함유된 Cang's soytone (CS) 배지에서 $28^{\circ}C$, pH 7.5의 조건으로 배양할 때 가장 많은 붉은 색소를 생성하였다. S. marcescens 균주로부터 붉은 색소를 분리, 정제하기 위하여 여러 가지 유기용매를 사용하였다. 분리 정제한 붉은 색소는 가시광선 영역의 537 nm에서 ${\lambda}_{max}$를 가지고 있었고, HPLC-Mass로 분석한 결과 분자량 537과 565 g을 가지는 두 가지 물질로 구성되어 있음을 확인하였다. 또한 상온과 pH 6 이하의 산성조건에서는 태양광에도 안정함을 확인하였다.

• Journal of Microbiology and Biotechnology
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• 제11권6호
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• pp.1018-1023
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• 2001

Oleamide (cis-9-octadecenamide) is endogenous primary amide of fatty acid that is produced in small amounts in animal brains. It is known to induce sleep and to lower temperature by destroying the lipid plasma membrane structure of cells, thereby disclosing gap junction channels. To develop a new biological production method for oleamide, a screening program was conducted to isolate a microorganism producing oleamide. Among 1,500 soil microorganisms tested, KK90378 exhibited a potent positive reaction with Dragendoff`s reagent, used to detect the primary amide of oleamide. KK90378 was identified as a Streptomyces species based on cultural and morpohological characteristics, the presence of diaminopimelic acid in the cell wall, and the sugar patterns for the whole-cell extrat. Streptomyces sp. KK90378 produced oleamide 3 days after culture at $28^{\circ}C$, pH 7.2 A series of purification steps, including hexane extraction, silica gel column, and preparative thin layer chromatographies, were performed for the purification of oleamide. A spectrophotometric analysis using $^1H$, $^13C$-NMR, and GC-MS confirmed that the chemical structure of the purified oleamide was identical to that of authentic oleamide.

• 한국미생물·생명공학회지
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• 제11권1호
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• pp.15-21
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• 1983

전보에서 분리 동정한 Y-33 균주의 $\beta$-galactosise 효소생산조건을 검토하고 효소를 정제하여 정제효소의 성질을 조사한 결과는 다음과 같다. 1. 효소생산을 위한 최적초발 pH는 7.0이었고 최적온도는 $65^{\circ}C$이었다. 2. 효소는 lactose와 galactose에 의하여 유도되어졌으며 세포내효소이었다. 3. 조효소액을 1차 DEAE-cellulose, 2차 DEAE-cellulose column chromatography 및 Sephadex G-150로 gel filtration하여 정제도가 28.3배, 수율이 15.2%의 정제효소를 얻었다. 4. 정제효소는 polyacrylamide gel 전기 영동에 의하여 순도가 검정되었다. 5. 정제효소의 유당가수분해를 위한 최적작용 온도는 $65^{\circ}C$. pH는 6.5이었다.

• 한국미생물·생명공학회지
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• 제19권1호
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• pp.70-75
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• 1991

Continuous and simultaneous production of gluconic acid and sorbitol from glucose and fructose was carried out by using glucose-fructose oxidoreductase and glucanolactonase of Zymomonas mobilis. In order to utilize the enzymes without purification, Zymomonas mobilis was permeabilized with toluene. Optimum conditions for permeabilization and reaction kinetics of permeabilized Zymomonas mobilis were studied. In batch operation with the permeabilized cells immobilized in alginate beads, about 90% conversion was obtained within 35 h reaction. Continuous production of gluconic acid and sorbitol using the immobilized permeabilized cells was carried out. Optimum conditions for continuous operation with the imn~obilized cells were; pH 6.2 and temperature $40^{\circ}C$. Maximum productivities for gluconic acid and sorbitol were about 14.5 g/l/h and 14.8 g/l/h respectively at the dilution rate of 0.075 $h^{-1}$ when 300 g/l each of substrates was fed.

• 한국식품영양과학회지
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• 제28권5호
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• pp.1010-1016
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• 1999

Protease related mold was isolated and selected as a starter culture for commercial production of meju. Isolated microorganism was identified as Syncephalastrum racemosum PDA 132 2. To obtain basic data about protease for production of soybean peptides and application of the strain in meju fermentation, we extrated and purified protease and charateristics of the enzyme were investigated. The optimum condition for the production of enzyme was pH 4.0, 30oC, 5 days. The protease was purified 19.7 folds by gel filtration and ion exchange chromatography and specific activity was 12.4unit/mg. The purified enzyme was 34kDa in size, thiol protease(100% inhibited by PCMB), and was acidic protease(stable between pH 2.0~5.0). Vmax of the enzyme was 2.14 g/min which was lower(1/50) than that of by Asp. wentti and B. subtilis.

• 한국식품영양학회지
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• 제12권3호
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• pp.240-245
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• 1999

The purpose of this study was to develop the new microbial bioflocculant available in a food and fer-mentation industal. This study was reported the results of the composition for optimum culture medium and elemental characteristic of crude purification bioflocculant following the previous report(I). The maximum production of the flocculant from Bacillus megaterium was observated in the culture medium containing 2% sucrose 0.3% NaNO3 0.01% tryptone 0.01% beef extract 0.05% MgSO4 ·7 H2O 0.005% CaCO3 Addition of the sucrose as carbon sources and inorganic salt such as MgSO4, CaCO3 significantly increased the production of flocculant more than nitrogen sources. In the result of color reaction of the crude purified bioflocculant it was investgated that anthrone was positive and benedict burette and nin-hydrin was negative. These result were indicated that the flocculant produced from Bacillus megaterium was a kind of exopolysaccharide.

• 한국농업기계학회:학술대회논문집
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• 한국농업기계학회 1993년도 Proceedings of International Conference for Agricultural Machinery and Process Engineering
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• pp.1405-1414
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• 1993

The purification of sewage deriving from agricultural and food industries is today a serious problem mainly in areas characterized by intensive production plants. The solution examined in this work, involves a system of natural evaporation which employs special panels with a large evaporating surface constituted by an internal cellular structure in polyethilene. Using renewable energy they allow to speed up the natural evaporating effect thus eliminating some drawbacks such as swamps and obtaining sewage concentration with relatively low costs. The institute of agricultural engineering has carried out tests on the disposal of sewage deriving from two very important production sectors; pig-breeding and olive oil production . at a were gathered in order to verify the operating capacity of plants and their variables . On the remaining concentrated part tests were also carried out in order to know its chemical and chemical-physical features and to study the possibility for its us .

• Journal of Microbiology and Biotechnology
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• 제24권4호
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• pp.489-496
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• 2014

High levels of extracellular xylanase activity (211.79 IU/mg) produced by Paenibacillus sp. NF1 were detected when it was submerged-cultured. After three consecutive purification steps using Octyl-Sepharose, Sephadex G75, and Q-Sepharose columns, a thermostable xylanase (XynNF) was purified to homogeneity and showed a molecular mass of 37 kDa according to SDS-PAGE. The specific activity of the purified XynNF was up to 3,081.05 IU/mg with a 14.55-fold purification. The activity of XynNF was stimulated by $Ca^{2+}$, $Ba^{2+}$, DTT, and ${\beta}$-mercaptoethanol, but was inhibited by $Fe^{2+}$, $Zn^{2+}$, $Fe^{2+}$, $Cu^{2+}$, SDS, and EDTA. The purified XynNF displayed a greater affinity for oat spelt xylan with the maximal enzymatic activity at $60^{\circ}C$ and pH 6.0. XynNF, which was shown to be cellulose-free, with high stability at high temperature ($70^{\circ}C-80^{\circ}C$) and low pH range (pH 4.0-7.0), is potentially valuable for various industrial applications. The enzyme hydrolyzed oat spelt xylan to yield mainly xylooligosaccharides (95.8%) of 2-4 degree of polymerization (DP2-4). Moreover, the majority of the xylooligosacharides (DP2-4) products was xylobiose (61.5%). The thermostable xylanase (XynNF) thus seems potentially usefull in the production of xylooligosaccharides.

• Journal of Microbiology and Biotechnology
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• 제12권2호
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• pp.306-311
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• 2002

O-linked N-acetylglucosamine (O-GlcNAc) is an abundant posttranslationally modified compound in eukaryotic cells. Human O-GlcNAc transferase (OGT) was produced as a maltose binding protein (MBP) fusion protein, which showed significant catalytic activity to modify recombinant Sp1, transcription factor. To facilitate the production of O-GlcNAc modified proteins, instead of using the tedious in vitro glycosylation reaction or expression in eukaryotic cells, a MBP-fusion OGT expression vector (pACYC184-MBPOGT) was constructed using pACYC184 plasmid, which could coexist with general prokaryotic expression vectors containing ColE1 origin. By cotransforming pACYC184-MBPOGT and pGEX-2T vectors into Escherichia coli BL21, intracellular O- GlcNAcylated proteins could be obtained by a simple purification procedure. It is expected that this may be a useful tool for production of O-GlcNAc modified proteins.