• 제목/요약/키워드: Acidic optimum pH

검색결과 126건 처리시간 0.028초

Aspergillus niger의 Acidic Nucleotidase의 특성 (Characterization of Acidic Nucleotidase from Aspergillus niger)

  • 김기남;박인식
    • 한국미생물·생명공학회지
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    • 제20권1호
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    • pp.40-45
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    • 1992
  • Aspergillus niger로부터 acidic nucleotidase를 Sepharose CL-6B gel 여과와 DEAE-Sephacel 이온교환수지를 이용하여 부분정제하였다. 5'-AMP 와 3'-AMP를 기질로 사용했을 경우에 효소의 최적 pH는 4.5, 그리고 최적온도는 $55^{\circ}C$였다. 그러나, p-nitrophenyl phosphate를 기질로 사용했을 경우에는 최적 pH는 변화가 없었으나, 최적 온도는 $70^{\circ}C$였다. 효소의 활성화에너지는 3'-AMP, 5'-AMP 그리고 p-nitrophenyl phosphate를 기질로 사용했을 경우에 각각 4.76kcal/mole, 6.95kcal/mole 그리고 11.82kcal/mole 였다.

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Two-Stage Fermentation for 2-Ketogluconic Acid Production by Klebsiella pneumoniae

  • Sun, Yuehong;Wei, Dong;Shi, Jiping;Mojovic, Ljiljana;Han, Zengsheng;Hao, Jian
    • Journal of Microbiology and Biotechnology
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    • 제24권6호
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    • pp.781-787
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    • 2014
  • 2-Ketogluconic acid production by Klebsiella pneumoniae is a pH-dependent process, strictly proceeding under acidic conditions. Unfortunately, cell growth is inhibited by acidic conditions, resulting in low productivity of 2-ketogluconic acid. To overcome this deficiency, a two-stage fermentation strategy was exploited in the current study. During the first stage, the culture was maintained at neutral pH, favoring cell growth. During the second stage, the culture pH was switched to acidic conditions favoring 2-ketogluconic acid accumulation. Culture parameters, including switching time, dissolved oxygen levels, pH, and temperature were optimized for the fed-batch fermentation. Characteristics of glucose dehydrogenase and gluconate dehydrogenase were revealed in vitro, and the optimal pHs of the two enzymes coincided with the optimum culture pH. Under optimum conditions, a total of 186 g/l 2-ketogluconic acid was produced at 26 h, and the conversion ratio was 0.98 mol/mol. This fermentation strategy has successfully overcome the mismatch between optimum parameters required for cell growth and 2-ketogluconic acid accumulation, and this result has the highest productivity and conversion ratio of 2-ketogluconic and produced by microorganism.

산과 알칼리 pH에서 어육 단백질의 용해를 이용한 수리미 제조 (Surimi Processing Using Acid and Alkali Solubilization of Fish Muscle Protein)

  • 박주동;정춘희;김진수;조득문;조민성;최영준
    • 한국식품영양과학회지
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    • 제32권3호
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    • pp.400-405
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    • 2003
  • 산과 알칼리 수리미 제조공정을 확립하기 위하여 단백질 가용화와 회수를 위한 최적 pH, 이온강도의 영향, 균질화 조건, 마쇄육에 대한 수도수의 비 및 수율을 검토하고, 산 및 알칼리 수리미 공정에 따른 폐수의 오염 저감 효과를 수세수리미와 비교하였다. 어육 단백질을 추출하기 위한 최적 pH는 2.5와 10.5부근이었으며, 가용성 단백질의 침전 회수를 위한 최적 pH는 5.0 부근이었다. 추출 용액의 이온강도 증가는 어육 단백질의 추출량을 현저히 감소시키는 것으로 나타났고, 균질화를 위한 최적 조건은 9500 rpm 이하에서 30초였다. 원심분리 부하량과 파괴강도 및 변형값을 고려한 최적수량은 어육에 대하여 6배량이었다. 산 혹은 알칼리 공정의 수리미 수율은 수세 공정에 비하여 높았으며, 폐수의 오염 부하량은 현저히 낮은 것으로 나타났다.

목질계 셀룰로오스 에탄올 생산공정에서 전처리과정의 설계 (Design of Pretreatment Process in Cellulosic Ethanol Production)

  • 김형진;이승범
    • 공업화학
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    • 제26권4호
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    • pp.511-514
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    • 2015
  • 차세대 바이오에탄올로 주목받고 있는 목질계 바이오매스를 이용한 셀룰로오스 에탄올 생산과정은 셀룰로오스를 단당류로 분해하는 전처리과정이 가장 중요한 역할을 한다. 본 연구에서는 산가수분해와 효소당화과정을 이용하여 볏짚, 톱밥, 복사지, 신문지 등과 같은 목질계 바이오매스로부터 셀룰로오스에탄올을 제조하였다. 전처리과정으로 10~30 wt% 황산을 이용한 산가수분해($100^{\circ}C$, 1 h), celluclast ($55^{\circ}C$, pH = 5.0), AMG ($60^{\circ}C$, pH = 4.5), spirizyme ($60^{\circ}C$, pH = 4.2)을 이용한 효소당화과정(30 min), 산가수분해 후 효소당화과정을 비교하였다. 전처리과정의 수율은 hybrid 과정 > 산가수분해 > 효소당화 순으로 셀룰로오스 에탄올로의 전환이 잘 이루어지는 것으로 나타났으며, 최적 발효시간은 2일이었다. 또한 20 wt% 황산을 이용한 산가수분해 후 celluclast를 이용하여 효소당화를 수행할 경우 톱밥 > 볏짚 > 복사지 > 신문지 순으로 셀룰로오스 에탄올 전환특성이 높게 나타났다.

중금속 산폐수 처리 후의 상등액을 이용한 염색폐수처리 연구 (A Study on the Treatment of Dyeing Wastewater Using the Supernatant after Treatment of Acidic Metal Wastewater)

  • 신진명;박장진;김미자;주소영
    • 환경위생공학
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    • 제18권1호
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    • pp.41-50
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    • 2003
  • Traditionally the supernatant after chemical treatment of metal acid wastewater is discharged in environment. The supernatant can be used as a coagulant as it contains effective metals. The aim of this study is to investigate the feasibility of treatment of dyeing wastewater using the supernatant after treatment by magnesium hydroxide and dolomite($Ca{\cdot}Mg(CO_3)_2$), of acidic metal wastewater. In dyeing wastewater treatment with the supernatant, optimum pH and dosage were determined. COD, turbidity and color were analyzed to evaluate the performance of treatment. In the case of magnesium hydroxide, the optimum dosage was 10%(v/v) for supernatant A and 3%(v/v) for supernatant B. Color, turbidity and COD removal was 99~100%, 85~97% and 43~53%, respectively. In the case of dolomite, the optimum dosage was 10%(v/v) for supernatant A and 3% for supernatant B. Color, turbidity and COD removal was 96~99%, 62~9l% and 52~53%, respectively.

A study of ribonuclease activity in venom of vietnam cobra

  • Nguyen, Thiet Van;Osipov, A.V.
    • Journal of Animal Science and Technology
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    • 제59권9호
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    • pp.20.1-20.9
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    • 2017
  • Background: Ribonuclease (RNase) is one of the few toxic proteins that are present constantly in snake venoms of all types. However, to date this RNase is still poorly studied in comparison not only with other toxic proteins of snake venom, but also with the enzymes of RNase group. The objective of this paper was to investigate some properties of RNase from venom of Vietnam cobra Naja atra. Methods: Kinetic methods and gel filtration chromatography were used to investigate RNase from venom of Vietnam cobra. Results: RNase from venom of Vietnam cobra Naja atra has some characteristic properties. This RNase is a thermostable enzyme and has high conformational stability. This is the only acidic enzyme of the RNase A superfamily exhibiting a high catalytic activity in the pH range of 1-4, with $pH_{opt}=2.58{\pm}0.35$. Its activity is considerably reduced with increasing ionic strength of reaction mixture. Venom proteins are separated by gel filtration into four peaks with ribonucleolytic activity, which is abnormally distributed among the isoforms: only a small part of the RNase activity is present in fractions of proteins with molecular weights of 12-15 kDa and more than 30 kDa, but most of the enzyme activity is detected in fractions of polypeptides, having molecular weights of less than 9 kDa, that is unexpected. Conclusions: RNase from the venom of Vietnam cobra is a unique member of RNase A superfamily according to its acidic optimum pH ($pH_{opt}=2.58{\pm}0.35$) and extremely low molecular weights of its major isoforms (approximately 8.95 kDa for RNase III and 5.93 kDa for RNase IV).

원수 탁도와 pH 변화가 혼화응집침전 과정에서 원생동물과 탁질 제거에 미치는 영향 (The Effects of Turbidity and pH on the Removal of Cryptosporidium and Giardia by Coagulation Process)

  • 정현미;박상정
    • 상하수도학회지
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    • 제20권1호
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    • pp.71-78
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    • 2006
  • The removal of protozoa in the coagulation process was evaluated under the different pH and turbidity using the jar test after the addition of polyaluminium chloride (PAC) as a coagulant. Two well-known protozoa of Cryptosporidium parvum and Giardia lamblia were tested at the same time with turbidity, the critical water quality parameter of the water treatment process. Both protozoa were removed about 1log (and up to 2log) at the optimum injection of PAC. The source water turbidity and pH affected the removal of protozoa and turbidity. At neutral and alkaline pH, 1.3-1.7log removal of protozoa for low turbid water with 5NTU, and 1.6-2.3log removal for high turbid water with 30NTU were achieved. However, at acidic pH, maximum 0.8-1.0log and 1.1-1.2log were removed for low and high turbid water, respectively, at the optimum PAC injection of 15mg/L. The relation of protozoa and turbidity removals were expressed as the 1st order equation (significantly positive relation) in the most of the tested conditions. In addition, the relation of protozoan removals with residual turbidity were also expressed the 1st order equation (significantly negative relation), although the significance of the equations were reduced at acidic pH. Therefore, residual turbidity could be a good index of efficient protozoan removal in the coagulation process, probably except at the low pH condition.

Changes in Optimum pH and Thermostability of $\alpha$-amylase from Bacillus licheniformis by Site-directed Mutagenesis of His 235 and Asp 328

  • Kim, Mi-Sook;Lee, Sang-Kyou;Jung, Han-Seung;Yang, Chul-Hak
    • Bulletin of the Korean Chemical Society
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    • 제15권10호
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    • pp.832-835
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    • 1994
  • The ${alpha}$-amylase gene of Bacillus licheniformis has been cloned and two mutant ${alpha}$-amylase genes of which histidine 235 was changed to glutamine (H235Q) and aspartic acid 328 to glutamic acid (D328E) have been produced by site-directed mutagenesis. The kinetic parameters, optimum pH and thermostability of wild type(WT) and these two mutant amylases expressed in E. coli MC1061 have been compared after purification. The $K_m$ values of WT, H235Q and D328E ${alpha}$-amylases were 0.22%, 0.73%, and 0.80% respectively, when using starch as the substrate. The $V_max$ values of wild type ${alpha}$ -amylase and mutant ${alpha}$-amylases were 0.6-0.7%/minute, and did not show any significant differences among them. The optimum pH of D328E ${alpha}$-amylase was shifted to more acidic pH. Also, the thermostability of H235Q ${alpha}$-amylase was increased compared to the wild type ${alpha}$-amylase.

섬유소분해균의 분리 및 그의 생리학적 특성 (Isolation of Cellulolytic Microorganisms and their Physiological Characteristics)

  • 홍순우;하영칠;민경희;이영하
    • 미생물학회지
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    • 제14권1호
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    • pp.17-24
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    • 1976
  • Celluloytic microorgnasims were isolated form the various sources and four of them were identified as Trichoderma roningi, Aspergillus niger, Penicillium chrysogenum, and Streptomyces sp. The induction of extracellular5 cellulase of these species in the liquid culture media containing carboxymethylcellulose (CMC) or Avicel as inducer showed that CMC was a better effective inducer for the production of CMCase(Cx cellulase component) as well as Avicelase(C$_{1}$ cellulase component) than Avicel. It is believed that certain hydrolysis products of cellulose(CMC) could serve as an inducer for an enzyme synthesis. In T. roningi, Asp. niger, and Strptomyces sp., the optimum temperature of CNCase on CMC-culture medium was 50.deg. but temperature around 40.deg.C was found to be optimum for the activities of CMCase prepared from P.ehrysogenum. The optimum temperature for Avicelase activitiles on Avicel-culture media of T. roningi and P. chrysogenum was $40{\circ}C$ whereas temperature $50{\circ}C$ was found to be optimum for Avicelase from A.niger and Streptomyces sp. The optimal activities of these CNCase and Avicelase prepared from. T. ronigi, Pen.chrysogenum and Streptomyces sp. were found similarly to be at pH's around 5.4 and 6.0 while pH 4.8 was optimum for the activities of CMCase and Avicelase from A.niger, indicating that A.niger in acidic media would yield an enzyme of high activity.

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Studies on The Lypolitic Enzymes of Carum Roxburgllianum Seed Meal

  • Mahmud, Shahid;Waheed, Amran;Khanum, Razia
    • Natural Product Sciences
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    • 제10권6호
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    • pp.302-305
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    • 2004
  • The lipase and phospholipase activities of meals of resting seeds of C. roxburghianum were studied at different temperatures, solvents and pH. Both the enzymes showed the maximum activities at $40^{\circ}C$ and in n-heptane used as solvent. However, lipase showed maximum activities at two different pH, one at pH 5 (acidic) and other at pH 8 (alkaline) whereas phospholipase showed only one pH optimum at pH 8. During the course of germination, the lipase showed an increase whereas reverse was the case with phospholipase.