• 제목/요약/키워드: Soil enzyme activity

검색결과 405건 처리시간 0.024초

Isolation and Characterization of Soil Strains Producing Glutaryl-7-Aminocephalosporanic Acid Acylase

  • Knang, Yong-Ho;Yoo, Ryong-Hoon
    • Biotechnology and Bioprocess Engineering:BBE
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    • 제2권2호
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    • pp.105-108
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    • 1997
  • A search was undertaken to screen microorganisms that produce an enzyme capable of deacylating glutary1-7-amincephalosporanic acid to 7-aminocephalosporanic acid in soil samples. The screening was carried out by preparing enrichment cultures containing glutary-7ACA and cephalosporin C as selective carbon sources. A non-${\beta}$-lactam model compound,, glutary-p-nitroanilide, was synthesized as a substrate suitable for the rapid screening of microorganisms isolated from the enrichment cultures. Two isolates exhibiting acylase activity, designated BY7.4 and BY8.1, were identified as strains of Pseudomonas species. Pseudomonas BY8.1 showed higher acylase activity toward G1-7ACA than Pseudomonas BY7.4. Environmental conditions for the optimal acylase activity of Pseudomonas BY8.1 were shown to be pH9 and 30$^{\circ}C$.

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Characterization of Kinetics of Urea Hydrolysis in A Newly Reclaimed Tidal Soils

  • Kim, Hye-Jin;Park, Mi-Suk;Woo, Hyun-Nyung;Kim, Gi-Rim;Chung, Doug-Young
    • 한국토양비료학회지
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    • 제44권1호
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    • pp.84-90
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    • 2011
  • It is imperative to study the hydrolysis of urea in high saline-sodic condition of a newly reclaimed tidal land in order to overcome the problems associated with use of urea fertilizer. The methodology adopted in this study tried to get a convenient way of estimating rate for N transformation needed in N fate and transport studies by reviewing pH and salt contents which can affect the microbial activity which is closely related to the rate of urea hydrolysis. The hydrolysis of urea over time follows first-order kinetics and soil urease activity in reclaimed soils will be represented by Michaelis-Menten-type kinetics. However, high pH and less microorganisms may delay the hydrolysis of urea due to decrease in urease activity with increasing pH. Therefore, the rate of urea hydrolysis should adopt $V_{max}$ referring enzyme activity ($E_0$) accounting for urease concentration which is indicative for urea hydrolysis, especially in a high saline and sodic soils.

An Immobilization of Extracellular Laccase to Humus-Iron Complex

  • Ginalska, Grazyna;Cho, Nam-Seok;Lobarzewski, Jerzy;Piccolo, Alessandro;Leonowicz, Andrzej
    • Journal of the Korean Wood Science and Technology
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    • 제29권3호
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    • pp.104-111
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    • 2001
  • There are some evidence that active enzymatic proteins, e.g. fungal laccase, exist in the naturally occured soil humus. This study was performed to investigate the covalent binding of fungal laccase to the humic acid-iron complex, and to measure laccase activity of immobilized ones. Seven methods were adopted to form the covalent binding of fungal laccase with soil humic acids complexed with iron. Using these seven methods it was possible to change the dimension of spacer arm between laccase and support, and also to regulate the mode of covalent binding of this enzyme. The spacer arm was regulated from 2C to 11C. There was not observed any straight relationship between the spacer arm longitude and the laccase activity after immobilization, but the binding mode more effective than the former. Three out of the seven methods gave the high activity of immobilized laccase, and which active products of laccase immobilization was stable up to 10 days after the process. It is indicated that natural soil condition might be prevented the laccase activation by the toxic influence of some phenolic humic compounds. It was shown, for the first time, the possibilities to obtain the high activity of fungal laccase by binding to humic acids, and especially in complex with iron.

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응유효소를 생산하는 Mucor mucedo C-7의 분리 및 동정 (Isolation and Identification of Mucor mueedo C-7 for Producing The Milk-clotting Enzyme)

  • 조재민;이웅수;김교창
    • 한국미생물·생명공학회지
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    • 제18권5호
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    • pp.449-453
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    • 1990
  • 대용응유효소를 생산하는 균주를 선별하기 위해 토양, 건초, 퇴비 등 114시료를 분리원으로 하여 응유효소를 생산하는 16균주를 분리하였으며 이들 각 균주들이 생산하는 유응고력과 단백질 분해력의 비는 균주번호 C-7 것이 1,929로 가장 좋았다. C-7 균주의 균사는 회백색으로 격막이 없었고 포자낭병은 균사로부터 단독으로 곧게 뻗어 갈라지지 않은 monomucor형으로 그 끝은 구형의 포자낭을 형성하였으며 적합한 생육온도와 생육 pH의 범위는 20-$30^{\circ}C$, pH 3.0-8.0이었다. 형태적, 생리적 여러 특성에 따라 C-7 균주는 Mucor mucedo로 동정되었다.

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Purification and Characterization of the Lipase from Acinetobacter sp. B2

  • Sohn, Sung-Hwa;Park, Kyeong-Ryang
    • Molecular & Cellular Toxicology
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    • 제1권3호
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    • pp.189-195
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    • 2005
  • Industrial development has increase consumption of crude oil and environmental pollution. A large number of microbial lipolytic enzymes have been identified and characterized to date. To development for a new lipase with catalytic activity in degradation of crude oil as a microbial enzyme, Acinetobactor sp. B2 was isolated from soil samples that were contaminated with oil in Daejon area. Acinetobactor sp. B2 showed high resistance up to 10 mg/mL unit to heavy metals such as Ba, Li, Al, Cr, Pb and Mn. Optimal growth condition of Acinetobactor sp. B2 was confirmed $30^{\circ}C$. Lipase was purified from the supernatant by Acinetobactor sp. B2. Its molecular mass was determined to the 60 kDa and the optimal activity was shown at $40^{\circ}C$ and pH 10. The activation energies for the hydrolysis of p-nitrophenyl palmitate were determined to be 2.7 kcal/mol in the temperature range 4 to $37^{\circ}C$. The enzyme was unstable at temperatures higher than $60^{\circ}C$. The Michaelis constant $(K_{m})\;and\;V_{max}$ for p-nitrophenyl palmitate were $21.8{\mu}M\;and\;270.3{\mu}M\;min^{-1}mg\;of\;protein^{-1}$, respectively. The enzyme was strongly inhibited by $Cd{2+},\;Co^{2+},\;Fe^{2+},\;Hg^{2+},\;EDTA$, 2-Mercaptoethalol. From these results, we suggested that lipase purified from Acinetobactor sp. B2 should be able to be used as a new enzyme for degradation of crude oil, one of the environmental contaminants.

Effect of cyclodextrin glucanotransferase enzyme in biodegradation of diesel oil

  • Sivaraman, C.;Ganguly, Anasuya;Mutnuri, Srikanth
    • Advances in environmental research
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    • 제1권2호
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    • pp.97-108
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    • 2012
  • Microbial degradation of hydrocarbons is found to be an attractive process for remediation of contaminated habitats. However the poor bioavailability of hydrocarbons results in low biodegradation rates. Cyclodextrins are known to increase the bioavailability of variety of hydrophobic compounds. In the present work we purified the Cyclodextrin Glucanotransferase (CGTase) enzyme which is responsible for converting starch into cyclodextrins and studied its role on biodegradation of diesel oil contaminated soil. Purification of CGTase from Enterobacter cloacae was done which resulted in 6 fold increase in enzyme activity. The enzyme showed maximum activity at pH 7, temperature $60^{\circ}C$ with a molecular weight of 66 kDa. Addition of purified CGTase to the treatment setup with Pseudomonas mendocina showed enhanced biodegradation of diesel oil ($57{\pm}1.37%$) which was similar to the treatment setup when added with Pseudomonas mendocina and Enterobacter cloacae ($52.7{\pm}6.51%$). The residual diesel oil found in treatment setup added with Pseudomonas mendocina at end of the study was found to be $73{\pm}0.21%$. Immobilization of Pseudomonas mendocina on alginate containing starch also led to enhanced biodegradation of hydrocarbons in diesel oil at 336 hours.

세포외 5-Fluorocytosine Deaminase의 특성 (Properties of an Extracellular 5-Fluorocytosine Deaminase)

  • 이인;전홍기;윤용균
    • 한국미생물·생명공학회지
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    • 제20권2호
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    • pp.150-155
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    • 1992
  • 토양 분리 균주로부터 얻은 배양액을 20-80 황산암모늄으로 분획한 후 세포의 cytosine deaminase의 성질을 검토하였다. 이 효소는 cytosine과 5-fluorocytosine(5-FC)에 기질 특이성을 가짐으로서 각각 uracil과 5-fluorouracil(5-FU)로 전환을 촉매하였다. 효소안정성에 대한 온도와 보존기간은 tris-HC1 완충용액에서 검토한 결과 최적온도는 $50^{\circ}C$ 부근이하에서 90 이상의 잔존활성을, 보존시간은 4일정도에서 80 이상의 잔존활성을 유지하였다. 최대 pH 8.0과 $37^{\circ}C$의 온도에서 나타났다. 활성에 적당한 pH는 8.0~8.5였고, 온도는 37~$45^{\circ}C$의 범위였다.

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알칼리성 Prottease를 생산하는 Xanthomonas sp. YL-37의 분리 및 조효소의 성질 (Production and Characterization of ans Alkaline Protease from an Isolate,Xanthomonas sp.YL-37)

  • 이창호;권태종;강상모;서현효;권기석;오희목;윤병대
    • 한국미생물·생명공학회지
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    • 제22권5호
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    • pp.515-521
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    • 1994
  • A bacterial strain, which showed the high protease activity at low temperature and the high tolerance for the surfactant, was isolated from soil and identified as Xanthomonas sp. YL-37. The optimal temperature, initial pH, and cultivation time for the production of the alkaline protease by Xanthomonas sp. YL-37 were 20$\circC , 11.0, and 84 hours, respectively. In the jar fermenter culture of Xanthomonas sp. YL-37, the alkaline protease activity was about 15,000 DU/ml/-broth after cultivating for 108 hours. The optimal pH and temperature for the protease activity were 70$\circC and 11.0, respectively. The protease was relatively stable at the pH range of 7.0~12.0 and at the temperatures below 50$\circC . The protease activity at 20$\circC was about the level of 40% of its activity at 70$\circC . The enzyme was suggested as a serine protease because the enzyme activity was inhibited by phenylmethane sulfonyl fluoride, a serine modifier.

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Long-term effects of ZnO nanoparticles on exoenzyme activities in planted soils

  • Kwak, Jin Il;Yoon, Sung-Ji;An, Youn-Joo
    • Environmental Engineering Research
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    • 제22권2호
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    • pp.224-229
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    • 2017
  • Zinc oxide nanoparticles (ZnO NPs) have been used as additives in a variety of consumer products. While these particles may enter the environment, only a limited number of studies have investigated the effects of ZnO NPs on soil exoenzymes. Here, we investigate the long-term effects of ZnO NPs at concentrations of 50 and 500 mg/kg on the activities of six soil exoenzymes in planted soils: Dehydrogenase, fluorescein diacetate (FDA) hydrolase, urease, acid phosphatase, arylsulfatase, and ${\beta}-glucosidase$. Significant effects were observed at one or more time points for all enzymes except for FDA hydrolase. These effects included both decreases and increases in enzyme activity. Our results suggest that ZnO NP treatments of 50 and 500 mg/kg can adversely affect soil enzymes, particularly acid phosphatase and urease, and thus, these data may have implications for phosphorous and nitrogen cycles in the soil.

두유 응고효소 생산 곰팡이의 분리 및 동정 (Isolation and Identification of the Fungi Producing a Soybean Milk Clotting Enzyme)

  • 이철우;강창훈;하덕모
    • 한국미생물·생명공학회지
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    • 제19권2호
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    • pp.109-115
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    • 1991
  • Twenty-five fungal strains producing an extracellular soybean milk clotting enzyme were isolated from 146 soil samples, and identified as 11 species belonging to six genera of Aspergillus oryzae (5 strains), Aspergillus flavus (2 strains), Aspergillus parasiticus (1 strain), Aspergillus tamarii (2 strains), Aspergillus niger (4 strains), Aspergillus fumigatus (2 strains), Mucor hiemalis (2 strains), Wallemia sebi (4 strains), Scopulariopsis condida (1 strain), Fusarium redolens(1 strain) and Verticillum lecanii (1 strain). Among them, Aspergillus oryzae 020 and Aspergillus tamarii 287 showed relatively high soybean milk clotting activity. The coagulabilities of the enzyme from representative strains of those species decreased as the pH of soybean milk increased from 6.0 to 7.0 The optimum temperature for soybean milk clotting enzymes of those strains were 65$^{\circ}C$.

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