• Title/Summary/Keyword: microbial enzyme

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The Succession of Microbial Populations and Variation of Enzyme Activities in Composting of Apple Pomace (사과박 퇴비화에서의 미생물군집의 천이와 효소활성도의 변화)

  • Lee, Yong-Ok;Jo, Ik-Hwan;Lee, Yong-Se;Jun, Ha-Joon
    • Journal of the Korea Organic Resources Recycling Association
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    • v.7 no.2
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    • pp.73-82
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    • 1999
  • To verify the usefulness of enzyme activity as a index for the stability or maturity of apple pomace composting. the succession of microbial populations using viable count procedure. and Vmax of ${\beta}$-glucosidase and cellobiohydrolase were measured. based on an increase in fluorescence as the nonfluorescent methylumbelliferyl substrates were enzymatically hydrolyzed, leading to the highly fluorescent methylumbelliferyl molecule 4-methylumbelliferone(MUF). The activities of these enzymes in the decomposition of carbohydrates were gradually decreased in the course of the time. Correlation between microbial population and enzyme activity was not significant with exception of fungi. and the fungi were represented in high density. This indicates that the fungi probably play a major role in composting of apple pomace.

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Purification of Progelatinase A (Matrix Metalloproteinase 2) and a Tissue Inhibitor of Metalloproteinase-2(TIMP-2) from T98G Human Glioblastoma Cells

  • Lee, Ho-Jae;Chung, Myung-Chul;Lee, Choong-Hwan;Chun, Hyo-Kon;Kho, Yung-Hee
    • BMB Reports
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    • v.28 no.1
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    • pp.33-39
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    • 1995
  • The Gelatinases (typeIV collagenases) are metalloproteinases that may play an important role in tumor invasion and metastasis. Progelatinase A was purified from a conditioned medium of T98G human glioblastoma cells. TIMP-2 complexed progelatinase A and free progelatinase A were separated by heparin affinity HPLC. The final product was homogeneous on SDS-PAGE, with a molecular weight of 64,000 daltons without reduction. TIMP-2 and free progelatinase A were separated from TIMP-2 complexed progelatinase A by reverse-phase HPLC in the presence of trifluoroacetic acid. TIMP-2 complexed progelatinase A was resistant to activation by p-aminophenyl mercuric acetate (APMA), and showed less than 20% of the activity of the TIMP-2 free active enzyme. TIMP-2 free progelatinase A was easily activated to the mature form with a molecular weight of 57,000 daltons by APMA and showed high activity compared to the TIMP-2 complexed enzyme.

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Effect of Different Pretreatment Methods on the Bioconversion of Rice Bran into Ethanol

  • Eyini, M.;Rajapandy, V.;Parani, K.;Lee, Min-Woong
    • Mycobiology
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    • v.32 no.4
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    • pp.170-172
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    • 2004
  • The efficiency of acid, enzyme and microbial pretreatment of rice bran was compared based on the content of cellulose, hemicellulose, reducing sugars and xylose in the substrate. An isolate of Aspergillus niger or a strain of Trichoderma viride(MTCC 800) was employed for microbial pretreatment of rice bran in solid state. Acid pretreatment resulted in the highest amount of reducing sugars followed by enzyme and microbial pretreatment. A. niger showed a higher rate of hydrolysis than T. viride. The rice bran hydrolysate obtained from the different methods was subsequently fermented to ethanol either by Zymomonas mobilis(NCIM 806) or by Pichia stipitis(NCIM 3497). P. stipitis fermentation resulted in higher ethanol(37% higher) and biomass production($76{\sim}83%$ higher) than those of Z. mobilis. Maximum ethanol production resulted at 12h in Zymomonas fermentation, while in Pichia fermentation, it was observed at 60h. Microbial pretreatment of rice bran by A. niger followed by fermentation employing P. stipitis was more efficient but slower than the other microbial pretreatment and fermentation.

Characteristics of Microbial Community Enzyme Activity and Substrate Availability of Damaged Soil (훼손 토양의 미생물군집 효소 활성과 기질 이용성 특성)

  • Ji Seul Kim;Gyo-Cheol Jeong;Myoung Hyeon Cho;Eun Young Lee
    • Journal of Soil and Groundwater Environment
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    • v.28 no.5
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    • pp.68-77
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    • 2023
  • The effect of soil damage on the physicochemical characteristics and activity of the soil microbial community is not well known. This study investigates this relationship by analyzing 11 soil samples collected from various points of soil damage across Gyeonggi-do. Soil damage resulted from forest fires, landslides, and development areas, with their impacts most severe on the topsoil layer (0-30 cm). Dehydrogenase and β-glucosidase activities were notably higher at locations damaged by forest fires compared to other sites. While enzyme activities in soils influenced by landslides and development areas were relatively low, sites with a pollution history exhibited elevated dehydrogenase activity, likely due to past microbial response to the pollution. Additionally, an assessment of carbon substrate usability by soil microorganisms indicated higher substrate availability in areas impacted by forest fires, contrasting with lower availability in landslide and development sites. Statistical analysis revealed a positive correlation between organic content of sand and clay and microbial activity. These findings provide valuable insights into soil damage and associated restoration research, as well as management strategies.

Secretory Expression, Functional Characterization, and Molecular Genetic Analysis of Novel Halo-Solvent-Tolerant Protease from Bacillus gibsonii

  • Deng, Aihua;Zhang, Guoqiang;Shi, Nana;Wu, Jie;Lu, Fuping;Wen, Tingyi
    • Journal of Microbiology and Biotechnology
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    • v.24 no.2
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    • pp.197-208
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    • 2014
  • A novel protease gene from Bacillus gibsonii, aprBG, was cloned, expressed in B. subtilis, and characterized. High-level expression of aprBG was achieved in the recombinant strain when a junction was present between the promoter and the target gene. The purified recombinant enzyme exhibited similar N-terminal sequences and catalytic properties to the native enzyme, including high affinity and hydrolytic efficiency toward various substrates and a superior performance when exposed to various metal ions, surfactants, oxidants, and commercial detergents. AprBG was remarkably stable in 50% organic solvents and retained 100% activity and stability in 0-4 M NaCl, which is better than the characteristics of previously reported proteases. AprBG was most closely related to the high-alkaline proteases of the subtilisin family with a 57-68% identity. The secretion and maturation mechanism of AprBG was dependent on the enzyme activity, as analyzed by site-directed mutagenesis. Thus, when taken together, the results revealed that the halo-solvent-tolerant protease AprBG displays significant activity and stability under various extreme conditions, indicating its potential for use in many biotechnology applications.

Potential Industrial Applications and Evolution of Carbohydrolases and Glycansucrases

  • Kim, Do-Man;Seo, Eun-Seong;Lee, Jin-Ha;Kang, Hee-Kyoung;Cho, Jae-Young
    • Proceedings of the Korean Society for Applied Microbiology Conference
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    • 2004.06a
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    • pp.215-218
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    • 2004
  • Dextrans make up a class of polysaccharides that are D-glucans of various structures with contiguous $\alpha$-1longrightarrow6 ~6 glycosidic linkages in the main chains and $\alpha$-1longrightarrow2, $\alpha$-1longrightarrow3, or $\alpha$-1longrightarrow4 branch glycosidic linkages, depending on the specificity of the particular dextransucrase. Glucansucrases that catalyze glucans synthesis from sucrose. When other carbohydrates, in addition to sucrose, are present in the enzyme digest, the enzyme transfers glucose to the carbohydrate acceptors in the secondary reaction that diverts some of the glucose from incorporation into glucan. Many carbohydrate acceptors have been recognized and the products that result are dependent on the particular enzyme and the structure of the particular acceptor. Because of these unique catalytic characteristics, various dextransucrases have many important industrial and medical uses. To improve the understanding of their action mode and extend their applications, this study describes mechanism of glucan synthesis and potential industrial uses of dextransucrases, and our recent findings on the structural, functional organization and directed evolution of the glucansucrases to offer for designing glucansucrases with improved properties.

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Inhibitory Activity against Protein Kinase C of Some Medicinal Plants (수종 생약의 Protein kinase C 저해활성)

  • Lee, Hyun-Sun;Ahn, Soon-Cheol;Kim, Bo-Hyun;Park, Moon-Su;Oh, Won-Keun;Yoon, Byung-Dae;Ahn, Jong-Seog;Mheen, Tae-Ick
    • Korean Journal of Pharmacognosy
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    • v.23 no.3
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    • pp.142-145
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    • 1992
  • MeOH extract of twenty medicinal herbs were screened for their effects against protein kinase C (PKC) using bleb-forming assay and PKC enzyme assay. Smilax china and Sanguisorba officinalis showed potent anti-PKC activity. Campsis grandiflora and Galla Halepensis showed moderate inhibitory effect on PKC.

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Relation between Chemical Properties and Microbial Activities in Soils from Reclaimed Tidal Lands at South-western Coast Area in Korea

  • Park, Mi-Na;Go, Gang-Seuk;Kim, Chang-Hwan;Bae, Hui-Su;Sa, Tongmin;Choi, Joon-Ho
    • Korean Journal of Soil Science and Fertilizer
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    • v.48 no.4
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    • pp.262-270
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    • 2015
  • The scientific information between microbial community and chemical properties of reclaimed tidal soil is not enough to understand the land reclamation process. This study was conducted to investigate the relation between chemical properties and microbial activities of soils from reclaimed tidal lands located at south-western coastal area (42 samples from Goheuong, Samsan, Bojun, Kunnae, Hwaong and Yeongsangang sites). Most of the reclaimed soils showed chemical characteristics as salinity soil based on EC. Only $Na^+$ in exchangeable cation was dependent on EC of reclaimed soil, whereas other cations such as $K^+$, $Ca^{2+}$, and $Mg^{2+}$ were independent on EC. The mesophilic bacteria decreased with an increase in EC of soil. Microbial population increased with soil organic content in the range of $0{\sim}10g\;kg^{-1}$ and dehydrogenase activity less than $100{\mu}g-TPF\;g^{-1}h^{-1}$. Microbial population of soils from reclaimed tidal lands was closely related to the microbial community containing hydrolytic enzyme activities of cellulase, amylase, protease, and lipase.

Purification and characterization of an alkaline protease produced by a xanthomonas sp. YL-37

  • Lee, Chang-Ho;Kim, Hee-Sik;Seok, Kwon-Gi;Oh, Hee-Mock;kang sang mo;Kwon, Tae-Jong;Yoon, Byung-Dae
    • Journal of Microbiology
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    • v.33 no.2
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    • pp.115-119
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    • 1995
  • The alkaline protease of Xanthomonas sp. YL-37 has been purified, and the properties of the enzyme investigated. The alkaline protease of Xanthomonas sp. YL-37 was purified form crude enzyme by ammonium sulfate fractionation, CM-cellulose ion exchange chromatography, and Sephadex G-100 gel filtration. Through the series of chromatographies, the enzyme was purified to homogenecity with specific activity of 4.23 fold higher than that of the crude broth. The molecular weight of the purified protease has been estimated to be 62 KDa on SDS-polyacrylamide gel electrophoresis. The optimal pH and temperature for alkaline protease activity were 11.0 and 50.deg.C, respectively. The enzyme was stable between pH 5.0 and 10.0 and up to 50.deg.C. Enzyme activity was lost up to 50% on heating at 70.deg.C for 30 minutes. The activity of alkaline protease was inhibited by Cu$\^$2+/, Zn$\^$2+/, Hg$\^$2+/, PMSF, and activated by Mn$\^$2+/ and Ca$\^$2+/. The $K_{m}$ value for casein as a substrate was 4.0 mg/ml.

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Purification and Characterization of a Cytochrome P-450 from Pravastatin-Producing Streptomyces sp. Y-110.

  • Park, Joo-Woong;Lee, Joo-Kyung;Kwon, Tae-Jong;Yi, Dong-Hee;Park, Yong-Il;Kang, Sang-Mo
    • Journal of Microbiology and Biotechnology
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    • v.11 no.6
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    • pp.1011-1017
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    • 2001
  • Streptomyces sp. Y-110 cytochrome P-450, induced by the addition of compactin -Na into the culture medium, was purified from the cell extract to apparent homogeniety, mainly by DEAE-Sepharose, hydroxyapatite, and Mono Q column chromatyography. The sepcific activity of purified enzyme on its substrate, compactin-Na, was determined to be 15 nmol of pravastatin per mg protein. The molecular mass of this enzyme on SDS-PAGE was $37{\pm}0.5$ kDa, pI was 4.5, and its CO difference spectrum showed maximum absorption peaks at 452 and 550nm, respectively. The N-terminal amino acid sequence was determined to be Met>Thr>Cys>Thr>Pro>Val>Thr>Val>The>Gly>Ala>Ala>Gly>Gln>Ile>Gly>Tyr>Ala>Leu. Its apparent $K_m$ on compactin-Na was $1.294{\mu}M{\cdot}min^-1,\;and\;V_{max}\;was\;1.028{\mu}M{\cdot}min^-1$. The maximum substrate concentration ($K_s$) for reaction was $270 {\mu}M$and thus $1/[K_s]$ was $3.7{\mu}M$. These physicochemical characteristics and kinetic behavior of this enzyme were compared and shown to be different from those of Streptomyces cytochrome P-450 enzymes reported, suggesting that this enzyme may be an additional member of the Streptomyces cytochrome P-450 family.

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