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Kim, Dong-Won,Hong, Young-Gwan,Ryu, Hai-Il 공주대학교 과학교육연구소 2001 과학교육연구 Vol.32 No.1
Trichoderma reesei 속 cellulose 로 부터 CBH I, CBH II와 core I과 core II의 셀룰로오스에 대한 흡착특성을 조사 하였다 5℃에서는, 15분 이내에 모든 흡착이 끝나며, 분리된 CBH I 성분효소가 CBH II 성분효소보다 더 빨리 흡착 되었고, 더 많은 양이 흡착되었다. 또한 core protein은 작은 양이 흡착되었다. 성분효소의 흡착을 유사 1차 반응 속도식에 적용시켜 흡착 파라미터, 즉 흡착 속도상수와 흡착활성화에너지를 구하였다. 흡착 속도상수값은 CBH I이 가장 컸고, core protein들은 작은 값을 나타내었다. 흡착활성화에너지는 core protein이 가장 큰값을 나타냈다. 이것은 CBH I이 셀룰로오스 표면에 보다 더 강하게 결합하고, core protein 표면에 느슨한 결합을 하기 때문이다.
( Colussi Francieli ),( Viviane Serpa ),( Priscila Da Silva Delabona ),( Livia Regina Manzine ),( Maria Luiza Voltatodio ),( Renata Alves ),( Bruno Luan Mello ),( Nei Pereira Jr. ),( Cristiane Sanches 한국미생물 · 생명공학회 2011 Journal of microbiology and biotechnology Vol.21 No.8
Because of its elevated cellulolytic activity, the filamentous fungus Trichoderma harzianum has a considerable potential in biomass hydrolysis applications. Trichoderma harzianum cellobiohydrolase I (ThCBHI), an exoglucanase, is an important enzyme in the process of cellulose degradation. Here, we report an easy single-step ion-exchange chromatographic method for purification of ThCBHI and its initial biophysical and biochemical characterization. The ThCBHI produced by induction with microcrystalline cellulose under submerged fermentation was purified on DEAE-Sephadex A-50 media and its identity was confirmed by mass spectrometry. The ThCBHI biochemical characterization showed that the protein has a molecular mass of 66 kDa and pI of 5.23. As confirmed by smallangle X-ray scattering (SAXS), both full-length ThCBHI and its catalytic core domain (CCD) obtained by digestion with papain are monomeric in solution. Secondary structure analysis of ThCBHI by circular dichroism revealed α- helices and β-strands contents in the 28% and 38% range, respectively. The intrinsic fluorescence emission maximum of 337 nm was accounted for as different degrees of exposure of ThCBHI tryptophan residues to water. Moreover, ThCBHI displayed maximum activity at pH 5.0 and temperature of 50℃ with specific activities against Avicel and p-nitrophenyl-β-D-cellobioside of 1.25 U/mg and 1.53 U/mg, respectively.
Purification and Characterization of a Thermostable Cellobiohydrolase from Fomitopsis pinicola
( Keum Shin ),( Yoon Hee Kim ),( Marimuthu Jeya ),( Jung Kul Lee ),( Yeong Suk Kim ) 한국미생물 · 생명공학회 2010 Journal of microbiology and biotechnology Vol.20 No.12
A screening for cellobiohydrolase (CBH) activity was performed and Fomitopsis pinicola KMJ812 was selected for further characterization as it produced a high level of CBH activity. An extracellular CBH was purified to homogeneity by sequential chromatography of F. pinicola culture supernatants. The molecular mass of the F. pinicola CBH was determined to be 64 kDa by SDS-PAGE and by size-exclusion chromatography, indicating that the enzyme is a monomer. The F. pinicola CBH showed a t1/2 value of 42 h at 70˚C and catalytic efficiency of 15.8 mM-1s-1 (Kcat/Km) for p-nitrophenyl-β-D-cellobioside, one of the highest levels seen for CBH-producing microorganisms. Its internal amino acid sequences showed a significant homology with hydrolases from glycoside hydrolase family 7. Although CBHs have been purified and characterized from other sources, the F. pinicola CBH is distinguished from other CBHs by its high catalytic efficiency and thermostability.
( Ekachai Chukeatirote ),( Sajeewa S. N. Maharachchikumbura ),( Shannaphimon Wongkham ),( Phongeun Sysouphanthong ),( Rungtiwa Phookamsak ),( Kevin D. Hyde ) 한국균학회 2012 Mycobiology Vol.40 No.2
Genes encoding the cellobiohydrolase enzyme (CBHI), designated as cbhI, were isolated from the basidiomycetes Auricularia fuscosuccinea, Pleurotus giganteus, P. eryngii, P. ostreatus, and P. sajor-caju. Initially, the fungal genomic DNA was extracted using a modified cetyltrimethyl ammonium bromide (CTAB) protocol and used as a DNA template. The cbhI genes were then amplified and cloned using the pGEM-T Easy Vector Systems. The sizes of these PCR amplicons were between 700~800 bp. The DNA sequences obtained were similar showing high identity to the cbhI gene family. These cbhI genes were partial consisting of three coding regions and two introns. The deduced amino acid sequences exhibited significant similarity to those of fungal CBHI enzymes belonging to glycosyl hydrolase family 7.
Characterization of Cellobiohydrolase from a Newly Isolated Strain of Agaricus arvencis
( Kyung Min Lee ),( Hee Jung Moon ),( Dayanand Kalyani ),( Hoon Kim ),( In Won Kim ),( Marimuthu Jeya ),( Jung Kul Lee ) 한국미생물 · 생명공학회 2011 Journal of microbiology and biotechnology Vol.21 No.7
A highly efficient cellobiohydrolase (CBH)-secreting basidiomycetous fungus, Agaricus arvensis KMJ623, was isolated and identified based on its morphological features and sequence analysis of internal transcribed spacer rDNA. An extracellular CBH was purified to homogeneity from A. arvencis culture supernatant using sequential chromatography. The relative molecular mass of A. arvencis CBH was determined to be 65 kDa by SDSPAGE and 130 kDa by size-exclusion chromatography, indicating that the enzyme is a dimer. A. arvencis CBH showed a catalytic efficiency (kcat/Km) of 31.8 mM-1 s-1 for p-nitrophenyl-β-D-cellobioside, the highest level seen for CBH-producing microorganisms. Its internal amino acid sequences showed significant homology with CBHs from glycoside hydrolase family 7. Although CBHs have been purified and characterized from other sources, A. arvencis CBH is distinguished from other CBHs by its high catalytic efficiency.
사과박 퇴비화에서의 미생물군집의 천이와 효소활성도의 변화
이영옥(Young-Ok Lee),조익환(Ik-Hwan Jo),이용세(Yong-Se Lee),전하준(Ha-Joon Jun) 유기성자원학회 1999 유기물자원화 Vol.7 No.2
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 κglucosidase 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. 사과박의 퇴비화에서 효소활성도가 퇴비의 안정성 혹은 부숙도를 나타내는 지표로서의 사용가능성이 있는지를 검증하기 위해 배양계수법에 의한 미생물군집의 천이와, 무형광상태로 기질에 결합되어있던 형광물질(MUF) 이 분해되면서 띠게 되는 형광정도가 해당효소의 활성도에 비례하여 높아지는 것을 이용하여 κglucosidase와 cellobiohydrolase 활성도를 측정하였다. 탄수화물의 분해에 관여하는 두 효소의 활성도는 시간변화에 따라 점점 낮아졌다. 미생물개체군과 효소활성도간의 상관성은 균류군을 제외하고는 없는 것으로 나타났고 또 균류가 높은 개체수를 나타내는 것으로 보아 균류가 사과박의 퇴비화에 지대한 역할을 담당할 것으로 사료된다.
Cloning of Cellobiohydrolase Gene (cbhI) in Radiation Induced Mutant of Pleurotus florida
이영근,Chandran Sathesh-Prabu,김민경 한국방사선산업학회 2014 방사선산업학회지 Vol.8 No.2
The cellobiohydrolase gene (cbhI), a key component of a cellulolytic system, of a mutantPfCM4 (Pleurotus florida), developed through gamma ray radiation mutagenesis, was isolated andcloned. The deduced amino acid sequence was closely related to the glycoside hydrolase family 7(GH7). The molecular weight of the deduced amino acid sequence of cbhI gene was found to be22.4 kDa. Though the percent identity was found to be much less (35.61%) between the wild typeand mutant, the cellulolytic activity of PfCM4 was 17.24% higher than that of the wild type. Thisshows that the catalytic domain of the cbhI gene was conserved in the mutant PfCM4.
Degradation of Crystalline Cellulose by the Brown-rot Basidiomycete Fomitopsis palustris
Yoon Jeong-Jun,Kim Young-Kyoon The Microbiological Society of Korea 2005 The journal of microbiology Vol.43 No.6
This study demonstrated that the brown rot basidiomycete Fomitopsis palustris was able to degrade crystalline cellulose (Avicel). This fungus could also produce the three major cellulases (exoglucanases, endoglucanases, and $\beta-glucosidase$) when the cells were grown on $2.0\%$ Avicel. Avicel degraded by F. palustris showed a decrease in relative crystallinity from $83\%\;to\;78.5\%$ after 14 days of incubation. The characterization study indicated that optimum pH was 4.5 and optimum temperature was $70^{\circ}C$ for exoglucanase (cellobiohydrolase) activity. Hydrolysis of Avicel by the crude enzyme from F. palustris yielded 1.6 mg/ml of glucose after 43 h, which corresponded to a cellulose conversion degree of $3.2\%$. Therefore, this study revealed for the first time that the brown rot basidiomycete F. palustris produces cellulases capable of yielding soluble sugars from crystalline cellulose.
Degradation of Crystalline Cellulose by the Brown-rot Basidiomycete Fomitopsis palustris
윤정준,Young-Kyoon Kim 한국미생물학회 2005 The journal of microbiology Vol.43 No.6
This study demonstrated that the brown rot basidiomycete Fomitopsis palustris was able to degrade crystalline cellulose (Avicel). This fungus could also produce the three major cellulases (exoglucanases, endoglucanases, and -glucosidase) when the cells were grown on 2.0% Avicel. Avicel degraded by F. palustris showed a decrease in relative crystallinity from 83% to 78.5% after 14 days of incubation. The characterization study indicated that optimum pH was 4.5 and optimum temperature was 70oC for exoglucanase (cellobiohydrolase) activity. Hydrolysis of Avicel by the crude enzyme from F. palustris yielded 1.6 mg/ml of glucose after 43 h, which corresponded to a cellulose conversion degree of 3.2%. Therefore, this study revealed for the first time that the brown rot basidiomycete F. palustris produces cellulases capable of yielding soluble sugars from crystalline cellulose.
Schizophyllum commune에 의한 Cellulase 생산 및 섬유소계 바이오매스의 당화를 위한 효소적 특성
김현정 ( Hyun Jung Kim ),김윤희 ( Yoon Hee Kim ),조문정 ( Moon Jung Cho ),신금 ( Keum Shin ),이동흡 ( Dong Heub Lee ),김태종 ( Tae Jong Kim ),김영숙 ( Yeong Suk Kim ) 한국목재공학회 2010 목재공학 Vol.38 No.6
The optimum culture condition of Schizophyllum commune for the cellulase production and its enzymatic characteristics for saccharification of cellulosic biomass were analyzed 5 commune secrets .β-l,4-xylosidase (BXL) and cellulases, including endo-.β-l,4-glucanase (EG), cellobiohydrolase (CBH), and . β-glucosidase (BGL). The optimum reaction temperature for all cellulases was 50℃ and the thermostable range was 30~40℃. The optimum reaction pH for all cellulases was 5.5 in a range of temperature from 0℃ to 55℃. The best nutritions for the cellulase production of s commune among tested nutrients were 2% cellulose for the carbon source and corn steep liquor or peptone/yeast extract for the nitrogen source without vitamins. The environmental culture condition for the cellulase production was 5.5~6.0 for pH at 25~30℃. The enzyme activities of EG, BGL, CBH, and BXL were 3670.5, 631.9, 398.5, and 15.2 U/㎖, respectively, after concentration forty times from the culture broth of 5 commune which was grown at the optimized culture condition. Alternative filter paper unit assay showed 11 FPU/㎖ enzyme activity. The saccharification tests using cellulase of 5 commune showed the low saccharification rate on tested hardwoods but a high value of 50.5% on cellulose, respectively. The saccharification rate (50.5%) of cellulose by cellulase produced in this work is higher than 45.7% in the commercial enzyme (Celluclast 1.51, 30 FPU/g, glucan).