• 한국미생물·생명공학회지
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• 제18권4호
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• pp.376-382
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• 1990

토양과 퇴비 등에서 섬유소 자화력이 있는 세균을 분리하고 이 균주들 중 cellulase 생산능이 가장 우수한 균주를 선별하여 Cellulomonas sp.로 동정하였다. Cellulomonas sp. YE-5의 최적 배양조건은 pH6.5 Solka floc 0.8(w/v), urea 0.06(w/v), K2HPO4 0.1(w/v), bacto peptone 0.2(w/v), yeast extract 0.2(w/v) 그리고 MgSO4.7H2O 0.0(w/v) 이었으며, 이러한 배지를 사용하여 $30^{\circ}C$ 에서 48시간 배양하였을 때 avicelase, CMCase 그리고 Beta-glucosidase는 각각 0.350, 3.180, 0.882units/ml의 활성을 나타내었다.

• Journal of Microbiology and Biotechnology
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• 제3권2호
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• pp.86-90
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• 1993

CMCase positive clones were screened from Cellulomonas sp. YE-5 and named pCE1, pCE2 and pCE3. Among the positive clones pCE1 was used for this study, because it has the smallest insert and the highest CMCase activity among the 3 clones, and its nucleotide sequence was determined. The CMCase gene in pCE1 was composed of 1071 bp of nucleotides coding 357 amino acids. Computer analysis showed that the pCE1 has 65% sequence homology with the endoglucanase from Cellulomonas fimi.

• 한국미생물·생명공학회지
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• 제20권2호
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• pp.164-168
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• 1992

Cellulomonas sp.YE-5가 생산하는 cellulase를 분리, 정제하여 효소의 특성을 알아보았다. Avicelase, CMCase, $\beta$-glucosidase의 반응 최적온도은 각각 40, 45, $40^{\circ}C$이었고, 반은 최적 pH는 5.5, 6.0 그리고 6.0이었다. 효소의 열안정성은 30~$70^{\circ}C$에서 6시간 처리하였을 때 avicelase와 $\beta$-glucosidase는 $50^{\circ}C$ 이상에서 거의 실활하였고, CMCase는 $50^{\circ}C$에서 약 40%의 활성을 유지하였다. 효소의 안정성에 미치는 pH의 영향은 $25^{\circ}C$에서 24시간 처리하였을 때 avicelase와 CMCase는 PH 5.0~9.0 사이에서 안정하였으며, $\beta$-glucosidase는 pH 5.0~8.0 사이에서 안정하였다.

• Preventive Nutrition and Food Science
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• 제2권2호
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• pp.174-179
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• 1997

CMCase produced by recombinant E. coli JM109 (pCEH#4) containing CMCase gene from Cellulomonas sp. YE-5 was purified to 24.3 fold and 2.6% yield by ammoniumsulfate precipitation, DEAE-cellulose column chromatography and gel filtration on Sephadex G-100. The optimum pH and temperature for CMCase activity were pH 7.0 and 5$0^{\circ}C$. The enzyme was stable between pH 5.0 and 10.0, and up to 6$0^{\circ}C$. The molecular weight of he enzyme was estimated to be approximately 40,000 daltons by SDS-PAGE. Analysis of the amino acid composition showed that the enzyme contained many glycines and acidic amino acids. The enzyme was an endo-type CMCase and the final enzyme reaction product from hydrolysis of Cm-cellulose by the enzyme was cellobiose. {TEX}$K_{M}${/TEX} value determined with CM-cellulose was 1.28mM.