지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제24권 제9호
- 발행연도
- 2014.1
- 수록면
- 1,196 - 1,206 (11page)
이용수
초록· 키워드
오류제보하기
A metagenomic fosmid library was constructed using genomic DNA isolated from the gut microflora of Hermetia illucens, a black soldier fly. A cellulase-positive clone, with the CS10 gene, was identified by extensive Congo-red overlay screenings for cellulase activity from the fosmid library of 92,000 clones. The CS10 gene was composed of a 996 bp DNA sequence encoding the mature protein of 331 amino acids. The deduced amino acids of CS10 showed 72% sequence identity with the glycosyl hydrolase family 5 gene of Dysgonomonas mossii, displaying no significant sequence homology to already known cellulases. The purified CS10 protein presented a single band of cellulase activity with a molecular mass of approximately 40 kDa on the SDS-PAGE gel and zymogram. The purified CS10 protein exhibited optimal activity at 50°C and pH 7.0, and the thermostability and pH stability of CS10 were preserved at the ranges of 20~50°C and pH 4.0~10.0. CS10 exhibited little loss of cellulase activity against various chemical reagents such as 10% polar organic solvents, 1% non-ionic detergents, and 0.5 M denaturing agents. Moreover, the substrate specificity and the product patterns by thinlayer chromatography suggested that CS10 is an endo-β-1,4-glucanase. From these biochemical properties of CS10, it is expected that the enzyme has the potential for application in industrial processes.
목차
등록된 정보가 없습니다.
참고문헌 (23)
참고문헌 신청
Amann RI / 1995 / Phylogenetic identification and in situ detection of individual microbial cells without cultivation / Microbiol. Rev 59 : 143 ~ 169
B olam DN / 1998 / Pseudomonas cellulosebinding domains mediate their effects by increasing enzyme substrate proximity / Biochem. J 331 : 775 ~ 781
Balachandrababu Malini Asha / 2012 / Purification and Characterization of a Thermophilic Cellulase from a Novel Cellulolytic Strain, Paenibacillus barcinonensis / Journal of
Beguin P / 1994 / The biological degradation of cellulose / FEMS Microbiol. Rev 13 : 25 ~ 58
Bhat MK / 1997 / Cellulose degrading enzymes and their potential industrial applications / Biotechnol. Adv 15 : 583 ~ 620
B olam DN / 1998 / Pseudomonas cellulosebinding domains mediate their effects by increasing enzyme substrate proximity / Biochem. J 331 : 775 ~ 781
Balachandrababu Malini Asha / 2012 / Purification and Characterization of a Thermophilic Cellulase from a Novel Cellulolytic Strain, Paenibacillus barcinonensis / Journal of
Beguin P / 1994 / The biological degradation of cellulose / FEMS Microbiol. Rev 13 : 25 ~ 58
Bhat MK / 1997 / Cellulose degrading enzymes and their potential industrial applications / Biotechnol. Adv 15 : 583 ~ 620
이 논문의 저자 정보
최근 본 자료
댓글(0)
0