http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
- 中文 을 입력하시려면 zhongwen을 입력하시고 space를누르시면됩니다.
- 北京 을 입력하시려면 beijing을 입력하시고 space를 누르시면 됩니다.
RISS 인기검색어
- 검색키워드
- 저자 : ( Bhattarai Saurabh ) (검색결과 4 건)
- 무료
- 기관 내 무료
- 유료
-
Homology Modeling and Docking Studies of Streptomyces peucetius CYP147F1 as Limonene Hydroxylase
( Bhattarai Saurabh ),( Kwangkyoung Liou ),( Tae Jin Oh ) 한국미생물 · 생명공학회 2012 Journal of microbiology and biotechnology Vol.22 No.7
Homology modeling of Streptomyces peucetius CYP147F1 was constructed using three cytochrome P450 structures, CYP107L1, CYPVdh, and CYPeryF, as templates. The lowest energy SPCYP147F1 model was then assessed for stereochemical quality and side-chain environment by Accelrys Discovery Studio 3.1 software. Further activesite optimization of the SPCYP147F1 was performed by molecular dynamics to generate the final SPCYP147F1 model. The substrate limonene was then docked into the model. The model-limonene complex was used to validate the active-site architecture, and functionally important residues within the substrate recognition site were identified by subsequent characterization of the secondary structure. The docking of limonene suggested that SPCYP147F1 would have broad specificity with the ligand based on the two different orientations of limonene within the active site facing to the heme. Limonene with C7 facing the heme with distance of 3.4 A from the Fe was predominant.
-
In-silico and In-vitro based studies of Streptomyces peucetius CYP107N3 for oleic acid epoxidation
( Saurabh Bhattarai ),( Narayan Prasad Niraula ),( Jae Kyung Sohng ),( Tae Jin Oh ) 생화학분자생물학회 2012 BMB Reports Vol.45 No.12
Certain members of the cytochromes P450 superfamily metabolize polyunsaturated long-chain fatty acids to several classes of oxygenated metabolites. An approach based on in silico analysis predicted that Streptomyces peucetius CYP107N3 might be a fatty acid-metabolizing enzyme, showing high homology with epoxidase enzymes. Homology modeling and docking studies of CYP107N3 showed that oleic acid can fit directly into the active site pocket of the double bond of oleic acid within optimum distance of 4.6 □ from the Fe. In order to confirm the epoxidation activity proposed by in silico analysis, a gene coding CYP107N3 was expressed in Escherichia coli. The purified CYP107N3 was shown to catalyze C9-C10 epoxidation of oleic acid in vitro to 9,10-epoxy stearic acid confirmed by ESI-MS, HPLC-MS and GC-MS spectral analysis. [BMB Reports 2012; 45(12): 736-741]
-
Biotransformation of Flavone by CYP105P2 from Streptomyces peucetius
( Niraula ),( Narayan Prasad ),( Saurabh Bhattarai ),( Na Rae Lee ),( Jae Kyung Sohng ),( Tae Jin Oh ) 한국미생물 · 생명공학회 2012 Journal of microbiology and biotechnology Vol.22 No.8
Biocatalytic transfer of oxygen in isolated cytochrome P450 or whole microbial cells is an elegant and efficient way to achieve selective hydroxylation. Cytochrome P450 CYP105P2 was isolated from Streptomyces peucetius that showed a high degree of amino acid identity with hydroxylases. Previously performed homology modeling, and subsequent docking of the model with flavone, displayed a reasonable docked structure. Therefore, in this study, in a pursuit to hydroxylate the flavone ring, CYP105P2 was co-expressed in a two-vector system with putidaredoxin reductase (camA) and putidaredoxin (camB) from Pseudomonas putida for efficient electron transport. HPLC analysis of the isolated product, together with LCMS analysis, showed a monohydroxylated flavone, which was further established by subsequent ESI/MS-MS, A successful 10.35% yield was achieved with the whole-cell bioconversion reaction in Escherichia coli. We verified that CYP105P2 is a potential bacterial hydroxylase.
-
Pilocarpus jaborandi로부터 필로카르핀의 효소반응추출
조전호 ( Jun Ho Cho ),사우라브바타라이 ( Saurabh Bhattarai ),오태진 ( Tae Jin Oh ),장종화 ( Jong Hwa Jang ) 한국미생물생명공학회(구 한국산업미생물학회) 2013 한국미생물·생명공학회지 Vol.41 No.2
필로카르핀은 Pilocarpus 속으로부터 유일하게 분리되는 이미다졸계 알칼로이드로서 상당히 제약적으로 중요하다. Pilocarpus jaborandi로부터 필로카르핀을 추출하기 위하여 환경친화적인 효소를 이용한 추출법을 이용하였다. 본 연구에서는 상업적으로 이용할 수 있는 효소칵테일인 Viscozyme® L을 사용하였다. 추출 조건은 기질, 효소, 온도 및 pH 등에 기초하여 최적화 되었다. 가장 높은 수율을 위한 최적화 조건은 pH4인 50 mM 아세트산 40 ml 하에서 45oC, 100 mg 기질, 30시간 반응이였다. 최적의 추출 효소농도는 10%이였다. Viscozyme® L 처리로부터 얻어진 전체 필로카르핀 함유량(1.14 μg/mg) 수준은 기존 리방법에서 얻어지는 양(0.37 μg/mg)보다 3.08배 높은 것을 확인하였다. Pilocarpine is an imidazole alkaloid, found exclusively in the Pilocarpus genus, with huge pharmaceutical importance. In order to extract pilocarpine from Pilocarpus jaborandi, environmentally friendly enzyme-assisted extraction was applied. Viscozyme® L, a commercially available enzyme cocktail, was used for the study. The conditions for extraction were optimized on the basis of substrates, enzymes, temperatures and pHs. Optimum conditions for extraction with the highest yield were 30 h reaction of 100 mg substance at 45oC in 40 ml of 50 mM acetic acid, pH 4. A 10% enzyme concentration was found to be the best for extraction. Total pilocarpine content after extraction was analyzed by HPLC. The total pilocarpine content (1.14 μg/mg) obtained from Viscozyme® L treatment was 3.08-fold greater than those of the control treatment (0.37 μg/mg).
ScienceON
KISS연관 검색어 추천
이 검색어로 많이 본 자료
활용도 높은 자료
