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논문 기본정보
Heterologous Expression and Characterization of a Thermostable Exo- beta;-D-Glucosaminidase from Aspergillus oryzae
논문 개요
| 기관명 | NDSL |
|---|---|
| 저널명 | Journal of microbiology and biotechnology |
| ISSN | 1017-7825,1738-8872 |
| ISBN |
논문저자 및 소속기관 정보
| 저자(한글) | Wu, Dingxin,Wang, Linchun,Li, Yuwei,Zhao, Shumiao,Peng, Nan,Liang, Yunxiang |
|---|---|
| 저자(영문) | |
| 소속기관 | |
| 소속기관(영문) | |
| 출판인 | |
| 간행물 번호 | |
| 발행연도 | 2016-01-01 |
| 초록 | An exo- beta;-D-glucosaminidase (AorCsxA) from Aspergillus oryzae FL402 was heterologously expressed and purified. The deduced amino acid sequence indicated that AorCsxA belonged to glycoside hydrolase family 2. AorCsxA digested colloid chitosan into glucosamine but not into chitosan oligosaccharides, demonstrating exo- beta;-D-glucosaminidase (CsxA) activity. AorCsxA exhibited optimal activity at pH 5.5 and 50 #8451;; however, the enzyme expressed in Pichia pastoris (PpAorCsxA) showed much stronger thermostability at 50 #8451; than that expressed in Escherichia coli (EcAorCsxA), which may be related to glycosylation. AorCsxA activity was inhibited by EDTA and most of the tested metal ions. A single amino acid mutation (F769W) in AorCsxA significantly enhanced the specific activity and hydrolysis velocity as revealed by comparison of V max and k cat values with those of the wild-type enzyme. The three-dimensional structure suggested the tightened pocket at the active site of F769W enabled efficient substrate binding. The AorCsxA gene was heterologously expressed in P. pastoris, and one transformant was found to produce 222 U/ml activity during the high-cell-density fermentation. This AorCsxA-overexpressing P. pastoris strain is feasible for large-scale production of AorCsxA. |
| 원문URL | http://click.ndsl.kr/servlet/OpenAPIDetailView?keyValue=03553784&target=NART&cn=JAKO201614735094031 |
| 첨부파일 |
추가정보
| 과학기술표준분류 | |
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| ICT 기술분류 | |
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| 주제어 (키워드) | Exo- beta,-D-glucosaminidase,thermostability,glucosamine,Aspergillus oryzae,high-cell-density fermentation |