Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/60797
標題: Gene cloning and characterization of a novel recombinant antifungal chitinase from papaya (Carica papaya)
作者: Chen, Y.T.
陳玉婷
Hsu, L.H.
Huang, I.P.
Tsai, T.C.
Lee, G.C.
Shaw, J.F.
關鍵字: chitinase
papaya
antifungal activity
recombinant expression
plant chitinases
chitinolytic activity
rhizoctonia-solani
purification
expression
substrate
resistance
mechanism
lysozyme
proteins
期刊/報告no:: Journal of Agricultural and Food Chemistry, Volume 55, Issue 3, Page(s) 714-722.
摘要: A chitinase cDNA clone (CpCHI, 1002 bp) was isolated from papaya fruit, which encoded a 275 amino acid protein containing a 28 amino acid signal peptide in the N-terminal end. The predicted molecular mass of the mature protein was 26.2 kDa, and its pI value was 6.32. On the basis of its amino acid sequence homology with other plant chitinases, it was classified as a class IV chitinase. An active recombinant CpCHI enzyme was overexpressed in Escherichia coli. The purified recombinant papaya chitinase showed an optimal reaction temperature at 30 degrees C and a broad optimal pH ranging from 5.0 to 9.0. The recombinant enzyme was quite stable, retaining > 64% activity for 3 weeks at 30 degrees C. The spore germination of Alternaria brassicicola could be completely inhibited by a 76 nM level of recombinant CpCHI. Recombinant CpCHI also showed antibacterial activity in which 50% of E. coli was inhibited by a 2.5 mu M concentration of the enzyme.
URI: http://hdl.handle.net/11455/60797
ISSN: 0021-8561
文章連結: http://dx.doi.org/10.1021/jf062453e
Appears in Collections:基因體暨生物資訊學研究所

文件中的檔案:

取得全文請前往華藝線上圖書館



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.