Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/69618
標題: Cloning of a Novel L-Amino Acid Oxidase from Trichoderma harzianum ETS 323 and Bioactivity Analysis of Overexpressed L-Amino Acid Oxidase
作者: Cheng, C.H.
Yang, C.A.
Liu, S.Y.
Lo, C.T.
Huang, H.C.
Liao, F.C.
Peng, K.C.
關鍵字: L-amino acid oxidase;L-phenylalanine oxidase;antibacterial;Trichoderma harzianum;Escherichia coli;Staphylococcus aureus;viper calloselasma-rhodostoma;apoptosis-inducing factor;cobra;ophiophagus hannah;lysine alpha-oxidase;antimicrobial peptides;rhizoctonia-solani;molecular-cloning;snake-venom;apoxin i;purification
Project: Journal of Agricultural and Food Chemistry
期刊/報告no:: Journal of Agricultural and Food Chemistry, Volume 59, Issue 17, Page(s) 9142-9149.
摘要: 
L-Amino acid oxidases (L-AAOs) have been isolated from many :organisms, such as snake, and are known to have antibacterial activity. To the best of the authors knowledge, this is the first report of the cloning of cDNA encoding a novel Trichoderma harzianum ETS 323 L-amino acid oxidase (Th-L-AAO). The protein was overexpressed in Escherichia coli and purified to homogeneity. Comparisons of its deduced amino acid sequence with the sequence of other L-AAOs revealed the similarity to be between 9 and 24%. The molecular mass of the purified protein was 52 kDa, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme substrate specificity was highest for L-phenylalanine, and its optimal pH and temperature for activity were 7 and 40 degrees C, respectively; exogenous metal ions had no significant effect on activity. Circular dichroism spectroscopy indicated that the secondary structure of Th-L-AAO is composed of 17% alpha-helices, 28% beta-sheets, and 55% random coils. The bacterially expressed Th-L-AAO also mediated antibacterial activity against both Gram-positive and Gram-negative food spoilage microorganisms. Furthermore, a three-dimensional protein structure was created to provide more information about the structural composition of Th-L-AAO, suggesting that the N-terminal sequence of Th-L-AAO may have contributed to the ! antibacterial activity of this protein.
URI: http://hdl.handle.net/11455/69618
ISSN: 0021-8561
DOI: 10.1021/jf201598z
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