Purification and Characterization of Chitinases from Transformed Callus Suspension Cultures of Trichosanthes kirilowii Maxim.

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概要

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• Three extracellular basic chitinases designated as TKC 15,TKC 28-I, and TKC 28-II were purified from Agrobacterium rhizogenes A4 transformed Trichosanthes kirilowii Maxim. callus suspension cultures using PerSeptive HS/M cation exchange and Sephadex G 75 S gel filtration chromatography. These chitinases exhibited maximal activity at pH 6 and temperature at 40-45℃. N-terminal analysis suggests that two chitinases (TKC 28-I and TKC 28-II) with indistinguishable molecular masses(28 kDa) belonged to the Class III chitinase family. Another basic protein with a molecular mass of 15 kDa(TKC 15) also possesses chitinase activity. Chitobiose was the major end product from chitin digested by TKC 28-I and TKC 28-II whereas TKC 15 released a mix of tetramers, trimers and dimers from chitin. Slow cleavage of chitotriose by TKC 28-I and 28-II and no cleavage of tetramers and trimers by TKC 15 were observed. TKC 28-I cleaved tetramer faster than trimers, 1.1×10^<-4> M・h^<-1>・μg^<-1> and 1.5×10^<-6> M・h^<0-1>・μg^<-1> respectively. All chitinases showed inhibitory ability in a cell-free protein translation system but were far less potent than trichosanthin, a ribosome inactivating protein, found in the storage root tuber of T. kirilowii. The purified T. kirilowii chitinases did not show antifungal activity against Aspergillus flavus or Trichoderma viride.

• 公益社団法人日本生物工学会の論文
• 1997-07-25

著者

• Shih N.-j.remi

  Department Of Chemnical Engineering And Materials Science University Of California At Davis

• McDONALD KAREN

  Department of Chemnical Engineering and Materials Science, University of California at Davis

• Mcdonald Karen

  Department Of Chemnical Engineering And Materials Science University Of California At Davis

関連論文

• Purification and Characterization of Chitinases from Transformed Callus Suspension Cultures of Trichosanthes kirilowii Maxim.

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