Stable expression of a thermostable xylanase of Clostridium thermocellum in cultured tobacco cells.
Two distinct domains of the xynA gene from Clostridium thermocellum encoding a xylanase catalytic domain (XynAl) and a xylanase catalytic domain with a cellulose binding domain (XynA2) under the control of the cauliflower mosaic virus 35S promoter were electroporated into cultured tobacco BY-2 cells. Transgenic BY -2 calli expressing xylan-hydrolyzing activity were obtained at high frequency for both genes. Western blot analysis using an anti-XynA antibody indicated that XynAl and XynA2 were produced in these calli.
Kimura
Tetsuya
T
Faculty of Bioresources, Mie University, 1515 Kamihama-cho, Tsu, Mie 514-8507, Japan. t-kimura@bio.mie-u.ac.jp
Mizutani
Tomomi
T
Sakka
Kazuo
K
Ohmiya
Kunio
K