Stable expression of a thermostable xylanase of Clostridium thermocellum in cultured tobacco cells

被引：0
|
作者：
Kimura, T [1 ]
Mizutani, T [1 ]
Sakka, K [1 ]
Ohmiya, K [1 ]
机构：
[1] Mie Univ, Fac Bioresources, Tsu, Mie 5148507, Japan
来源：
JOURNAL OF BIOSCIENCE AND BIOENGINEERING | 2003年 / 95卷 / 04期
关键词：
Clostridium thermocellum; tobacco BY-2; xylanase;
D O I：
暂无
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
Two distinct domains of the xynA gene from Clostridium thermocellum encoding a xylanase catalytic domain (XynA1) 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 XynA1 and XynA2 were produced in these calli.
引用
收藏
页码：397 / 400
页数：4
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