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

页码：397 / 400

页数：4

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