In-fusion expression and characterization of β-xylanase and β-1,3-1,4-glucanase in Pichia pastoris

被引：2
|
作者：
Qiao, Jiayun [1 ]
Cao, Yunhe [1 ]
机构：
[1] China Agr Univ, Natl Key Lab Anim Nutr, Beijing 100193, Peoples R China
来源：
BIOLOGIA | 2012年 / 67卷 / 04期
关键词：
in-fusion; expression; beta-xylanase; beta-1,3-1,4-glucanase; Pichia pastoris; BIFUNCTIONAL ENZYME; GENE; WHEAT; PERFORMANCE; GLUCANASE; PROTEIN; SUPPLEMENTATION; DIGESTIBILITY; ENERGY; DIETS;
D O I：
10.2478/s11756-012-0056-3
中图分类号：
Q [生物科学];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Two chimeric genes, XynA-Bs-Glu-1 and XynA-Bs-Glu-2, encoding Aspergillus sulphureus beta-xylanase (XynA, 26 kDa) and Bacillus subtilis beta-1,3-1,4-glucanase (Bs-Glu, 30 kDa), were constructed via in-fusion by different linkers and expressed successfully in Pichia pastoris. The fusion protein (50 kDa) exhibited both beta-xylanase and beta-1,3-1,4-glucanase activities. Compared with parental enzymes, the moiety activities were decreased in fermentation supernatants. Parental XynA and Bs-Glu were superior to corresponding moieties in each fusion enzymes because of lower K-n higher k(cat). Despite some variations, common optima were generally 50A degrees C and pH 3.4 for the XynA moiety and parent, and 40A degrees C and pH 6.4 for the Bs-Glu counterparts. Thus, the fusion enzyme XynA-Bs-Glu-1 and XynA-Bs-Glu-2 were bifunctional.
引用
收藏
页码：649 / 653
页数：5
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