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在短短芽孢杆菌表达和分泌系统中高效生产嗜热纤维素酶

High-level production of hyperthermophilic cellulase in the Bacillus brevis expression and secretion system.

作者信息

Kashima Yasuhiro, Udaka Shigezo

机构信息

Special Division for Human Life Technology, National Institute of Advanced Industrial Science and Technology (AIST Kansai), Osaka, Japan.

出版信息

Biosci Biotechnol Biochem. 2004 Jan;68(1):235-7. doi: 10.1271/bbb.68.235.

DOI:10.1271/bbb.68.235
PMID:14745191
Abstract

A hyperthermophilic cellulase derived from Pyrococcus horikoshii was successfully produced with the Bacillus brevis host-vector system. The production of the recombinant enzyme was increased about 20-fold (to a level of 100 mg per liter) by the insertion of certain amino acid such as alanine and peptides like AEEAADP between the carboxyl end of signal peptide and the N-terminus of the mature cellulase. These recombinant cellulases had the same characteristics as that of the cellulase expressed in Escherichia coli.

摘要

利用短短芽孢杆菌宿主-载体系统成功生产了源自嗜热栖热菌的一种超嗜热纤维素酶。通过在信号肽羧基末端与成熟纤维素酶N端之间插入某些氨基酸(如丙氨酸)和肽(如AEEAADP),重组酶的产量提高了约20倍(达到每升100毫克的水平)。这些重组纤维素酶具有与在大肠杆菌中表达的纤维素酶相同的特性。

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