The Sequence Analysis of Signal Peptide of α-amylase from Bacillus licheniformis and Its Secretory Characteristic

doi:10.7668/hbnxb.2008.02.024

Abstract

Abstract: The gene encoding a hyperthermostable α- amylase from a Bacillus licheniformis strain was cloned in p ET-22b transcription vector containing T7 promoter,and expressed in Escherichia coli BL21 (DE3) cells. The recombinant strain can secret the active recombinant enzyme into the medium. These indicated the signal peptide of this Bacillus sp.could be recognized by E. Coli secretory system. At the same time,the signal peptide secreted sweet protein monellin fromperiplasm to the medium too.This study gives a theory support for other foreign proteins expressed in E. Coli through theuse of this signal peptide.

Key words: &alpha, - amylase, Bacillus licheniformis, Secretory expression, Signal peptide

CLC Number:

CAI Heng, CHEN Zhong-jun, WAN Hong-gui, WANG Tao, DU Lian-xiang. The Sequence Analysis of Signal Peptide of α-amylase from Bacillus licheniformis and Its Secretory Characteristic[J]. ACTA AGRICULTURAE BOREALI-SINICA, 2008, 23(2): 106-109. doi: 10.7668/hbnxb.2008.02.024.

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