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Functional analysis of the C-terminal propeptide of keratinase from Bacillus licheniformis BBE11-1 and its effect on the production of keratinase in Bacillus subtilis

Paper ID Volume ID Publish Year Pages File Format Full-Text
34665 45038 2014 5 PDF Available
Title
Functional analysis of the C-terminal propeptide of keratinase from Bacillus licheniformis BBE11-1 and its effect on the production of keratinase in Bacillus subtilis
Abstract

•Optimizing the C-terminus of propeptide will affect the cleavage efficiency of propeptide.•Inserting linkers and deleting residues at P2 position decrease the mature keratinase production.•The primary structure of C-terminus propeptide is crucial for the mature keratinase production.

The keratinase from Bacillus licheniformis BBE11-1 is a serine protease and expressed as a pre-pro-precursor. To produce a mature and active keratinase, the propeptide must be cleaved on the C-terminal via cis or trans. In this study, to enhance the production of keratinase in Bacillus subtilis, single amino acid substitutions, single residue deletions and linkers were introduced at the C-terminus of the propeptide. The results showed that optimizing the residue of cleavage site of propeptide will affect the cleavage efficiency of propeptide, and the mature enzyme yield of Leu(P1)Ala mutant increases 50% compared with the wild-type. In addition, inserting linkers and deleting individual residues at the C-terminal of the propeptide decreases the mature keratinase production. Our results indicated that the primary structure of the C-terminus of propeptide is crucial for the mature keratinase production. Propeptide engineering at C-terminus may be an effective approach to increase the yield of keratinase.

Keywords
Keratinase; Bacillus licheniformis; Propeptide; Cleavage efficiency
First Page Preview
Functional analysis of the C-terminal propeptide of keratinase from Bacillus licheniformis BBE11-1 and its effect on the production of keratinase in Bacillus subtilis
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 49, Issue 9, September 2014, Pages 1538–1542
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering