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A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
Lysobacter strain with high lysyl endopeptidase production
Shigeru Chohnan1, Junko Nonaka, Kousei Teramoto
1Department of Bioresource Science, College of Agriculture, Ibaraki University, 3-21-1 Chu-ou, Ami, Ibaraki, Japan.
FEMS Microbiology Letters
|July 20, 2002
Summary
A novel soil bacterium, Lysobacter sp. IB-9374, produces a highly efficient lysyl endopeptidase enzyme. This enzyme exhibits identical characteristics to Achromobacter lysyl endopeptidase but is secreted at significantly higher levels.
Area of Science:
- Microbiology
- Enzymology
- Molecular Biology
Background:
- Lysyl endopeptidases are crucial enzymes with specific cleavage properties.
- Identifying novel microbial sources for high-yield enzyme production is of significant interest.
- Achromobacter lysyl endopeptidase is a well-characterized enzyme with desirable enzymatic properties.
Purpose of the Study:
- To isolate and characterize a new strain producing lysyl endopeptidase.
- To compare the enzymatic properties and gene sequence of the novel enzyme with known counterparts.
- To investigate the production levels of the novel lysyl endopeptidase.
Main Methods:
- Isolation of microbial strains from soil samples.
- Enzymatic assays to determine enzyme activity, specificity, pH optimum, and stability.
- Nucleotide sequencing of the lysyl endopeptidase gene.
- Analysis of precursor protein structure and comparison with related enzymes.
Main Results:
- Lysobacter sp. IB-9374 was identified as a high producer of lysyl endopeptidase.
- The secreted enzyme demonstrated identical enzymatic properties to Achromobacter lysyl endopeptidase.
- Gene sequence analysis revealed identical mature enzyme sequences but variations in precursor protein structure.
- Lysobacter sp. IB-9374 secreted the enzyme 6-12 fold higher than reference strains.
Conclusions:
- Lysobacter sp. IB-9374 is a promising source for efficient lysyl endopeptidase production.
- The novel enzyme offers a potentially superior alternative to existing lysyl endopeptidases.
- Understanding precursor protein variations can provide insights into enhanced enzyme secretion mechanisms.
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