Chitinase B from Serratia marcescens BJL200 is exported to the periplasm without processing
Article Abstract:
Nucleotide sequencing of a chitinase-encoding gene from Serratia marcescens BJL200 that is expressed in S. marcescens and Escherichia coli reveals the presence of an open reading frame that codes for a 55.5 kDa protein with 499 amino acids, but no signal peptides that characterize export. Cell fractionation and immunocytochemical examination of the cellular positioning of the chitinase reveals its presence in E. coli cytoplasm and export to S. marcescens periplasm, which is not simultaneous with processing at the N-terminus. Export featuring other non-processed extracellular proteins are absent in the chitinase.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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Comparative studies of class IIa bacteriocins of lactic acid bacteria
Article Abstract:
Research was conducted to investigate the activities of four pure class IIa bacteriocins, pediocin PA-1, enterocin A, curvacin A and sakacin P, against a large number of lactic acid bacteria. Test was also conducted against various strains of the food pathogen Listeria monocytogenes. Optimized purification protocol affording highly pure samples was the methodology used to purify the bacteriocins from their respective producer strains. Results suggest that the various degrees of homology displayed by immunity genes may be responsible for the remarkable variation in bacteriocin sensitivity.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
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Comparative studies of chitinases A and B from Serratia marcescens
Article Abstract:
The chitinase A (ChiA) and ChiB enzymes of the Gram-negative bacteria Serratia marcescens have a broad pH optimum of 5.0 to 6.0, a temperature optimum from 50 to 60 degrees celsius, and high stability. Their activity is unaffected by NaCl or divalent metal ions. They possess an exo-N,N'-diacetylchitobiohydrolase activity and produce monomers from long N-acetylglucosamine oligomers. However, they differ in their specific activity and mechanism by which they degrade chitin. ChiA shows cooperative kinetics with a (GlcNAc)3 analogue, while ChiB has hyperbolic kinetics.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1996
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