Enzyme characteristics of beta-D-galactosidase- and beta-D-glucuronidase-positive bacteria and their interference in rapid methods for detection of waterborne coliforms and Escherichia coli
Article Abstract:
An investigation of the enzyme characteristics of beta-D-galactosidase- and beta-D-glucuronidase-positive bacteria isolated from environmental water samples revealed large variations in their enzyme levels. Induced and noninduced beta-D-glucuronidase activities of Bacillus spp. and Aerococcus viridans as well as the activities of induced Escherichia coli were found to be about the same. All induced and noninduced beta-D-galactosidase-positive isolates showed lesser activity than beta-D-galactosidase activity than induced E. coli, except some isolates identified as Aeromonas spp.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
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High-level production of recombinant hman parathyroid hormone 1-34
Article Abstract:
The application of a gene fusion strategy to the expression of synthetic human parathyroid hormone 1-34 gene [hPTH(1-34)] was described. At the C terminus of partner peptides involving amino acids of a modified Escherichia coli, hPTH(1-34) was produced. The fusion proteins in the inclusion bodies were made soluble with urea and subjected to site-specific cleavage with the secretory type yeast Kex2 protease. Optimal expression and enzymatic processing were achieved in the fusion protein betaG-117S4HPT. The fusion protein garnered more than 20% of the E. coli total protein.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
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Utilization of Escherichia coli outer-membrane endoprotease OmpT variants as processing enzymes for production of peptides from designer fusion proteins
Article Abstract:
Results demonstrate that the variant forms of Escherichia coli endoprotease OmpT efficiently cleave fusion proteins containing cognate amino acid sequence clevable by the enzyme. Data indicate that the variant enzyme cleaves motilin, human adrenocorticotropic hormone, and human calcitonin precursor from fusion proteins.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2004
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