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  • 1
    Electronic Resource
    Electronic Resource
    The Efficient Production of Human Epidermal Growth Factor by Bacillus brevis (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 782 (1996), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1996.tb40553.x
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  • 2
    Electronic Resource
    Electronic Resource
    Very efficient extracellular production of cholera toxin B subunit using Bacillus brevis (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 111 (1993), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract We have constructed a very efficient synthesis and secretion system for cholera toxin B subunit (CTB) of Vibrio cholerae 569B using Bacillus brevis. The constructed expression-secretion vector has the multiple promoters and the signal peptide coding region of the mwp gene, a structural gene for one of the major cell wall proteins of B. brevis strain 47, directly followed by the gene encoding the mature CTB. A large amount of mature CTB (1.4 g per liter of culture) was secreted into the medium. It had the same amino terminal amino acid sequence as that of authentic CTB and was fully active in GM1 ganglioside binding assay.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1993.tb06389.x
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  • 3
    Electronic Resource
    Electronic Resource
    Efficient production of thermostable Thermus thermophilus xylose isomerase in Escherichia coli and Bacillus brevis (1992)
    Springer
    Applied microbiology and biotechnology 36 (1992), S. 727-732 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The xylose (glucose) isomerase from the thermophile Thermus thermophilus seems to have potential for the development of new isomerization processes using high temperatures and slightly acidic pH. The isomerase has an optimum temperature at 95° C, and is also very stable at high temperatures. The optimum pH is around 7.0, close to where by-product formation is minimal. Since Thermus produces only a little of this useful isomerase, the production of the cloned gene in Escherichia coli and Bacillus brevis were compared. Especially B. brevis was able to produce the isomerase effeciently, more than 1 g/l, in spite of the high G + content (67%) of the Thermus gene, and the presence of codons not frequently used in E. coli or B. brevis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00172183
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  • 4
    Electronic Resource
    Electronic Resource
    Production of swine pepsinogen by protein-producing Bacillus brevis carrying swine pepsinogen cDNA (1989)
    Springer
    Applied microbiology and biotechnology 30 (1989), S. 75-80 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary An expression-secretion vector, pNU100, was constructed, utilizing the promoter and coding sequences for the signal peptide and nine amino-terminal amino acids of the middle wall protein, to produce foreign proteins by protein-producing Bacillus brevis. Expression of swine pepsinogen cDNA in B. brevis was examined with pNU100 as a vector. The recombinant swine pepsinogen synthesized by B. brevis was found to accumulate extracellularly in the form of a soluble protein and to have acid protease activity. The acid protease activity was completely inhibited by pepstatin. Furthermore, the recombinant pepsinogen was converted autocatalytically to pepsin under acidic conditions. This indicates that B. brevis produces a pepsinogen with the same conformation as authentic pepsinogen. Efficient production of the enzyme (11 mg/l) was achieved by regulating the pH of the medium. The enzyme produced by B. brevis remained stable on cultivation for a long period, up to 40 h. This is suggested to be due to a unique property of protein-producing B. brevis, i. e. a deficiency in extracellular protease production.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00256000
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  • 5
    Electronic Resource
    Electronic Resource
    Efficient production of human α-amylase by a Bacillus brevis mutant (1990)
    Springer
    Applied microbiology and biotechnology 34 (1990), S. 297-302 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A cDNA for mature human salivary α-amylase was directly joined to a sequence encoding the signal peptide of the middle wall protein (MWP) gene of Bacillus brevis 47. This hybrid gene was placed downstream from the multiple promoter region of the MWP gene on a low copy-number plasmid vector, pHW1. B. brevis 47 carrying the plasmid produced 0.9 mg/l of active human α-amylase in the medium. A B. brevis 47 mutant obtained on mutagenesis with N-methyl-N′-nitro-N-nitrosoguanidine produced an increased amount of the α-amylase (6 mg/l). When the fused gene was inserted into a high copy-number expression vector, pNU200, and then introduced into the mutant, a large amount (60 mg/l) of the α-amylase was produced in the medium. The α-amylase showed approximately the same specific activity and molecular weight as those of the natural enzyme. The mutant showed higher sensitivity to various antibiotics than the original strain, and altered cell wall and cytoplasmic membrane protein compositions. The results of reversion analysis suggested that a single mutation is responsible for the above phenotypes and hyper-productivity of human α-amylase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00170046
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  • 6
    Electronic Resource
    Electronic Resource
    Production of a fungal protein, Taka-amylase A, by protein-producingBacillus brevis HPD31 (1993)
    Springer
    Journal of industrial microbiology and biotechnology 11 (1993), S. 83-88 
    Details
    ISSN: 1476-5535
    Keywords: Protein producingB. brevis ; Secretion vector ; pMK300 ; Taka-amylase A production
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary An expression-secretion vector, pMK300, was constructed to express theAspergillus oryzae Taka-amylase A (Taa) cDNA. The promoter and signal peptide regions of the HWP (a major cell wall protein ofBacillus brevis HPD31) gene on pMK300 were efficiently utilized inB. brevis HPD31 and a large amount of Taa (22 mg/l) was secreted into the medium. The HWP signal peptide utilized for secretion of Taa was correctly processed during the protein transport across the membrane. The enzymatic properties of Taa produced byB. brevis HPD31 were the same as those of theAspergillus oryzae Taa in several respects; specific activity thermal and pH stabilities, and temperature and pH optima. These results, in combination with previous results, indicate thatB. brevis HPD31 could be used to produce extracellularly foreign proteins of diverse orgins as functional proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01583679
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  • 7
    Electronic Resource
    Electronic Resource
    Protein secretion inBacillus brevis (1993)
    Springer
    Antonie van Leeuwenhoek 64 (1993), S. 137-143 
    Details
    ISSN: 1572-9699
    Keywords: protein secretion ; Bacillus brevis host-vector system ; cell surface structure ; signal peptide ; protein folding enzyme
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Many strains ofBacillus brevis were isolated from nature as very efficient producers of extracellular proteins. Strains identified asB. brevis including these protein-hyperproducers were reclassified into at least 6 species according to numerical analysis, DNA base composition, and DNA-DNA hybridization. We developed a host-vector system using appropriate strains of theseBacillus brevis as a host, which is excellent for the secretion of heterologous proteins. Utilizing the powerful promoters and signal peptide-coding regions of the cell wall protein gene, various expression-secretion vectors were constructed. The cell wall protein genes of theseB. brevis are transcribed from multiple and tandemly arranged promoters. Transcription from P2, one of the major promoters among them, was enhanced at the early stationary phase of growth, when divalent cations in the medium was depleted and the cell wall protein layers started to be shed. Translation of the cell wall protein gene transcripts starts at the two sites located tandemly in the same reading frame. The two forms of secretory precursors, translation products from the two sites, are cleaved at the same position giving rise to the same mature proteins. The nucleotide sequence from the promoter to the translation start site is highly conserved in protein-hyperproducingB. brevis. For the efficient secretion of some heterologous proteins, protein-hypersecreting mutants had to be selected. The engineering of the signal peptide was also often necessary to obtain a good secretion of heterologous proteins. Thus, high levels of secretion were achieved only after extensive improvements were made for host, vector and culture conditions. From these experimental results, a great deal of diversity has been observed in various aspects of protein secretion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00873023
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  • 8
    Electronic Resource
    Electronic Resource
    Genetic characterization of a gene for prolipoprotein signal peptidase in Escherichia coli (1983)
    Springer
    Molecular genetics and genomics 192 (1983), S. 10-14 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A mutation (lspA, prolipoprotein signal peptidase) rendering the prolipoprotein signal peptidase temperature-sensitive in Escherichia coli has been analyzed. The mutation was mapped in the dnaJ-rpsT-ileS-dapB region by interrupted mating with various Hfr strains and P1 phage transduction. λ transducing phage λddapB2 that carries the rpsT-ileS-dapB region was shown to complement the lspA mutation. Plasmid pLC3-13 which had been isolated from Clarke and Carbon's collection as a plasmid carrying the lspA locus was shown to carry the dnaJ and rpsT loci. Complementation analysis with plasmids carrying various DNA fragments derived from pLC3-13 showed that the lspA locus is between the rpsT and ileS loci. The wildtype allele was dominant over the lspA allele.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00327640
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  • 9
    Electronic Resource
    Electronic Resource
    Characteristics of batch culture of a recombinant bacillus brevis excreting a foreign esterase (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 38 (1991), S. 1247-1252 
    Details
    ISSN: 0006-3592
    Keywords: batch culture ; Bacillus brevis ; esterase ; host-vector system ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The productivity of extracellular enzyme was evaluated in batch culture using a protein hyperexcreting host, Bacillus brevis HPD315 harboring pHSC131, which carried a gene (est) encoding esterase activity from Bacillus stearother mophilus. Optimum temperature and pH for the bacterial growth and the production of extracellular esterase were found to be 35°C and pH 6.5, by using the standard medium (GPY) containing neomycin as a selective pressure, Under the cultivation condition employed, cell growth reached 5 g dry cell weight/L, while the extracellular esterase activity amounted to 4.5 U/mL. Most (79%-92%) of the esterase produced was excreted into the medium. pHSC131 was stably retained in the host cell during cultivation in the presence of neomycin. However, in the absence of neomycin, the plasmid was completely lost from the host after 12-h cultivation accompanied by decreases in both esterase activity and production of total extracellular protein. The copy number of the plasmid was estimated to be approximately 7 throughout the cultivation. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the excreted proteins showed the presence of a protein having an apparent molecular weight of 32,000, which equals to the value predicted from the DNA sequence of the est gene.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260381018
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  • 10
    Electronic Resource
    Electronic Resource
    Effective extracellular production of Bacillus stearothermophilus esterase by pH-stat modal fed-batch culture of recombinant Bacillus brevis (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 40 (1992), S. 844-850 
    Details
    ISSN: 0006-3592
    Keywords: automated substrate feeding ; Bacillus stearothermophilus esterase ; pH-stat modal fed-batch culture ; recombinant Bacillus brevis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: An automated two-component substrate feeding strategy with a pH-stat modal fed-batch culture using a high pH limit was developed to effectively porduce esterase from a hyperprotein exreting Bacillus brevis HPD31 harboring a plasmid pHSC131 which carries a Bacillus stearothermo philus esterase gene. First, the effect of single- and multi-substrate feedings on the growth and activity of the excreted esterase was investigated. Then a two-component (polypepton + glucose) feeding using different feed rates was studied. Highest activity of the excreted esterase (34 U/mL) was obtained when the concentrations of poly-pepton and glucose in the nutrient feed solution were 250 and 41.60 g/L respectively. The absence and excessive amount of glucose in the nutrient feed solution was ineffective for the exracellular esterase formation because without glucose the increase in cell concentration was minimum while excessive amount of glucose favored cell growth at the expense of the esterase production. It is believed that the mechanism of enzyme excretion is growth dependent and that a higher cell growth of the host is in effect unfavorable for the enzyme production. The feed rate, automatically controlled by the direct signal of the pH change, at 0.30 mL/pulse was found optimum for the esterase production while lower (0.15 mL/pulse) and higher (0.67 mL/pulse) feed rates did not produce good results. The activity of the excreted esterase was increased more than eight times from 4 U/mL obtained in the conventional batch culture to 34 U/mL obtained in this study. The esterase productivity was likewise increased more than threefold. © 1992 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260400712
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