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Comparative study on the cell wall structure of protein-producing Bacillus brevis (1988)

Gruber, Karin ; Tanahashi, Hiroyuki ; Tsuboi, Akio ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

FEMS microbiology letters 56 (1988), S. 0

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ISSN: 1574-6968

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology

Notes: Abstract Among eight strains of protein-producing Bacillus brevis, three morphological groups have been identified according to the structure of the cell walls.〈list xml:id="l1" style="custom"〉(I)Cell wall consisting of a peptidoglycanlayer(II)Two-layered cell wall consisting of a peptidoglycan-layer and an S-layer(III)Three-layered cell wall consisting of a peptidoglycan-layer and two S-layersGroup I and group II cell walls have not been described yet for protein-producing bacteria. The S-layers observed in this study all had hexagonal symmetry and lattice constants of approximately 18 nm. The immunological relation between the S-layer proteins of the newly isolated B. brevis strains and those of B. brevis 47 has been examined using antisera against both S-layer-proteins of B. brevis 47. S-layers from protein-producing B. brevis strains, which were adjacent to the peptidoglycan-layer, were similar to each other, whether they were the outermost cell wall layer (group II) or not (group III). However, no similarity was found between these layers and the outermost S-layer of B. brevis 47 (group III).

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb03160.x

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Production of swine pepsinogen by protein-producing Bacillus brevis carrying swine pepsinogen cDNA (1989)

Takao, Makoto ; Morioka, Tomoko ; Yamagata, Hideo ; [et al.]

Springer

Applied microbiology and biotechnology 30 (1989), S. 75-80

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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.