Selection of cultivation medium for production of late stationary phase serine proteinases from <i>Bacillus intermedius</i>

Balaban, N. P.; Gabdrakhmanova, L. A.; Шарипова, М. Р.; Соколова, Е. А.; Malikova, L. A.; Марданова, А. М.; Rudenskaya, G. N.; Leshchinskaya, I. B.

doi:10.1002/jobm.200410426

Cited by 9 publications

(8 citation statements)

References 17 publications

(16 reference statements)

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“…Nitrogen catabolite repression is a well known phenomenon in the yeast Saccharomyces cerevisiae and bacteria such as Pseudomonas maltophilia and Bacillus intermedius , in which the presence of easily metabolized nitrogen sources repress the expression of genes encoding transporters and proteases (Boethling 1975; Hofman‐Bang 1999; Winderickx et al. 2003; Balaban et al. 2004).…”

Section: Discussionmentioning

confidence: 99%

Effect of nutritional conditions on extracellular protease production by the haloalkaliphilic archaeon Natrialba magadii

D’Alessandro

Castro

Giménez

et al. 2007

Lett Appl Microbiol

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Aims: The effect of various nitrogen sources and nutritional starvation was examined on the production of an extracellular protease secreted by the haloalkaliphilic archaeon Natrialba magadii. Methods and Results: Cell growth and proteolytic activity were measured in cells grown with different nitrogen sources. Proteolytic activity was produced in complex and easily metabolized nitrogen sources such as yeast extract, casein and casamino acids; meanwhile, ammonium repressed enzyme production. The time course and amount of protease accumulated showed an inverse correlation with growth rate and nutrient concentration. Starvation did not induce extracellular protease production. Conclusion: The accumulation of Nab. magadii extracellular protease is stimulated by nutrient limitation and slow growth rate indicating that it is probably induced in response to a deficit in the energetic status of the cells. Nutritional starvation did not induce protease accumulation suggesting that de novo synthesis of this protease and/or factor/s necessary for its activation are required. This enzyme may be regulated by nitrogen catabolite repression and it does not require protein substrates for induction. Significance and Impact of the Study: These results contribute to the basic knowledge on protease regulation in haloalkaliphilic archaea and will help to optimize the production of this extremozyme for biotechnological applications such as protease‐catalysed peptide synthesis.

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Section: Discussionmentioning

confidence: 99%

Effect of nutritional conditions on extracellular protease production by the haloalkaliphilic archaeon Natrialba magadii

D’Alessandro

Castro

Giménez

et al. 2007

Lett Appl Microbiol

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“…Cloning, identification and sequence analysis of B. intermedius mprBi gene B. intermedius is a rich source of extracellular enzymes. Among other hydrolases, we have previously isolated and characterized two secreted serine proteinases from B. intermedius [13][14][15][16][17][18][19]. During the course of these earlier studies, we detected an additional weak proteolytic activity present in B. intermedius culture medium, and preliminary experiments indicated that this enzyme may represent a previously uncharacterized metalloproteinase.…”

Section: Resultsmentioning

confidence: 92%

“…As mentioned before, the original B. intermedius strain secretes a number of serine proteinases [13–15]. To analyze the nature of MprBi proteolytic activity, we tested the effects of several specific proteinase inhibitors on the enzyme activity (Table 2 ).…”

Section: Resultsmentioning

confidence: 99%

“…Bacillus intermedius 3-19 is a species of soil bacterium, which secretes a number of extracellular enzymes, including a glutamyl-endopeptidase and a subtilisin-like proteinase [13][14][15][16][17][18][19]. Here we report the cloning, purification and sequence analysis of a novel extracellular metalloproteinase from B. intermedius, dubbed MprBi.…”

Section: Introductionmentioning

confidence: 99%

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A novel secreted metzincin metalloproteinase from Bacillus intermedius

et al. 2010

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a b s t r a c tThe mprBi gene from Bacillus intermedius 3-19 encoding a novel secreted metalloproteinase was identified. The mpriBi gene was expressed in an extracellular proteinase-deficient Bacillus subtilis BG 2036 strain and the corresponding protein was characterized biochemically. The 19 kDa MprBi protein was purified to homogeneity and sequenced by mass spectroscopy and Edman degradation methods. Amino acid sequence analysis of MprBi identified an active site motif HEYGHNFGLPHD and a conserved structural component Met-turn, both of which are unique features of the metzincin clan. Furthermore, MprBi harbors a number of distinct sequence elements characteristic of proteinase domains in eukaryotic adamalysins. We conclude that MprBi and similar proteins from other Bacillus species form a novel group of metzincin metalloproteinases in prokaryotes.

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“…The plasmid free and recombinant strains of B. subtilis, as well as the initial strain B. pumilus 3 19, were cultivated in the previously described medium for 30 h at 200 rpm [26]. The medium to flask volume ratio was 1 : 7.…”

Section: Methodsmentioning

confidence: 99%