Study of Different Media for Production of Penicillin G Acylase from Bacillus megaterium ATCC 14945

Pinotti, L.; Silva, Astrea F. S.; Silva, Rosineide G.; Giordano, Raquel de Lima Camargo

doi:10.1007/978-1-4612-1392-5_50

Cited by 10 publications

(16 citation statements)

References 12 publications

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“…Acevedo and Cooney (1973), Illanes et al (1994) and Gentina et al (1997) presented studies on optimization of the culture medium for the production of PGA by B. megaterium. Pinotti et al (2000) confirmed the glucose repression of PGA production by B. megaterium and that the presence of cheese whey was necessary for this purpose -probably due to micronutrients in the whey, since lactose consumption was negligible. Therefore, a medium with free amino acids, acting as both nitrogen and carbon sources, was a natural choice at this point, and Souza et al (2002) studied the effect of the concentration of different free amino acids on the production of the enzyme in shaking flasks.…”

Section: Introductionsupporting

confidence: 69%

Using a medium of free amino acids to produce penicillin g acylase in fed-batch cultivations of Bacillus megaterium ATCC 14945

Silva

Souza

Nucci

et al. 2006

Braz. J. Chem. Eng.

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-The production of penicillin G acylase (PGA, an important industrial enzyme) from a wild strain of Bacillus megaterium using a pool of free amino acids as substrate was studied in a bench-scale bioreactor. Experiments carried out in shakers showed that the substitution of casein for free amino acids in the presence of cheese whey was the culture medium that provided the highest productivity. Several cultivations were carried out in a bioreactor operated in either batch or fed-batch mode. Batch runs showed that enzyme production is associated with microorganism growth. The following set of amino acids was preferentially consumed: Ala, Arg, Asp, Gly, Lys, Ser, Thr and Trp. On the other hand, the rates of consumption of His, Ile, Leu, Met, Phe, Pro, Tyr and Val were lower.

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Section: Introductionsupporting

confidence: 69%

Using a medium of free amino acids to produce penicillin g acylase in fed-batch cultivations of Bacillus megaterium ATCC 14945

Silva

Souza

Nucci

et al. 2006

Braz. J. Chem. Eng.

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“…Figure 1a presents the results of penicillin G acylase production, obtained after the cultivation of cultures of B. megaterium ATCC 14945 preserved using the previously described methods. All the tested methods resulted in a reduced activity when compared to the initial stock culture, 97 IU l -1 (Pinotti et al, 2000). The experiment with the subcultured microorganism (S) presented the best results, 57 IU l -1 of PGA.…”

Section: Protease Detectionmentioning

confidence: 96%

“…However, at high concentrations it may inhibit enzyme production (Acevedo and Cooney,1973;Shewale and Sivaraman, 1989;Gentina et al,1997). Another factor that influences enzyme production is the carbon source: glucose acts as a repressor of penicillin G acylase synthesis (Savidge, 1984;Illanes et al,1994, Pinotti et al,2000. Optimum growth conditions for B. megaterium are [28][29][30][31][32][33][34][35] o C and pH 7.0-8.5 (Murao et al, 1964).…”

Section: Introductionmentioning

confidence: 99%

Maintenance of penicillin G acylase expression by B. megaterium: preservation methods and activity recovery

Pinotti

Silva

Zangirolami

et al. 2007

Braz. J. Chem. Eng.

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-This work reports the influence of different culture preservation methods on the production of penicillin G acylase (PGA) by Bacillus megaterium ATCC 14945. The initial stock culture, presenting PGA activity of 97 IU l -1 , was preserved for two years using different procedures: monthly subculturing and storage in refrigerator (S), freeze-drying using skim milk 10%, plus inositol 5% as cryoprotectors (L1), freeze-drying using sucrose 7%, plus peptone 7% (L2), and freezing with glycerol 10% (F). After cultivations at standard operational conditions, different values of enzyme activity were obtained: 56 IU l -1 for monthly subculturing (S), 15-41 IU l -1 for freeze-dried cells and frozen spores. All the tested methods have failed in preserving the PGA expression. Among all tested cultures, S presented the highest specific activity, and was used to prepare a standard inoculum in cryovials (-50 o C, frozen spores in a 20% glycerol solution). By cultivation of this inoculum under different conditions, it was found that PGA activity raised to 128 IU l -1 when 0.4 g l -1 of salts was added to the medium.

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“…Bacillus megaterium secretes the enzyme produced, simplifying the separation process. The PGA production by B. megaterium has been studied by Pinotti et al, (2000 and2002) aiming to increase the final enzyme concentration in the culture medium. Enzyme characterization is necessary to compare its properties with those produced by other microorganisms.…”

Section: Introductionmentioning

confidence: 99%

Characterization of the penicillin G acylase from Bacillus megaterium ATCC 14945

Souza¹,

Silva²,

Pinotti

et al. 2005

Braz. arch. biol. technol.

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Study of Different Media for Production of Penicillin G Acylase from Bacillus megaterium ATCC 14945

Cited by 10 publications

References 12 publications

Using a medium of free amino acids to produce penicillin g acylase in fed-batch cultivations of Bacillus megaterium ATCC 14945

Using a medium of free amino acids to produce penicillin g acylase in fed-batch cultivations of Bacillus megaterium ATCC 14945

Maintenance of penicillin G acylase expression by B. megaterium: preservation methods and activity recovery

Characterization of the penicillin G acylase from Bacillus megaterium ATCC 14945

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