Production of penicillin acylase from Bacillus megaterium in complex and defined media

Illanes, Andrés; Acevedo, Fernando; Gentina, Juan Carlos; Reyes, Isabel; Torres, Rodrigo; Cartagena, O.; Ruiz, A.; Vasquez, Marta

doi:10.1016/0032-9592(94)80067-7

Cited by 36 publications

(21 citation statements)

References 16 publications

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“…It can be concluded that glucose concentration above 5 g/l is not beneficial for PGA production in the culture medium as it delays the onset of synthesis, which might be attributed to catabolic repression. Illanes et al (1994) have reported that when glucose was omitted from the complex medium, both penicillin acylase production and productivity from Bacillus megaterium were significantly higher, and only a slight decrease in specific growth rates was observed.…”

Section: Resultsmentioning

confidence: 99%

Kinetic Study of Growth and Penicillin G Acylase Production by Escherichia coli

Arshad¹,

Ahmad²

2000

Pakistan J. of Biological Sciences

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Penicillin G acylase (PGA) is one of the most widely used enzymes at an industrial scale. It is used to hydrolyze penicillin G to produce 6-aminopenicillanic acid (6-APA), a required intermediate in the production of semisynthetic penicillins. Escherichia coli is the most abundantly used organism for PGA production. Present study was focused on the kinetics of growth and PGA production of three local E. coli isolates, FH6-NIAB, FMu2-NIAB and FD25-NIAB. Optimal enzyme production was reached after 18 hr. For longer incubations, the enzymatic activity decreased slightly. PGA activity was detectable after about 6 hours of incubation. For the selected isolates, PGA production was determined for various concentrations of glucose and phenylacetic acid in the medium. PGA production by E. coli isolates was completely repressed by glucose concentration above 5 g/l. Production of PGA by E. coli isolates was completely dependent upon the presence of PAA in the medium and optimal enzyme activity was obtained between 1 g/l and 2 g/l of PAA. Enzyme activity was found to be highest when PAA was used as an inducer. PGA production by our local E. coli isolates was completely inducible.

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Section: Resultsmentioning

confidence: 99%

Kinetic Study of Growth and Penicillin G Acylase Production by Escherichia coli

Arshad¹,

Ahmad²

2000

Pakistan J. of Biological Sciences

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“…The initial pH was adjusted to 8.3, except in the assays used to study the influence of pH. The salt solution added to the medium, in some experiments, was (mg l (Illanes et al,1994). Shake incubators were used at 300 rpm and 30 o C for 72 hours.…”

Section: Enzyme Production Mediummentioning

confidence: 99%

“…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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“…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.…”

Section: Introductionmentioning

confidence: 99%

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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Production of penicillin acylase from Bacillus megaterium in complex and defined media

Cited by 36 publications

References 16 publications

Kinetic Study of Growth and Penicillin G Acylase Production by Escherichia coli

Kinetic Study of Growth and Penicillin G Acylase Production by Escherichia coli

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

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

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