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Production, purification, characterization and immunological studies of E.coli E-U₁₀ penicillin amidase [electronic reource].

By:

Temsah, S

Contributor(s):

Mabrouk, A

Description: p.1-16Uniform titles:

Alexandria journal of veterinary science, 2001 v. 17 (1) [electronic reource].

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In: Alexandria Journal of Veterinary Science 2001.v.17(1)Summary: Penicillin amidase enzyme (PA) was isolated from the culture filtrate of one isolated strain of E. coli E-U₁₀ grown on optimized medium after 24 hours incubation. The enzyme was purified to homogeneity by sequential ammonium sulfate fractionation and ion exchange and gel filtration chromatography. On using Disc-PAGE, the final purification fraction showed only one distinctive band indicating high purity. On using SDS-PAGE the final fraction showed two distinctive units with molecular weight of 22000 and 59000 Dalton. The optimal pH, temperature and time course for activity were 7.5, 37°C and 10 minutes respectively. The enzyme with penicillin G as substrate had a Km of 13 mM and Vmax 3.92 U/ml.

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Penicillin amidase enzyme (PA) was isolated from the culture filtrate of one isolated strain of E. coli E-U₁₀ grown on optimized medium after 24 hours incubation. The enzyme was purified to homogeneity by sequential ammonium sulfate fractionation and ion exchange and gel filtration chromatography. On using Disc-PAGE, the final purification fraction showed only one distinctive band indicating high purity. On using SDS-PAGE the final fraction showed two distinctive units with molecular weight of 22000 and 59000 Dalton. The optimal pH, temperature and time course for activity were 7.5, 37°C and 10 minutes respectively. The enzyme with penicillin G as substrate had a Km of 13 mM and Vmax 3.92 U/ml.

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