PMID: 9170259Feb 1, 1997

Immobilization of whole-cell penicillin G acylase by entrapping within polymethacrylamide beads

Applied Biochemistry and Biotechnology
L T HsiauF S Wang

Abstract

Escherichia coli ATCC 11105 containing the periplasmic penicillin G acylase was entrapped within a copolymer of methacrylamide and N,N'-methylenebisacrylamide. A solution of monomer that was made up from methacrylamide and N,N'-methylenebisacrylamide dissolved in buffer was mixed with lyophilized cells and ammonium persulfate. This suspension was then pumped drop by drop into in soybean oil supplemented with 0.06% (v/v) 3-(dimethylamino)-propionitril. During submerging in the oil phase, the droplets were hardened and induced to polymerize within the droplets. Particles with a volume ranging from 0.013-0.017 mL per bead containing a biomass concentration up to 38.0 g/L were prepared. The optimal condition for the deacylation of penicillin G to 6-aminopencillanic acid (6-APA) catalyzed by the immobilized whole-cell penicillin G acylase was found to be 45 degrees C and pH 8.0. Product inhibition of this enzyme by 6-APA could be eliminated by controlling pH value at 8 during the course of penicillin G hydrolysis using a pH-stat. Conversion determined by the pH-stat method were 0.3% higher than that by p-dimethylaminobenzaldehyde method. Cell concentration in the matrix was found to be an important factor influencing the maximum vel...Continue Reading

References

Feb 1, 1992·Enzyme and Microbial Technology·A A PrabhuneH SivaRaman
Jul 13, 1972·Biochimica Et Biophysica Acta·K BalasinghamM D Lilly

Citations

Jan 9, 2013·Applied Microbiology and Biotechnology·Petra ZajkoskaM Rosenberg

Related Concepts

Cell Density
Alkalescens-Dispar Group
Hydrogen-Ion Concentration
Hydrolysis
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Penicillin V Acylase
Polymethacrylic Acids
Log-Linear Models

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