Showing papers on "Penicillin amidase published in 1977"

Penicillin amidase from E. coli. Some physicochemical properties of the enzyme incorporated into polyacrylamide gel

Abstract: The physico-chemical properties of penicillinamidase (PA) immobilized in polyacrylamide gel (IPA) were investigated. It was shown that simple incorporation of PA into polyacrylamide gel was not effective because of gradual washing out of the enzyme. The use of a complex method for the immobilization (immobilization in the presence of a linking agent) resulted in higher stability of IPA, the choice of the optimal ratio of the reagents being of paramount importance. The mechanical strength of IPA was studied in model experiments.

[Penicillin amidase from E. coli. A direct spectrophotometric method of determining the enzyme's activity].

Abstract: A method for determination of the enzymatic activity of penicillinamidas (PA) based on spectrophotometric estimation of the stained product amount produced in hydrolysis of 4-phenylacetamido-2-nitrobenzoic acid (PANBA) catalyzed by the enzyme is proposed. Some physico-chemical properties of the substrate and the stained product were studied. The kinetic parameters of the PANABA enzymatic hydrolysis were determined. Catalytic activity of some enzyme products of PA of different purity levels was studied comparatively in reactions of PANBA and benzylpenicillin hydrolysis.

Novel developments for the production of 6APA in the penicillin g fermentation plant by using fiber-entrapped penicillin amidase

Abstract: The production of 6APA by enzymatic hydrolysis of penicillin G can be integrated with the production of penicillin G. The penicillin G solutions obtained during the extraction from the fermented broth can be directly hydrolyzed to 6APA and phenyl acetic acid. The 6APA is then recovered while the phenyl acetic acid can also be recovered and recycled to the fermentation plant. Some of the results obtained by the research work performed by SNAM Progetti in their Microbiological Laboratories with the advice of Biochem Design are presented and analyzed. The economic potential of the integrated process is discussed.

Penicillin amidase from E. coli. A comparative study of the stability of penicillin amidase immobilized by various means

Abstract: The properties of immobilized penicillinamidases prepared by different methods were studied. Immobilization of penicillinamidase was achieved by using the covalend binding ion exchange sorption, incorporation into gel and other procedures. The effect of the carrier type, purification level of the native enzyme and other factors on stability of the immobilized preparations was studied. In 4 cases significant stabilization of the enzyme in the immobilized state was observed, while in 3 cases destabilization was registered.