Showing papers on "Penicillin amidase published in 1973"
TL;DR: The integrated from of the rate equation has been shown to predict satisfactorily the progress of the reaction in a batch reactor using either soluble or immobilized penicillin amidase, and to predict the performance of a continuous feed stirred tank reactor containing immobilized enzyme.
Abstract: A rate equation has been derived to describe the hydrolysis of benzylpenicillin to 6-aminopenicillanic acid by penicillin amidase. The integrated from of the rate equation has been shown to predict satisfactorily the progress of the reaction in a batch reactor using either soluble or immobilized penicillin amidase. The rate equation was also used to predict the performance of a continuous feed stirred tank reactor containing immobilized enzyme. There was good agreement with experimental measurements.
80 citations
TL;DR: Collagen was used as carrier for the immobilization of invertase, lysozyme, urease, glucose oxidase, penicillin amidase, Penicillin Amidase, and glucose isomerase.
Abstract: Collagen was used as carrier for the immobilization of invertase, lysozyme, urease, glucose oxidase, penicillin amidase, and glucose isomerase. Immobilization was accomplished by either impregnation of a preswollen collagen membrane with enzyme solution or electrocodeposition of collagen and enzyme from a collagen dispersion containing dissolved enzyme. The collagen-enzyme complexes prepared are in membrane form.
Membranous collagen-enzyme complexes were used to construct biocatalytic reactors such as the capillaric coil modular reactor. Such biocatalytic reactors were used in a recirculation system for the conversion of substrates. The biocatalytic reactors showed initial decreases of activity to stable limits which are maintained over a large number of reactor volume replacements. The stable limits correspond to approximately 35% of the initial activities for lysozyme and invertase, 25% for urease, 15% for glucose oxidase.
The mechanism of complex formation between collagen and enzyme involves multiple salt linkages, hydrogen bonds, and van der Waals interactions. This protein-protein interaction which leads to stable complexes by both impregnation and electrocodeposition processes is unique among the enzyme immobilization methods currently available.
65 citations
TL;DR: Penicillin amidase, an enzyme which hydrolyzes benzylpenicillin to 6‐aminopenicillanic acid and phenylacetic acid, is produced by Bacillus megaterium ATCC 14945 as an extracellular enzyme and this system was used as a model to examine the effects of nitrogen, sulfur, and phosphorous limitation on enzyme production in continuous culture.
Abstract: Summary Penicillin amidase, an enzyme which hydrolyzes benzylpenicillin to 6-aminopenicillanic acid and phenylacetic acid, is produced by Bacillus megaterium ATCC 14945 as an extracellular enzyme. We used this system as a model to examine the effects of nitrogen, sulfur, and phosphorous limitation on enzyme production in continuous culture. For these studies, we developed a minimal medium for B. megaterium which contained histidine as the sole nitrogen source. Batch experiments showed that this enzyme is produced as a growth-associated metabolite. Enzyme production was shown to be a function of the growth-limiting conditions and the concentration of the inducer, phenylacetic acid. Sulfur limitation in continuous culture yielded enzyme activities approximately three to five times those observed in nitrogen- and phosphorous-limited chemostats. These results are discussed in terms of the environment’s influence on enzyme production in continuous culture.
35 citations