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Penicillin amidase

About: Penicillin amidase is a research topic. Over the lifetime, 576 publications have been published within this topic receiving 15563 citations. The topic is also known as: penicillin amidohydrolase & ampicillin acylase.


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Journal ArticleDOI
TL;DR: This review describes the most recent developments in the biotechnological applications of penicillin acylases, including advances in detection of new enzyme specificities towards other natural penicillins, enzyme immobilization, and optimization of enzyme-catalyzed hydrolysis and synthesis in the presence of organic solvents.
Abstract: This review describes the most recent developments in the biotechnological applications of penicillin acylases. This group of enzymes is involved mainly in the industrial production of 6-aminopenicillanic acid and the synthesis of semisynthetic β-lactam antibiotics. In addition, penicillin acylases can also be employed in other useful biotransformations, such as peptide synthesis and the resolution of racemic mixtures of chiral compounds. Particular emphasis is placed on advances in detection of new enzyme specificities towards other natural penicillins, enzyme immobilization, and optimization of enzyme-catalyzed hydrolysis and synthesis in the presence of organic solvents.

187 citations

Journal ArticleDOI
TL;DR: A novel method for the immobilization of penicillin G acylase involves the physical aggregation of the enzyme, followed by chemical cross-linking to form insoluble cross-linked enzyme aggregates (CLEAs) that possess a high specific activity as well as a high productivity and synthesis/hydrolysis ratio in the synthesis of semi-synthetic antibiotics in aqueous media.
Abstract: A novel method for the immobilization of penicillin G acylase (penicillin amidohydrolase, EC 35111) is reported It involves the physical aggregation of the enzyme, followed by chemical cross-linking to form insoluble cross-linked enzyme aggregates (CLEAs) Compared with conventionally immobilized penicillin G acylases, these CLEAs possess a high specific activity as well as a high productivity and synthesis/hydrolysis (S/H) ratio in the synthesis of semi-synthetic antibiotics in aqueous media Moreover, they are active in a broad range of polar and apolar organic solvents

150 citations

Journal ArticleDOI
TL;DR: A strategy for immobilization-stabilization of penicillin G acylase from E.coli by multipoint covalent attachment to agarose (aldehyde) gels is developed, able to prepare very active and very stable PGA derivatives containing up to 200 International Units of catalytic activity per mL.
Abstract: We have developed a strategy for immobilization-stabilization of penicillin G acylase from E. coli, PGA, by multipoint covalent attachment to agarose (aldehyde) gels. We hve studied the role of three main variables that control the intensity of these enzyme-support multiinteraction processes: 1. surface density of aldehyde groups in the activated support; 2. temperature; and 3. contact-time between the immobilized enzyme and the activated support prior to borohydride reduction of the derivatives. Different combinations of these three variables have been tested to prepare a number of PGA-agarose derivatives. All these derivatives preserve 100% of catalytic activity corresponding to the soluble enzyme that has been immobilized but they show very different stability. The less stable derivative has exactly the same thermal stability of soluble penicillin G acylase and the most stable one is approximately 1,400 fold more stable. A similar increase in the stability of the enzyme against the deleterious effect of organic solvents was also observed. On the other hand, the agarose aldehyde gels present a very great capacity to immobilize enzymes through multipoint covalent attachment. In this way, we have been able to prepare very active and very stable PGA derivatives containing up to 200 International Units of catalytic activity per mL. of derivative with 100% yields in the overall immobilization procedure.

145 citations

Journal ArticleDOI
TL;DR: Assay results show that mesoporous MCM-41 is a more effective support for the immobilization of Penicillin Acylase (PA) than many of other supports due to its structural and surface characteristics.
Abstract: Mesoporous MCM-41 having well ordered long-range structure, large pore diameters, narrow pore-size distribution, high pore volume and specific surface area has been synthesized. The surface of MCM-41 has an abundance of weakly acidic hydroxyl groups. Assay results show that MCM-41 is a more effective support for the immobilization of Penicillin Acylase (PA) than many of other supports due to its structural and surface characteristics. PA can be immobilized on MCM-41 through either direct immobilization or covalent coupling. The former gives higher activity of IME than the later. In the direct immobilization, PA molecules are immobilized on MCM-41 through the hydrogen-bonded interaction between hydroxyl groups of MCM-41 and carbonyl or amino groups in the PA molecule.

129 citations

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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20234
20222
20183
20175
20165
20153