Journal ArticleDOI
Recent biotechnological interventions for developing improved penicillin G acylases
Reads0
Chats0
TLDR
An overview of recent advances in the production, stabilization and application of PAC is provided, highlighting the recent biotechnological approaches for the improved catalysis of PAC.About:
This article is published in Journal of Bioscience and Bioengineering.The article was published on 2004-01-01. It has received 55 citations till now. The article focuses on the topics: Penicillin amidase & Penicillin.read more
Citations
More filters
Journal ArticleDOI
Mesoporous silica nanoparticles for bioadsorption, enzyme immobilisation, and delivery carriers
TL;DR: A comprehensive summary of the advances made in the last decade and a future outlook on possible applications of MSNs as nanocontainers for storage and delivery of biomolecules and some promising work on enzyme immobilisation using mesoporous silica nanoparticles are highlighted.
Journal ArticleDOI
Progress in enzyme immobilization in ordered mesoporous materials and related applications
Zhou Zhou,Martin Hartmann +1 more
TL;DR: This review focuses on the relation between the progress in ordered mesoporous materials and its corresponding contribution to enzyme immobilization as well as the applications of these materials in biocatalysis.
Journal ArticleDOI
Enzymes supported on ordered mesoporous solids: a special case of an inorganic–organic hybrid
TL;DR: The studies on enzymes immobilized on ordered mesoporous solids and the need for careful studies in real applications are reviewed and the emerging applications of related biomolecule–mesoporous solid hybrids in other applications are noted.
Journal ArticleDOI
The realm of penicillin G acylase in β-lactam antibiotics
TL;DR: The advancements made in PGA biotechnology are described and its simulation for production of β-lactam antibiotics is advocated.
Journal ArticleDOI
Structural features of Penicillin acylase adsorption on APTES functionalized SBA-15
TL;DR: In this paper, the effect of silica as a host matrix on the enzyme kinetics was investigated. And the authors found that the PGA enzyme is more stable than the soluble form to temperature and pH environments and retained 73% of its activity after immobilization.
References
More filters
Journal ArticleDOI
Rapid evolution of a protein in vitro by DNA shuffling.
TL;DR: It is reported here that selected mutants had a minimum inhibitory concentration of 640 μg ml-1, a 32,000-fold increase and 64-fold greater than any published TEM-1 derived enzyme.
Journal ArticleDOI
DNA shuffling of a family of genes from diverse species accelerates directed evolution
TL;DR: This work compared the efficiency of obtaining moxalactamase activity from four cephalosporinase genes evolved separately with that from a mixed pool of the four genes, and found the best clone contained eight segments from three of theFour genes as well as 33 amino-acid point mutations.
Journal ArticleDOI
A common export pathway for proteins binding complex redox cofactors
TL;DR: The precursor polypeptides of periplasmic proteins binding seven types of redox cofactor have unusually long signal sequences bearing a consensus (S/T)‐R‐ R‐x‐F‐L‐K motif immediately before the hydrophobic region that are suggested to share a common specialization in their export pathway.
Journal ArticleDOI
A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
James A. Brannigan,Guy Dodson,Guy Dodson,Helen J. Duggleby,Peter C. E. Moody,Peter C. E. Moody,Janet L. Smith,Diana R. Tomchick,Alexey G. Murzin +8 more
TL;DR: The name Ntn (N-terminal nucleophile) hydrolases is suggested for this structural superfamily of enzymes which appear to be evolutionarily related but which have diverged beyond any recog-nizable sequence similarity.
Journal ArticleDOI
Penicillin acylase has a single-amino-acid catalytic centre.
Helen J. Duggleby,S.P. Tolley,Christopher P. Hill,Christopher P. Hill,Eleanor J. Dodson,Guy Dodson,Peter C. E. Moody +6 more
TL;DR: The analysis shows that the environment of the catalytically active N-terminal serine of the B chain contains no adjacent histidine equivalent to that found in the serine proteases, indicating that this must be an important recognition site for cleavage.