Influence of the enzyme derivative preparation and substrate structure on the enantioselectivity of penicillin G acylase
- 1 July 2002
- journal article
- Published by Elsevier in Enzyme and Microbial Technology
- Vol. 31 (1-2) , 88-93
- https://doi.org/10.1016/s0141-0229(02)00070-4
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- Structural and Functional Stabilization of L‐Asparaginase via Multisubunit Immobilization onto Highly Activated SupportsBiotechnology Progress, 2001
- Ligand-induced conformational change in penicillin acylaseJournal of Molecular Biology, 1998
- Penicillin Acylase in the Industrial Production of β-Lactam AntibioticsOrganic Process Research & Development, 1998
- Preparation of activated supports containing low pK amino groups. A new tool for protein immobilization via the carboxyl coupling methodEnzyme and Microbial Technology, 1993
- Penicillin G acylase fromKluyvera citrophila new choice as industrial enzymeBiotechnology Letters, 1992
- Immobilization-stabilization of Penicillin G acylase fromEscherichia coliApplied Biochemistry and Biotechnology, 1990
- Expression, purification and crystallization of penicillin G acylase from Escherichia coli ATCC 11105Protein Engineering, Design and Selection, 1990
- Aldehyde-agarose gels as activated supports for immobilization-stabilization of enzymesEnzyme and Microbial Technology, 1988
- Approach to the use of benzylpenicillin acylase for configurational correlations of amino compounds. 2. Hydrolysis of N-(p-aminophenylacetyl) derivatives of some chiral primary aminesThe Journal of Organic Chemistry, 1979
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976