7 research outputs found
Expression and Stability of a Recombinant Plasmid in Zymomonas mobilis and Escherichia coli
Characterization and Replication Properties of the Zymomonas mobilis ATCC 10988 Plasmids pZMO1 and pZMO2
Kinetic constraints and features imposed by the immobilization of enzymes onto solid matrices: A key to advanced biotransformation
1045-1051The kinetics of immobilized enzymes can not
be analyzed by means of the simple Michaelis-Menten concept, which generally
fails to describe the immobilized state due to both its probable barriers, and
because the active concentration of the enzyme approaches, or even exceeds this
of its substrate(s). In such cases, the various experimental data are usually
treated by complex rate equations comprising too many parameters acquiring
different natures and meanings, depending on both the properties of the
immobilization state and the experimental conditions; thus, more likely, only
apparent values of the Michaelis-Menten kinetic parameters can be estimated
experimentally. Likewise, immobilization is often a key method in optimizing
the operational performance of enzymes, in both laboratory and industrial
scale, and affects considerably the kinetics in non-aqueous and
non-conventional media due to several issues as the structural changes of the
enzyme molecule, the heterogeneity of the system, and the partial or total
absence of water. In this work a theoretical approach is described on the
formulation of simplified rate equations, reflecting also the actual mass
balances of the reactants, in the case where esterification synthetic reactions
are catalyzed by immobilized lipases, in either a non-aqueous organic solvent
or in a non-solvent system
Correction to: Molecular, biochemical and kinetic analysis of a novel, thermostable lipase (LipSm) from Stenotrophomonas maltophilia Psi‑1, the first member of a new bacterial lipase family (XIX)
We have recently (8th February 2018) published our article entitled “Molecular, biochemical and kinetic analysis of a novel, thermostable lipase (LipSm) from Stenotrophomonas maltophilia Psi-1, the first member of a new bacterial lipase family (XVIII)” [1]. While our manuscript was going through the final stages of publication, an article by Samoylova et al. [2] was published (12th January 2018) in the journal Extremophiles, entitled “Cloning, expression and characterization of the esterase estUT1 from Ureibacillus thermosphaericus which belongs to a new lipase family XVIII”. Since we could not have known of the work of Samoylova et al. [2] when we submitted our manuscript, and in order to avoid confusion in the scientific community, we propose to reclassify LipSm as the first characterized member of the new bacterial lipase family XIX. Therefore throughout our article [1] “lipase family XVIII” should read “lipase family XIX” (title included)