Journal ArticleDOI
Improving enzymes by using them in organic solvents
Reads0
Chats0
TLDR
The technological utility of enzymes can be enhanced greatly by using them in organic solvents rather than their natural aqueous reaction media, and they have found numerous potential applications, some of which are already commercialized.Abstract:
The technological utility of enzymes can be enhanced greatly by using them in organic solvents rather than their natural aqueous reaction media. Studies over the past 15 years have revealed not only that this change in solvent is feasible, but also that in such seemingly hostile environments enzymes can catalyse reactions impossible in water, become more stable, and exhibit new behaviour such as 'molecular memory'. Of particular importance has been the discovery that enzymatic selectivity, including substrate, stereo-, regio- and chemoselectivity, can be markedly affected, and sometimes even inverted, by the solvent. Enzyme-catalysed reactions in organic solvents, and even in supercritical fluids and the gas phase, have found numerous potential applications, some of which are already commercialized.read more
Citations
More filters
Journal ArticleDOI
Water follows polar and nonpolar protein surface domains.
TL;DR: The results demonstrate that the water−amino acid degree of correlation follows the same trend as the amino acid contribution in proteins solubility, namely, the negatively charged amino acids are the most beneficial for protein solubilty, then the positively charge amino acids, and finally the charge-neutral amino acids.
Journal ArticleDOI
Part per trillion label-free electronic bioanalytical detection.
Maria Magliulo,Antonia Mallardi,Roberto Gristina,Francesca Ridi,Luigia Sabbatini,Nicola Cioffi,Gerardo Palazzo,Gerardo Palazzo,Luisa Torsi +8 more
TL;DR: A Functional Bio-Interlayer Organic Field-Effect Transistor (FBI-OFET) sensor, embedding a streptavidin protein capturing layer, capable of performing label-free selective electronic detection of biotin at 3 part per trillion (mass fraction) or 15 pM, is proposed here.
Journal ArticleDOI
The thioesterase domain from a nonribosomal peptide synthetase as a cyclization catalyst for integrin binding peptides.
TL;DR: Evidence is provided for TycC TE as a versatile macrocyclization catalyst and the prospect of using TE catalysis for the generation of diverse macrocyclic peptide libraries that can be probed for novel biological function is raised.
Journal ArticleDOI
Relation between pore sizes of protein crystals and anisotropic solute diffusivities.
Aleksandar Cvetkovic,Cristian Picioreanu,Adrie J. J. Straathof,Rajamani Krishna,Luuk A.M. van der Wielen +4 more
TL;DR: The origin ofsolute diffusion anisotropy can be found in the packing of the protein molecules in the crystals, which determines the crystal pore organization, and proves that size exclusion is the key mechanism for solute diffusion in protein crystals.
Journal ArticleDOI
Highly Selective Enzymatic Kinetic Resolution of Primary Amines at 80 °C: A Comparative Study of Carboxylic Acids and Their Ethyl Esters as Acyl Donors
TL;DR: Optimization of the kinetic resolution of 2-amino-4-phenyl-butane was achieved at 80 degrees C using CAL-B-catalyzed aminolysis of carboxylic acids and their ethyl esters using long chain esters and the corresponding acids as acyl donors with remarkably high enantioselectivity.
References
More filters
Book
Principles of Biochemistry
TL;DR: The third edition, coming ten years after the first, emphasizes both the flowering of biochemical research and the prodigious effort by busy teachers and scientists to keep up to date this popular text and reference.
Book
Hydrogen Bonding in Biological Structures
TL;DR: In this article, the van der Waals Radii cut-off criterion is used to define the strong and weak hydrogen-bond configurations, as well as the relationship between two-center and three-center hydrogen bonds.
Book
Structure and Mechanism in Protein Science
TL;DR: The three-dimensional structure of proteins chemical catalysis the basic equations of enzyme kinetics measurement and magnitude of enzymatic rate constants the pH dependence of enzyme catalysis practical kinetics detection of intermediaries in reactions by kinetics stereochemistry of enzymes reactions active-site-directed and enzyme-activated irreversible inhibitors - affinity labels and suicide inhibitors conformational change, allosteric regulation, motors and work forces between molecules, and enzymesubstrate binding energies enzyme-substrate complementarity and the use of binding energy in catalysis specificity and editing mechanisms recombinant DNA technology case studies of enzyme
Journal ArticleDOI
Quantitative analyses of biochemical kinetic resolutions of enantiomers
BookDOI
Structure and Mechanism in Protein Science : a guide to enzyme catalysis and protein folding
TL;DR: The three-dimensional structure of proteins chemical catalysis, kinetics measurement and magnitude of enzymatic rate constants, and the use of binding energy in catalysis specificity and editing mechanisms are studied.