In this review, we detail the efforts performed to couple the purification and the immobilization of industrial enzymes in a single step. The use of antibodies, the …
A heterofunctional support for enzyme immobilization may be defined as that which possesses several distinct functionalities on its surface able to interact with a protein. We will …
MY Kiriukhin, KD Collins - Biophysical chemistry, 2002 - Elsevier
The role of ionized groups in biological systems is determined by their affinity for water [Biophys. J. 72 (1997) 65–76]. The tightly bound water associated with biologically important …
JA Queiroz, CT Tomaz, JMS Cabral - Journal of biotechnology, 2001 - Elsevier
In this article, an overview of hydrophobic interaction chromatography (HIC) of proteins is given. After a brief description of protein hydrophobicity and hydrophobic interactions, we …
Sepabeads‐EP (a new epoxy support) has been utilized to immobilize‐stabilize the enzyme penicillin G acylase (PGA) via multipoint covalent attachment. These supports are very …
Multifunctional supports containing epoxy groups are here proposed as a second generation of activated supports for covalent immobilization of enzymes following the epoxy …
The properties of a new commercially available amino-epoxy support (amino-epoxy- Sepabeads) for immobilizing enzymes have been compared to those of conventional epoxy …
R Freitag, F Garret-Flaudy - Langmuir, 2002 - ACS Publications
Simple salts are known to influence the cloud point temperature of the aqueous solution of thermoresponsive compounds, such as poly-(N-isopropylacrylamide), PNIPAM. The effect of …
WR Melander, Z El Rassi, C Horváth - Journal of Chromatography A, 1989 - Elsevier
The effect of salt on the retention behavior of proteins in electrostatic and hydrophobic interaction chromatography is described by a three-parameter equation, log k′= AB log m …