z-logo
Premium
Conformational changes of enzymes adsorbed at liquid– solid interface: Relevance to enzymatic activity
Author(s) -
Noinville S.,
Revault M.,
Baron M.H.
Publication year - 2002
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10117
Subject(s) - chemistry , adsorption , lipase , solvation , hydrophobic effect , enzyme , hydrolysis , conformational isomerism , organic chemistry , crystallography , stereochemistry , molecule
FTIR with attenuated total reflectance spectroscopy was used to study in situ adsorption of enzymes at water–solid interfaces to better understand how conformational changes may monitor enzymatic activity. Because the adsorption process depends on hydrophobic and electrostatic interactions, conformational changes were studied as a function of the nature of the adsorbing substrates, which are hydrophobic or hydrophilic in character. The adsorption kinetics of two examples of serine enzymes, α‐chymotrypsin (α‐chym) and Humicola lanuginosa lipase (HLL), were studied. The secondary structure and solvation of the adsorbed enzymes were both compared to the dissolved enzymes. The positively charged α‐ chym was adsorbed on a negatively charged hydrophilic support with minor structural changes, but the negatively charged lipase had no affinity for a similar support. Both enzymes were strongly retained on the hydrophobic support. The secondary and tertiary structures of the α‐chym adsorbed on the hydrophobic support were strongly altered, which correlates to the inhibition of enzymatic hydrolysis. The specific solvation obtained for the adsorbed HLL is consistent with the existence of the open conformer in relation to the enhanced enzymatic activity at the water–hydrophobic interface. © 2002 Wiley Periodicals, Inc. Biopolymers (Biospectroscopy) 67: 323–326, 2002

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here