Adsorption kinetics, conformational change, and enzymatic activity of β-glucosidase on hematite (α-Fe
Conformational change
Enzymatic activity
Enzyme-mineral interactions
Hematite surface
Protein adsorption
β-Glucosidase
Journal
Colloids and surfaces. B, Biointerfaces
ISSN: 1873-4367
Titre abrégé: Colloids Surf B Biointerfaces
Pays: Netherlands
ID NLM: 9315133
Informations de publication
Date de publication:
Sep 2020
Sep 2020
Historique:
received:
04
04
2020
revised:
27
04
2020
accepted:
05
05
2020
pubmed:
24
5
2020
medline:
7
4
2021
entrez:
24
5
2020
Statut:
ppublish
Résumé
Substantial fractions of extracellular enzymes are intimately associated with soil minerals, which may protect enzymes from denaturation, precipitation, proteolysis, or microbial consumption in soil environments. However, how mineral surface properties affect enzyme-mineral interactions and enzymatic activity of enzymes associated to mineral surface is still unclear. In the present study, adsorption behavior, conformational change, and enzymatic activity of β-glucosidase (BG) on hematite (001) face and (104) face, respectively, were investigated using in situ attenuated total reflectance FTIR spectroscopy and batch experiments. β-glucosidase undergoes greater conformational changes upon adsorption onto hematite (104) face than on hematite (001) face, probably due to the stronger protein-surface interactions on (104) face with the relatively higher surface hydroxyl density. On the other hand, the amount of BG sorbed on hematite (001) face was nearly two times higher than that on hematite (104) at the end of the 150-min adsorption experiments, due to the higher extent of conformational change in β-glucosidase on hematite (104) face. Correspondingly, the initial rate of cellobiose hydrolysis by per gram of β-glucosidase adsorbed on hematite (104) face was 1.7 times higher than that on hematite (001) face. However, when the density of hematite particles was same, the extent of cellobiose hydrolysis was 1.2 times higher on hematite (001) face than that on the (104) face, because of the higher adsorbed amount of β-glucosidase on the former. This study decoupled the effects of mineral surface properties on adsorption kinetics and conformational changes of soil enzymes bound to soil minerals and provided new insights into the correlation between mineral surface properties and catalytical activity of mineral-associated enzymes in soil environments.
Identifiants
pubmed: 32446160
pii: S0927-7765(20)30345-3
doi: 10.1016/j.colsurfb.2020.111115
pii:
doi:
Substances chimiques
Ferric Compounds
0
ferric oxide
1K09F3G675
beta-Glucosidase
EC 3.2.1.21
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
111115Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.