z-logo
open-access-imgOpen Access
Clay Minerals Change the Toxic Effect of Cadmium on the Activities of Leucine Aminopeptidase
Author(s) -
Shunyu Huang,
Jingji Li,
Jipeng Wang
Publication year - 2021
Publication title -
adsorption science and technology
Language(s) - English
Resource type - Journals
eISSN - 2048-4038
pISSN - 0263-6174
DOI - 10.1155/2021/1024085
Subject(s) - kaolinite , aminopeptidase , cadmium , leucyl aminopeptidase , chemistry , montmorillonite , substrate (aquarium) , clay minerals , hydrolysis , leucine , enzyme assay , enzyme , nuclear chemistry , food science , biochemistry , mineralogy , amino acid , organic chemistry , biology , ecology
Soil leucine aminopeptidase (LAP) is a hydrolytic enzyme involved in the acquisition of nitrogen by microorganisms. In contaminated soils, LAP activity is affected not only by the type and concentration of heavy metals but also by the form of enzyme. Here, we investigated the degree and mechanism of cadmium (Cd) inhibition of soil LAP and purified LAP. We also examined the effect of montmorillonite and kaolinite on LAP and LAP contaminated with Cd. The results showed that Cd inhibition of LAP activity increased with increasing Cd concentration and that Cd exerted noncompetitive inhibition of LAP. The addition of clay minerals decreases LAP activity and the maximum reaction rate ( V max ), regardless of the presence of Cd. Montmorillonite decreases the affinity of LAP to the substrate ( K m ), while kaolinite increases the affinity of LAP to the substrate. The clay mineral-immobilized LAP showed an increase in resistance to Cd contamination compared with the free LAP. The results obtained in this study may aid in understanding the toxic effects of heavy metals on soil enzymes.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom