Unknown

Dataset Information

0

Controlling enzymatic activity by immobilization on graphene oxide.


ABSTRACT: In this study, graphene oxide (GO) has been applied as a matrix for enzyme immobilization. The protein adsorption capacity of GO is much higher than of other large surface area carbonaceous materials. Its structure and physicochemical properties are reported beneficial also for enzymatic activity modifications. The experimental proof was done here that GO-based biocatalytic systems with immobilized catalase are modifiable in terms of catalyzed reaction kinetic constants. It was found that activity and stability of catalase, considered here as model enzyme, closely depend on enzyme/GO ratio. The changes in kinetic parameters can be related to secondary structure alterations. The correlation between enzyme/GO ratio and kinetic and structure parameters is reported for the first time and enables the conscious control of biocatalytic processes and their extended applications. The biological activity of obtained biocatalytic systems was confirmed in vitro by the use of functional test. The addition of immobilized catalase improved the cells' viability after they were exposed to hydrogen peroxide and tert-butyl-hydroperoxide used as source of reactive oxygen species.

SUBMITTER: Bolibok P 

PROVIDER: S-EPMC5374183 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

Controlling enzymatic activity by immobilization on graphene oxide.

Bolibok Paulina P   Wiśniewski Marek M   Roszek Katarzyna K   Terzyk Artur P AP  

Die Naturwissenschaften 20170330 3-4


In this study, graphene oxide (GO) has been applied as a matrix for enzyme immobilization. The protein adsorption capacity of GO is much higher than of other large surface area carbonaceous materials. Its structure and physicochemical properties are reported beneficial also for enzymatic activity modifications. The experimental proof was done here that GO-based biocatalytic systems with immobilized catalase are modifiable in terms of catalyzed reaction kinetic constants. It was found that activi  ...[more]

Similar Datasets

| S-EPMC3062704 | biostudies-literature
| S-EPMC6718962 | biostudies-literature
| S-EPMC6449378 | biostudies-literature
| S-EPMC7081415 | biostudies-literature
| S-EPMC3863589 | biostudies-literature
| S-EPMC8533581 | biostudies-literature
| S-EPMC6582274 | biostudies-literature
| S-EPMC6003706 | biostudies-literature
| S-EPMC8781742 | biostudies-literature
| S-EPMC8002523 | biostudies-literature