Immobilization of inorganic pyrophosphatase on nanodiamond particles retaining its high enzymatic activity.

Abstract:

:Nanodiamond (ND) particles are popular platforms for the immobilization of molecular species. In the present research, enzyme Escherichia coli inorganic pyrophosphatase (PPase) was immobilized on detonation ND through covalent or noncovalent bonding and its enzymatic activity was characterized. Factors affecting adsorption of PPase such as ND size and surface chemistry were studied. The obtained material is a submicron size association of ND particles and protein molecules in approximately equal amounts. Both covalently and noncovalently immobilized PPase retains a significant enzymatic activity (up to 95% of its soluble form) as well as thermostability. The obtained hybrid material has a very high enzyme loading capacity (∼1 mg mg(-1)) and may be considered as a promising delivery system of biologically active proteinaceous substances, particularly in the treatment of diseases such as calcium pyrophosphate crystal deposition disease and related pathologies. They can also be used as recoverable heterogeneous catalysts in the traditional uses of PPase.

journal_name

Biointerphases

journal_title

Biointerphases

authors

Rodina EV,Valueva AV,Yakovlev RY,Vorobyeva NN,Kulakova II,Lisichkin GV,Leonidov NB

doi

10.1116/1.4934483

subject

Has Abstract

pub_date

2015-12-21 00:00:00

pages

041005

issue

4

eissn

1934-8630

issn

1559-4106

journal_volume

10

pub_type

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