Immobilization of inorganic pyrophosphatase on nanodiamond particles retaining its high enzymatic activity.
Biointerphases
; 10(4): 041005, 2015 Dec 21.
Article
in En
| MEDLINE
| ID: mdl-26489420
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 (â¼1 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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Inorganic Pyrophosphatase
/
Enzymes, Immobilized
/
Nanodiamonds
Language:
En
Journal:
Biointerphases
Journal subject:
BIOTECNOLOGIA
/
ENGENHARIA BIOMEDICA
Year:
2015
Document type:
Article
Affiliation country:
RUSSIA