期刊
COLLOIDS AND SURFACES B-BIOINTERFACES
卷 145, 期 -, 页码 785-794出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.colsurfb.2016.05.074
关键词
Graphene oxide; Nuclease P-1; Enzyme immobilization; Interface; Modification
资金
- National Outstanding Youth Foundation of China [21025625]
- National High-Tech Research and Development Program of China (863) [2012AA021200]
- National Key Technology RD Program [2012BAI44G01]
- National Natural Science Foundation of China [201390204, 21506090]
- Natural Science Foundation of Jiangsu [BK20130929, BK20140940]
- Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD)
The use of graphene oxide (GO) nanosheets for functional enzyme support has attracted intensive interest owing to their unique planar structure and intriguing physical and chemical properties. However, the detailed effects of the interface properties of GO and its functionalized derivatives on active biomolecules are not well understood. We immobilize nuclease P-1, a common industrial nucleic acid production enzyme, on pristine and amino poly(ethylene glycol) (PEG-NH2) modified GO nanosheets with interface property heterogeneity using two approaches, physical adsorption and chemical crosslinking. It is demonstrated that nuclease P-1 could be stable immobilized on the surface of pristine GO by physical adsorption and on the edge of modified GO nanosheets by chemical crosslinking. The resultant loading capacity of nuclease P-1 on pristine GO is as high as 6.45 mg/mg as a consequence of strong electrostatic and hydrophobic interactions between the enzyme and carrier. However, it is determined that the acid resistance, thermal stability, reusability and degradation efficiency of the immobilized enzyme on PEG-NH2-modified GO are obviously improved compared to those of the enzyme immobilized on pristine GO. The enhanced catalytic behavior demonstrates that GO and its derivatives have great potential in efficient biocatalytic systems. (C) 2016 Elsevier B.V. All rights reserved.
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