Immobilized trypsin on hydrophobic cellulose decorated nanoparticles shows good stability and reusability for protein digestion

NWIPB OpenIR

	Immobilized trypsin on hydrophobic cellulose decorated nanoparticles shows good stability and reusability for protein digestion
	Sun, XX ; Cai, XD ; Wang, RQ ; Xiao, JX
	2015
发表期刊	ANALYTICAL BIOCHEMISTRY
摘要	The preparation of biocatalysts based on immobilized trypsin is of great importance for both proteomic research and industrial applications. Here, we have developed a facile method to immobilize trypsin on hydrophobic cellulose-coated silica nanoparticles by surface adsorption. The immobilization conditions for the trypsin enzyme were optimized. The as-prepared biocatalyst was characterized by Fourier transform infrared spectroscopy, transmission electron microscopy, and elemental analysis. In comparison with free enzyme, the immobilized trypsin exhibited greater resistances against thermal inactivation and denaturants. In addition, the immobilized trypsin showed good durability for multiple recycling. The general applicability of the immobilized trypsin for proteomic studies was confirmed by enzymatic digestion of two widely used protein substrates: bovine serum albumin (BSA) and cytochrome c. The surface adsorption protocols for trypsin immobilization may provide a promising strategy for enzyme immobilization in general, with great potential for a range of applications in proteomic studies. (C) 2015 Elsevier Inc. All rights reserved.; The preparation of biocatalysts based on immobilized trypsin is of great importance for both proteomic research and industrial applications. Here, we have developed a facile method to immobilize trypsin on hydrophobic cellulose-coated silica nanoparticles by surface adsorption. The immobilization conditions for the trypsin enzyme were optimized. The as-prepared biocatalyst was characterized by Fourier transform infrared spectroscopy, transmission electron microscopy, and elemental analysis. In comparison with free enzyme, the immobilized trypsin exhibited greater resistances against thermal inactivation and denaturants. In addition, the immobilized trypsin showed good durability for multiple recycling. The general applicability of the immobilized trypsin for proteomic studies was confirmed by enzymatic digestion of two widely used protein substrates: bovine serum albumin (BSA) and cytochrome c. The surface adsorption protocols for trypsin immobilization may provide a promising strategy for enzyme immobilization in general, with great potential for a range of applications in proteomic studies. (C) 2015 Elsevier Inc. All rights reserved.
文献类型	期刊论文
条目标识符	http://210.75.249.4/handle/363003/17336
专题	中国科学院西北高原生物研究所
推荐引用方式 GB/T 7714	Sun, XX,Cai, XD,Wang, RQ,et al. Immobilized trypsin on hydrophobic cellulose decorated nanoparticles shows good stability and reusability for protein digestion[J]. ANALYTICAL BIOCHEMISTRY,2015.
APA	Sun, XX,Cai, XD,Wang, RQ,&Xiao, JX.(2015).Immobilized trypsin on hydrophobic cellulose decorated nanoparticles shows good stability and reusability for protein digestion.ANALYTICAL BIOCHEMISTRY.
MLA	Sun, XX,et al."Immobilized trypsin on hydrophobic cellulose decorated nanoparticles shows good stability and reusability for protein digestion".ANALYTICAL BIOCHEMISTRY (2015).