Trypsin-Immobilized Metal-Organic Framework as a Biocatalyst In Proteomics Analysis

被引：148

作者：

Shih, Yung-Han ^{[1
]}

Lo, Sheng-Han ^{[1
]}

Yang, Ni-Shin ^{[1
]}

Singco, Brenda ^{[1
]}

Cheng, Yi-Jie ^{[1
]}

Wu, Cheng-You ^{[1
]}

Chang, I-Hsin ^{[1
]}

Huang, Hsi-Ya ^{[1
]}

Lin, Chia-Her ^{[1
]}

机构：

[1] Chung Yuan Christian Univ, Dept Chem, Chungli 320, Taiwan

来源：

CHEMPLUSCHEM | 2012年 / 77卷 / 11期

关键词：

enzyme immobilization; mass spectrometry; metal-organic framework; nanobiocatalysis; proteomics; PROTEIN DIGESTION; MESOPOROUS SILICA; MASS-SPECTROMETRY; COORDINATION POLYMERS; ENZYME-IMMOBILIZATION; HYDROGEN STORAGE; PROTEOLYSIS; ADSORPTION; CATALYSIS; NANOPARTICLES;

D O I：

10.1002/cplu.201200186

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Enzyme immobilization: The protease enzyme was successfully immobilized onto dicyclohexylcarbodiimide (DCC)-activated metal-organic frameworks (MOFs). After separation by nano-LCMS2 (liquid chromatography-mass spectrometry), detection, and database searching the protein digestion efficiency of trypsin-MOF was comparable to traditional in-solution digestion (see figure). Furthermore, the trypsin-MOF was reusable. © 2012 Wiley-VCH Verlag GmbH&Co. KGaA, Weinheim.

引用

页码：982 / 986

页数：5

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