Microwalve-assisted enzyme-catalyzed reactions in various solvent systems

被引：86

作者：

Lin, SS ^{[1
]}

Wu, CH ^{[1
]}

Sun, MC ^{[1
]}

Sun, CM ^{[1
]}

Ho, YP ^{[1
]}

机构：

[1] Natl Dong Hwa Univ, Dept Chem, Hualien 974, Taiwan

来源：

JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY | 2005年 / 16卷 / 04期

关键词：

D O I：

10.1016/j.jasms.2005.01.012

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The work describes the accelerated enzymatic digestion of several proteins in various solvent systems under microwave irradiation. The tryptic fragments of the proteins were analyzed by matrix-assisted laser desorption/ionization mass spectrometry. Under the influence of rapid microwave heating, these enzymatic reactions can proceed in a solvent such as chloroform, which, under traditional digestion conditions, renders the enzyme inactive. The digestion efficiencies and Sequence coverages were increased when the trypsin digestions occurred in acetonitrile-, methanol- and chloroform-containing solutions that were heated under microwave irradiation for 10 min using a commercial microwave applicator. The percentage of the protein digested under microwave irradiation increased with the relative acetonitrile content, but decreased as the methanol content was increased. These observations suggest that acetonitrile does not deactivate the enzyme during the irradiation period; in contrast, methanol does deactivate it. In all cases, the digestion efficiencies under microwave irradiation exceed those under conventional conditions. (J Am Soc Mass Spectrom 2005, 16, 581-588) (c) 2005 American Society for Mass Spectrometry

引用

页码：581 / 588

页数：8

共 32 条

[1] Microwave enhanced Akabori reaction for peptide analysis [J].