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

Enzyme immobilization: The protease enzyme was successfully immobilized onto dicyclohexylcarbodiimide (DCC)‐activated metal–organic frameworks (MOFs). After separation by nano‐LC‐MS2 (liquid chromatography–mass spectrometry), detection, and database searching the protein digestion efficiency of tryp...

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Published inChemPlusChem (Weinheim, Germany) Vol. 77; no. 11; pp. 982 - 986
Main Authors Shih, Yung-Han, Lo, Sheng-Han, Yang, Ni-Shin, Singco, Brenda, Cheng, Yi-Jie, Wu, Cheng-You, Chang, I-Hsin, Huang, Hsi-Ya, Lin, Chia-Her
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag 01.11.2012
WILEY‐VCH Verlag
Subjects
enzyme immobilization
mass spectrometry
metal-organic framework
nanobiocatalysis
proteomics
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ISSN2192-6506
2192-6506
DOI10.1002/cplu.201200186

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Summary:Enzyme immobilization: The protease enzyme was successfully immobilized onto dicyclohexylcarbodiimide (DCC)‐activated metal–organic frameworks (MOFs). After separation by nano‐LC‐MS2 (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.
Bibliography:ark:/67375/WNG-JV0RXL9F-5
ArticleID:CPLU201200186
National Science Council of Taiwan - No. NSC-100-2632M-033-001-MY3
istex:CE30ACDCF73BC22968008FA207A2EE252E4F1321
ISSN:2192-6506
2192-6506
DOI:10.1002/cplu.201200186