Trypsin-immobilized metal-organic framework as a biocatalyst in proteomics analysis

  • Yung Han Shih
  • , Sheng Han Lo
  • , Ni Shin Yang
  • , Brenda Singco
  • , Yi Jie Cheng
  • , Cheng You Wu
  • , I. Hsin Chang
  • , Hsi Ya Huang*
  • , Chia Her Lin
  • *Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

166 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)982-986
Number of pages5
JournalChemPlusChem
Volume77
Issue number11
DOIs
Publication statusPublished - 2012 Nov
Externally publishedYes

Keywords

  • Enzyme immobilization
  • Mass spectrometry
  • Metal-organic framework
  • Nanobiocatalysis
  • Proteomics

ASJC Scopus subject areas

  • General Chemistry

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