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Trypsin‐Immobilized Metal–Organic Framework as a Biocatalyst In Proteomics Analysis
Author(s) -
Shih YungHan,
Lo ShengHan,
Yang NiShin,
Singco Brenda,
Cheng YiJie,
Wu ChengYou,
Chang IHsin,
Huang HsiYa,
Lin ChiaHer
Publication year - 2012
Publication title -
chempluschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.801
H-Index - 61
ISSN - 2192-6506
DOI - 10.1002/cplu.201200186
Subject(s) - trypsin , chemistry , biocatalysis , metal organic framework , mass spectrometry , chromatography , immobilized enzyme , combinatorial chemistry , enzyme , organic chemistry , catalysis , reaction mechanism , adsorption
Enzyme immobilization : The protease enzyme was successfully immobilized onto dicyclohexylcarbodiimide (DCC)‐activated metal–organic frameworks (MOFs). After separation by nano‐LC‐MS 2 (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.