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Reversible and irreversible immobilization of enzymes on graphite fibrils TM
Author(s) -
Dong Liwen,
Fischer Alan B.,
Lu Ming,
Martin Mark T.,
Moy David,
Simpson David
Publication year - 1996
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/(sici)1099-1352(199634/12)9:5/6<383::aid-jmr269>3.0.co;2-z
Subject(s) - fibril , chemistry , horseradish peroxidase , biocatalysis , immobilized enzyme , enzyme , covalent bond , macromolecule , graphite , alkyl , biochemistry , organic chemistry , catalysis , reaction mechanism
Graphite Fibrils are hollow tubes (0.01 × 1–10 μm) consisting of concentric layers of graphite. Fibrils can be chemically modified to introduce surface functionalities such as carboxyl groups. Carboxylated fibrils were further functionalized to amino alkyl derivatives which were covalently linked to an enzyme, horseradish peroxidase (HRP). HRP fibrils showed substantial catalytic activity. Additionally, carboxyl fibrils were derivatized with specific inhibitors of the enzymes β‐galactosidase (β‐Gal) and alkaline phosphatase (AP). Enzyme inhibitor‐modified fibrils were used to specifically purify both β‐Gal (using β‐Gal inhibitor fibrils) and AP (using AP inhibitor fibrils) from mixtures of these two enzymes. These studies demonstrate the feasibility of using Graphite Fibrils as supports in biocatalysis and biospecific affinity chromatography.