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Chemical modification of glucose oxidase: possible formation of molten globule‐like intermediate structure
Author(s) -
Hosseinkhani Saman,
Ranjbar Bijan,
Naderi-Manesh Hossein,
Nemat-Gorgani Mohsen
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00134-6
Subject(s) - chemical modification , molten globule , glucose oxidase , chemistry , circular dichroism , fluorescence , tryptophan , lysine , enzyme , chemical structure , conformational change , organic chemistry , biochemistry , amino acid , physics , quantum mechanics
Chemical modification of lysine residues in glucose oxidase was carried out using citraconic anhydride. Modification brought about changes in the kinetic properties of the enzyme as evident by substantial lowering of V max and K m . Enhancement of tryptophan fluorescence was observed with a dramatic change in its pH dependence due to modification. Near‐ and far‐UV circular dichroism spectra of the native and modified forms suggested formation of molten globule‐like structures, further supported by 8‐anilino‐1‐naphthalenesulfonic acid fluorescence which indicated higher exposure of hydrophobic residues as a result of chemical modification.