Stabilization of D-hydantoinase by intersubunit cross-linking

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It was observed that tetrameric D-hydantoinase from Bacillus stearothermophilus SD1 is dissociated into monomers under operational conditions, resulting in a detrimental loss of its catalytic activity. As an approach to reduce the dissociation of subunits and to maintain its catalytic activity, intersubunit cross-linking was attempted by using EDC (1-ethyl-3-(3-dimethylaminopropyl) carbodiimide, hydrochloride). The cross-linking conditions were optimized in terms of stabilization and catalytic activity of the recovered enzyme. Cross-linked D-hydantoinase showed a four-fold longer half-life under operational conditions and was very stable even at an elevated temperature, whereas the native enzyme was almost completely deactivated. In addition, intersubunit cross-linking of D-hydantoinase also led to stabilization of the enzyme in the presence of 20% methanol and under acidic conditions. The cross-linked enzyme was more efficient in the conversion of substrate, which seems to be due to the increased stability of enzyme. (C) 2000 Elsevier Science B.V. All rights reserved.
Publisher
ELSEVIER SCIENCE BV
Issue Date
2000
Language
English
Article Type
Article
Keywords

THERMOSTABLE D-HYDANTOINASE; BACILLUS-STEAROTHERMOPHILUS SD-1; ENZYME; CROSSLINKING; INACTIVATION; EXPRESSION; STABILITY; PROTEINS

Citation

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, v.11, no.1, pp.29 - 35

ISSN
1381-1177
DOI
10.1016/S1381-1177(00)00193-4
URI
http://hdl.handle.net/10203/14275
Appears in Collection
BS-Journal Papers(저널논문)
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