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Chemical Modification of L-Asparaginase from Cladosporium Sp. for Improved Activity and Thermal Stability.
Mohan Kumar, N. S. and Vijay, Kishore and Manonmani, H. K. (2014) Chemical Modification of L-Asparaginase from Cladosporium Sp. for Improved Activity and Thermal Stability. Preparative Biochemistry and Biotechnology, 44 (5). pp. 433-450.
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Preparative Biochemistry and BiotechnologyVolume 44, Issue 5, July 2014, pages 433-450.pdf - Published Version Restricted to Registered users only Download (372kB) |
Abstract
L-Asparaginase (ASNase), an antileukemia enzyme, is facing problems with antigenicity in the blood. Modification of L-asparaginase from Cladosporium sp. was tried to obtain improved stability and improved functionality. In our experiment, modification of the enzyme was tried with bovine serum albumin, ovalbumin by crosslinking using glutaraldehyde, N-bromosuccinimide, and mono-methoxy polyethylene glycol. Modified enzymes were studied for activity, temperature stability, rate constants (kd), and protection to proteolytic digestion. Modification with ovalbumin resulted in improved enzyme activity that was 10-fold higher compared to native enzyme, while modification with bovine serum albumin through glutaraldehyde cross-linking resulted in high stability of L-asparaginase that was 8.5- and 7.62-fold more compared to native enzyme at 28�C and 37�C by the end of 24 hr. These effects were dependent on the quantity of conjugate formed. Modification also markedly prolonged L-asparaginase half-life and serum stability. N-Bromosuccinimidemodified ASNase presented greater stability with prolonged in vitro half-life of 144 hr to proteolytic digestion relative to unmodified enzyme (93 h). The present work could be seen as producing a modified L-asparaginase with improved activity and stability and can be a potential source for developing therapeutic agents for cancer treatment.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | chemical modification, in vitro half-life, L-asparaginase, thermal stability, tryptophan |
| Subjects: | 500 Natural Sciences and Mathematics > 07 Life Sciences > 03 Biochemistry & Molecular Biology > 07 Enzyme Biochemistry |
| Divisions: | Fermentation Technology and Bioengineering |
| Depositing User: | Food Sci. & Technol. Information Services |
| Date Deposited: | 28 May 2014 12:13 |
| Last Modified: | 28 May 2014 12:13 |
| URI: | http://ir.cftri.res.in/id/eprint/11587 |
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