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Chemical modification of chloroperoxidase for enhanced stability and activity

Authorized Users Only
2014
Authors
Pešić, Milja
Božić, Nataša
Lopez, Carmen
Lončar, Nikola
Alvaro, Gregorio
Vujčić, Zoran
Article (Published version)
Metadata
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Abstract
Chloroperoxidase from Caldariomyces fumago (CPO, EC 1.11.1.10) is one of the most interesting enzymes from the group of heme peroxidases and has been extensively applied in synthetic processes. Nevertheless, the practical application of CPO is limited due to its very low operational stability, especially in the presence of peroxidative compounds. For this reason, effect of chemical modifications of CPO in the stability of the enzyme was studied. Side-chain selective modifications of amino groups of Lys residues, and carboxyl groups of Asp and Glu residues, as well as crosslinking and periodate oxidation of sugar moiety were carried out. The stability of modified CPOs was evaluated at elevated pH and temperature, and in the presence of tert-butyl hydroperoxide. Effect of modification of CPO on the performance of the reaction of Cbz-ethanolamine oxidation was studied as well. Those modifications that involved carboxyl groups via carbodiimide coupled method and the periodate oxidation of ...the sugar moiety produced better catalysts than native CPO in terms of stability and activity at elevated pH values and temperatures.

Keywords:
Chemical modifications / Chloroperoxidase from Caldariomyces fumago / Cbz-ethanolamine oxidation / Cbz-glycinal synthesis / Peroxide dependent inactivation
Source:
Process Biochemistry, 2014, 49, 9, 1472-1479
Publisher:
  • Elsevier Sci Ltd, Oxford
Funding / projects:
  • Production, purification and characterization of enzymes and small molecules and their application as soluble or immobilized in food biotechnology, biofuels production and environmental protection (RS-172048)
  • Spanish MICINN [CTQ2011-28398-CO2-01]
  • Joint Serbian-Spanish Action [A IB2010 SE-00122]
Note:
  • The peer-reviewed version: http://cer.ihtm.bg.ac.rs/handle/123456789/3162

DOI: 10.1016/j.procbio.2014.05.025

ISSN: 1359-5113

WoS: 000341549600013

Scopus: 2-s2.0-84906787968
[ Google Scholar ]
5
5
URI
https://cer.ihtm.bg.ac.rs/handle/123456789/1428
Collections
  • Radovi istraživača / Researchers' publications
Institution/Community
IHTM
TY  - JOUR
AU  - Pešić, Milja
AU  - Božić, Nataša
AU  - Lopez, Carmen
AU  - Lončar, Nikola
AU  - Alvaro, Gregorio
AU  - Vujčić, Zoran
PY  - 2014
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1428
AB  - Chloroperoxidase from Caldariomyces fumago (CPO, EC 1.11.1.10) is one of the most interesting enzymes from the group of heme peroxidases and has been extensively applied in synthetic processes. Nevertheless, the practical application of CPO is limited due to its very low operational stability, especially in the presence of peroxidative compounds. For this reason, effect of chemical modifications of CPO in the stability of the enzyme was studied. Side-chain selective modifications of amino groups of Lys residues, and carboxyl groups of Asp and Glu residues, as well as crosslinking and periodate oxidation of sugar moiety were carried out. The stability of modified CPOs was evaluated at elevated pH and temperature, and in the presence of tert-butyl hydroperoxide. Effect of modification of CPO on the performance of the reaction of Cbz-ethanolamine oxidation was studied as well. Those modifications that involved carboxyl groups via carbodiimide coupled method and the periodate oxidation of the sugar moiety produced better catalysts than native CPO in terms of stability and activity at elevated pH values and temperatures.
PB  - Elsevier Sci Ltd, Oxford
T2  - Process Biochemistry
T1  - Chemical modification of chloroperoxidase for enhanced stability and activity
VL  - 49
IS  - 9
SP  - 1472
EP  - 1479
DO  - 10.1016/j.procbio.2014.05.025
ER  - 
@article{
author = "Pešić, Milja and Božić, Nataša and Lopez, Carmen and Lončar, Nikola and Alvaro, Gregorio and Vujčić, Zoran",
year = "2014",
abstract = "Chloroperoxidase from Caldariomyces fumago (CPO, EC 1.11.1.10) is one of the most interesting enzymes from the group of heme peroxidases and has been extensively applied in synthetic processes. Nevertheless, the practical application of CPO is limited due to its very low operational stability, especially in the presence of peroxidative compounds. For this reason, effect of chemical modifications of CPO in the stability of the enzyme was studied. Side-chain selective modifications of amino groups of Lys residues, and carboxyl groups of Asp and Glu residues, as well as crosslinking and periodate oxidation of sugar moiety were carried out. The stability of modified CPOs was evaluated at elevated pH and temperature, and in the presence of tert-butyl hydroperoxide. Effect of modification of CPO on the performance of the reaction of Cbz-ethanolamine oxidation was studied as well. Those modifications that involved carboxyl groups via carbodiimide coupled method and the periodate oxidation of the sugar moiety produced better catalysts than native CPO in terms of stability and activity at elevated pH values and temperatures.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Process Biochemistry",
title = "Chemical modification of chloroperoxidase for enhanced stability and activity",
volume = "49",
number = "9",
pages = "1472-1479",
doi = "10.1016/j.procbio.2014.05.025"
}
Pešić, M., Božić, N., Lopez, C., Lončar, N., Alvaro, G.,& Vujčić, Z.. (2014). Chemical modification of chloroperoxidase for enhanced stability and activity. in Process Biochemistry
Elsevier Sci Ltd, Oxford., 49(9), 1472-1479.
https://doi.org/10.1016/j.procbio.2014.05.025
Pešić M, Božić N, Lopez C, Lončar N, Alvaro G, Vujčić Z. Chemical modification of chloroperoxidase for enhanced stability and activity. in Process Biochemistry. 2014;49(9):1472-1479.
doi:10.1016/j.procbio.2014.05.025 .
Pešić, Milja, Božić, Nataša, Lopez, Carmen, Lončar, Nikola, Alvaro, Gregorio, Vujčić, Zoran, "Chemical modification of chloroperoxidase for enhanced stability and activity" in Process Biochemistry, 49, no. 9 (2014):1472-1479,
https://doi.org/10.1016/j.procbio.2014.05.025 . .

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