Chemical modification of chloroperoxidase for enhanced stability and activity
2014
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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.
Кључне речи:
Chemical modifications / Chloroperoxidase from Caldariomyces fumago / Cbz-ethanolamine oxidation / Cbz-glycinal synthesis / Peroxide dependent inactivationИзвор:
Process Biochemistry, 2014, 49, 9, 1472-1479Издавач:
- Elsevier Sci Ltd, Oxford
Финансирање / пројекти:
- Производња, изоловање и карактеризација ензима и малих молекула и њихова примена у растворном и имобилизованом облику у биотехнологији хране, биогоривима и заштитити животне средине (RS-MESTD-Basic Research (BR or ON)-172048)
- Spanish MICINN [CTQ2011-28398-CO2-01]
- Joint Serbian-Spanish Action [A IB2010 SE-00122]
Напомена:
- This is the peer-reviewed version of the article: : Pesic M, Bozic N, Lopez C, Loncar N, Alvaro G, Vujcic Z, Chemical modification of chloroperoxidase for enhanced stability and activity, Process Biochemistry (2014), http://dx.doi.org/10.1016/j.procbio.2014.05.025
- http://cer.ihtm.bg.ac.rs/handle/123456789/1428
DOI: 10.1016/j.procbio.2014.05.025
ISSN: 1359-5113
WoS: 000341549600013
Scopus: 2-s2.0-84906787968
Институција/група
IHTMTY - 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/123456789/3162 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 . .