TY  - CONF
AU  - Zelenović, Jelena
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2017
UR  - http://www.bds.org.rs/en/conferences.php
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3282
AB  - Cellulase (EC 3.2.1.4) are important enzymes in food, paper, textile, detergent and biofuel industries. Most cellulases have low activity and stability. Improving these properties would have substantial impact on numerous industrial processes. Enzymatic properties can be improved by directed evolution, but the screening process is the limiting step. Coupled cellulase assay has been developed in order to improve the screening process. This method does not require boiling samples and allows rapid screening of mutants in a microtiter plate. The aim of this study was to establish enzyme coupled assay where cellulase first hydrolyzes carboxymethylcellulose (CMC), and cellobioses dehydrogenase (CBDH) and dichlorophenolindophenol (DCPIP) is used subsequently for detection of reducing ends.
PB  - Faculty of Chemistry, Serbian Biochemical Society
C3  - Serbian Biochemical Society Seventh Conference "Biochemistry of Control in Life and Technology" - Proceedings
T1  - Directed evolution of cellulase from Trichoderma reesei for higher activity and development of microtiter plate assay based on cellobiose dehydrogenase
UR  - https://hdl.handle.net/21.15107/rcub_cer_3282
ER  - 

@conference{
author = "Zelenović, Jelena and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2017",
abstract = "Cellulase (EC 3.2.1.4) are important enzymes in food, paper, textile, detergent and biofuel industries. Most cellulases have low activity and stability. Improving these properties would have substantial impact on numerous industrial processes. Enzymatic properties can be improved by directed evolution, but the screening process is the limiting step. Coupled cellulase assay has been developed in order to improve the screening process. This method does not require boiling samples and allows rapid screening of mutants in a microtiter plate. The aim of this study was to establish enzyme coupled assay where cellulase first hydrolyzes carboxymethylcellulose (CMC), and cellobioses dehydrogenase (CBDH) and dichlorophenolindophenol (DCPIP) is used subsequently for detection of reducing ends.",
publisher = "Faculty of Chemistry, Serbian Biochemical Society",
journal = "Serbian Biochemical Society Seventh Conference "Biochemistry of Control in Life and Technology" - Proceedings",
title = "Directed evolution of cellulase from Trichoderma reesei for higher activity and development of microtiter plate assay based on cellobiose dehydrogenase",
url = "https://hdl.handle.net/21.15107/rcub_cer_3282"
}

Zelenović, J., Ostafe, R., Fischer, R.,& Prodanović, R.. (2017). Directed evolution of cellulase from Trichoderma reesei for higher activity and development of microtiter plate assay based on cellobiose dehydrogenase. in Serbian Biochemical Society Seventh Conference "Biochemistry of Control in Life and Technology" - Proceedings
Faculty of Chemistry, Serbian Biochemical Society..
https://hdl.handle.net/21.15107/rcub_cer_3282

Zelenović J, Ostafe R, Fischer R, Prodanović R. Directed evolution of cellulase from Trichoderma reesei for higher activity and development of microtiter plate assay based on cellobiose dehydrogenase. in Serbian Biochemical Society Seventh Conference "Biochemistry of Control in Life and Technology" - Proceedings. 2017;.
https://hdl.handle.net/21.15107/rcub_cer_3282 .

Zelenović, Jelena, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Directed evolution of cellulase from Trichoderma reesei for higher activity and development of microtiter plate assay based on cellobiose dehydrogenase" in Serbian Biochemical Society Seventh Conference "Biochemistry of Control in Life and Technology" - Proceedings (2017),
https://hdl.handle.net/21.15107/rcub_cer_3282 .