ELISA-based competitive trypsin inhibition assay

Proteolytic enzymes are crucial for numerous biological processes and are tightly controlled by specific inhibitors. In addition to the research activities to investigate the natural effects of these inhibitors, it is important to determine the inhibition capabilities of inhibitors due to their impo...

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Autores principales:	Bengü Ergenoğlu, Özlem Ertekin, Şerife Şeyda Pirinçci Göktürk, Göknur Gizem Dinç, Esin Akçael, Melahat Bağirova, Fatıma Yücel
Formato:	article
Lenguaje:	EN
Publicado:	Taylor & Francis Group 2021
Materias:	trypsin inhibition ic50 inhibition efficiency elisa Biotechnology TP248.13-248.65
Acceso en línea:	https://doaj.org/article/474c2071fa1f4d9caf3f323e4a181613
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spelling	oai:doaj.org-article:474c2071fa1f4d9caf3f323e4a1816132021-11-17T14:21:55ZELISA-based competitive trypsin inhibition assay1310-28181314-353010.1080/13102818.2021.1977697https://doaj.org/article/474c2071fa1f4d9caf3f323e4a1816132021-01-01T00:00:00Zhttp://dx.doi.org/10.1080/13102818.2021.1977697https://doaj.org/toc/1310-2818https://doaj.org/toc/1314-3530Proteolytic enzymes are crucial for numerous biological processes and are tightly controlled by specific inhibitors. In addition to the research activities to investigate the natural effects of these inhibitors, it is important to determine the inhibition capabilities of inhibitors due to their importance in different fields, including food and health industry. In this study, we describe a high-throughput adaptable screening method to detect inhibitors and compare their inhibition efficiency at nanogram levels, using a Competitive enzyme-linked immunosorbent assay (ELISA) based Trypsin Inhibition Assay (E-CTIA). We worked with four different inhibitors from different sources and action mechanisms, all of which were competitive inhibitors. The half-maximal inhibitory concentration (IC50) strongly correlated with the experimental inhibition capacities introduced in the user manuals. E-CTIA successfully fulfills the requirements of an assay, such as reproducibility, low cost, low sample requirement and ease of use. It also enables to test multiple samples simultaneously in a short time, and it has the potential to be adapted to bigger plate formats such as 384 well or even bigger. Besides being the first successful example of Competitive ELISA Based Inhibition Assay, it has the potential to be used for many competitive inhibitors.Bengü ErgenoğluÖzlem ErtekinŞerife Şeyda Pirinçci GöktürkGöknur Gizem DinçEsin AkçaelMelahat BağirovaFatıma YücelTaylor & Francis Grouparticletrypsin inhibitionic50 inhibition efficiencyelisaBiotechnologyTP248.13-248.65ENBiotechnology & Biotechnological Equipment, Vol 35, Iss 1, Pp 1385-1392 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	trypsin inhibition ic50 inhibition efficiency elisa Biotechnology TP248.13-248.65
spellingShingle	trypsin inhibition ic50 inhibition efficiency elisa Biotechnology TP248.13-248.65 Bengü Ergenoğlu Özlem Ertekin Şerife Şeyda Pirinçci Göktürk Göknur Gizem Dinç Esin Akçael Melahat Bağirova Fatıma Yücel ELISA-based competitive trypsin inhibition assay
description	Proteolytic enzymes are crucial for numerous biological processes and are tightly controlled by specific inhibitors. In addition to the research activities to investigate the natural effects of these inhibitors, it is important to determine the inhibition capabilities of inhibitors due to their importance in different fields, including food and health industry. In this study, we describe a high-throughput adaptable screening method to detect inhibitors and compare their inhibition efficiency at nanogram levels, using a Competitive enzyme-linked immunosorbent assay (ELISA) based Trypsin Inhibition Assay (E-CTIA). We worked with four different inhibitors from different sources and action mechanisms, all of which were competitive inhibitors. The half-maximal inhibitory concentration (IC50) strongly correlated with the experimental inhibition capacities introduced in the user manuals. E-CTIA successfully fulfills the requirements of an assay, such as reproducibility, low cost, low sample requirement and ease of use. It also enables to test multiple samples simultaneously in a short time, and it has the potential to be adapted to bigger plate formats such as 384 well or even bigger. Besides being the first successful example of Competitive ELISA Based Inhibition Assay, it has the potential to be used for many competitive inhibitors.
format	article
author	Bengü Ergenoğlu Özlem Ertekin Şerife Şeyda Pirinçci Göktürk Göknur Gizem Dinç Esin Akçael Melahat Bağirova Fatıma Yücel
author_facet	Bengü Ergenoğlu Özlem Ertekin Şerife Şeyda Pirinçci Göktürk Göknur Gizem Dinç Esin Akçael Melahat Bağirova Fatıma Yücel
author_sort	Bengü Ergenoğlu
title	ELISA-based competitive trypsin inhibition assay
title_short	ELISA-based competitive trypsin inhibition assay
title_full	ELISA-based competitive trypsin inhibition assay
title_fullStr	ELISA-based competitive trypsin inhibition assay
title_full_unstemmed	ELISA-based competitive trypsin inhibition assay
title_sort	elisa-based competitive trypsin inhibition assay
publisher	Taylor & Francis Group
publishDate	2021
url	https://doaj.org/article/474c2071fa1f4d9caf3f323e4a181613
work_keys_str_mv	AT benguergenoglu elisabasedcompetitivetrypsininhibitionassay AT ozlemertekin elisabasedcompetitivetrypsininhibitionassay AT serifeseydapirinccigokturk elisabasedcompetitivetrypsininhibitionassay AT goknurgizemdinc elisabasedcompetitivetrypsininhibitionassay AT esinakcael elisabasedcompetitivetrypsininhibitionassay AT melahatbagirova elisabasedcompetitivetrypsininhibitionassay AT fatımayucel elisabasedcompetitivetrypsininhibitionassay
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ELISA-based competitive trypsin inhibition assay

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