Cohnella 1759 cysteine protease shows significant long term half-life and impressive increased activity in presence of some chemical reagents

Abstract Thermostability and substrate specificity of proteases are major factors in their industrial applications. rEla is a novel recombinant cysteine protease obtained from a thermophilic bacterium, Cohnella sp.A01 (PTCC No: 1921). Herein, we were interested in recombinant production and characte...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Rayan Saghian, Elham Mokhtari, Saeed Aminzadeh
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/52e621d7b3ef4939a94075969f9577fe
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:52e621d7b3ef4939a94075969f9577fe
record_format	dspace
spelling	oai:doaj.org-article:52e621d7b3ef4939a94075969f9577fe2021-12-02T13:33:50ZCohnella 1759 cysteine protease shows significant long term half-life and impressive increased activity in presence of some chemical reagents10.1038/s41598-021-84267-w2045-2322https://doaj.org/article/52e621d7b3ef4939a94075969f9577fe2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-84267-whttps://doaj.org/toc/2045-2322Abstract Thermostability and substrate specificity of proteases are major factors in their industrial applications. rEla is a novel recombinant cysteine protease obtained from a thermophilic bacterium, Cohnella sp.A01 (PTCC No: 1921). Herein, we were interested in recombinant production and characterization of the enzyme and finding the novel features in comparison with other well-studied cysteine proteases. The bioinformatics analysis showed that rEla is allosteric cysteine protease from DJ-1/ThiJ/PfpI superfamily. The enzyme was heterologously expressed and characterized and the recombinant enzyme molecular mass was 19.38 kD which seems to be smaller than most of the cysteine proteases. rEla exhibited acceptable activity in broad pH and temperature ranges. The optimum activity was observed at 50℃ and pH 8 and the enzyme showed remarkable stability by keeping 50% of residual activity after 100 days storage at room temperature. The enzyme Km and Vmax values were 21.93 mM, 8 U/ml, respectively. To the best of our knowledge, in comparison with the other characterized cysteine proteases, rEla is the only reported cysteine protease with collagen specificity. The enzymes activity increases up to 1.4 times in the presence of calcium ion (2 mM) suggesting it as the enzyme’s co-factor. When exposed to surfactants including Tween20, Tween80, Triton X-100 and SDS (1% and 4% v/v) the enzyme activity surprisingly increased up to 5 times.Rayan SaghianElham MokhtariSaeed AminzadehNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-18 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Rayan Saghian Elham Mokhtari Saeed Aminzadeh Cohnella 1759 cysteine protease shows significant long term half-life and impressive increased activity in presence of some chemical reagents
description	Abstract Thermostability and substrate specificity of proteases are major factors in their industrial applications. rEla is a novel recombinant cysteine protease obtained from a thermophilic bacterium, Cohnella sp.A01 (PTCC No: 1921). Herein, we were interested in recombinant production and characterization of the enzyme and finding the novel features in comparison with other well-studied cysteine proteases. The bioinformatics analysis showed that rEla is allosteric cysteine protease from DJ-1/ThiJ/PfpI superfamily. The enzyme was heterologously expressed and characterized and the recombinant enzyme molecular mass was 19.38 kD which seems to be smaller than most of the cysteine proteases. rEla exhibited acceptable activity in broad pH and temperature ranges. The optimum activity was observed at 50℃ and pH 8 and the enzyme showed remarkable stability by keeping 50% of residual activity after 100 days storage at room temperature. The enzyme Km and Vmax values were 21.93 mM, 8 U/ml, respectively. To the best of our knowledge, in comparison with the other characterized cysteine proteases, rEla is the only reported cysteine protease with collagen specificity. The enzymes activity increases up to 1.4 times in the presence of calcium ion (2 mM) suggesting it as the enzyme’s co-factor. When exposed to surfactants including Tween20, Tween80, Triton X-100 and SDS (1% and 4% v/v) the enzyme activity surprisingly increased up to 5 times.
format	article
author	Rayan Saghian Elham Mokhtari Saeed Aminzadeh
author_facet	Rayan Saghian Elham Mokhtari Saeed Aminzadeh
author_sort	Rayan Saghian
title	Cohnella 1759 cysteine protease shows significant long term half-life and impressive increased activity in presence of some chemical reagents
title_short	Cohnella 1759 cysteine protease shows significant long term half-life and impressive increased activity in presence of some chemical reagents
title_full	Cohnella 1759 cysteine protease shows significant long term half-life and impressive increased activity in presence of some chemical reagents
title_fullStr	Cohnella 1759 cysteine protease shows significant long term half-life and impressive increased activity in presence of some chemical reagents
title_full_unstemmed	Cohnella 1759 cysteine protease shows significant long term half-life and impressive increased activity in presence of some chemical reagents
title_sort	cohnella 1759 cysteine protease shows significant long term half-life and impressive increased activity in presence of some chemical reagents
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/52e621d7b3ef4939a94075969f9577fe
work_keys_str_mv	AT rayansaghian cohnella1759cysteineproteaseshowssignificantlongtermhalflifeandimpressiveincreasedactivityinpresenceofsomechemicalreagents AT elhammokhtari cohnella1759cysteineproteaseshowssignificantlongtermhalflifeandimpressiveincreasedactivityinpresenceofsomechemicalreagents AT saeedaminzadeh cohnella1759cysteineproteaseshowssignificantlongtermhalflifeandimpressiveincreasedactivityinpresenceofsomechemicalreagents
_version_	1718392851802357760

Cohnella 1759 cysteine protease shows significant long term half-life and impressive increased activity in presence of some chemical reagents

Ejemplares similares