Characterization of a New L-Glutaminase Produced by <i>Achromobacter xylosoxidans</i> RSHG1, Isolated from an Expired Hydrolyzed L-Glutamine Sample

As significant biocatalyst, L-glutaminases find potential applications in various fields, from nourishment to the pharmaceutical industry. Anticancer activity and flavor enhancement are the most promising applications of L-glutaminases. In this study, L-glutaminase was isolated and purified from an...

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Autores principales:	Rabia Saleem, Safia Ahmed
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	L-glutaminase production optimization characterization molecular identification <i>Achromobacter xylosoxidans</i> RSHG1 Chemical technology TP1-1185 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/35e0479446cc48e59f3978f8edcf3524
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spelling	oai:doaj.org-article:35e0479446cc48e59f3978f8edcf35242021-11-25T17:05:04ZCharacterization of a New L-Glutaminase Produced by <i>Achromobacter xylosoxidans</i> RSHG1, Isolated from an Expired Hydrolyzed L-Glutamine Sample10.3390/catal111112622073-4344https://doaj.org/article/35e0479446cc48e59f3978f8edcf35242021-10-01T00:00:00Zhttps://www.mdpi.com/2073-4344/11/11/1262https://doaj.org/toc/2073-4344As significant biocatalyst, L-glutaminases find potential applications in various fields, from nourishment to the pharmaceutical industry. Anticancer activity and flavor enhancement are the most promising applications of L-glutaminases. In this study, L-glutaminase was isolated and purified from an old glutamine sample. A selected bacterial isolate was characterized taxonomically by morphological characters, biochemical testing and 16S rDNA sequence homology testing. The taxonomical characterization of the isolate identified it as <i>Achromobacter xylosoxidans</i> strain RSHG1. The isolate showed maximum enzyme production at 30 °C, pH 9, with Sorbitol as a carbon source and L-Glutamine as a nitrogen and inducer source. L-Glutaminsae was purified by using column chromatography on a Sephadex G-75. The enzyme has a molecular weight of 40 KDa, pH optimal 7 and is stable in the pH range of 6–8. The optimum temperature for the catalyst was 40 °C and stable at 35–50 °C. The kinetic studies of the purified L-glutaminase exhibited Km and Vmax of 0.236 mM and 443.8 U/mg, respectively. L-Glutaminase activity was increased when incubated with 20 mM CaCl<sub>2</sub>, BaCl<sub>2</sub>, ZnSO<sub>4</sub>, KCl, MgSO<sub>4</sub> and NaCl, whereas EDTA, CoCl<sub>2</sub>, HgCl, ZnSO<sub>4</sub> and FeSO<sub>4</sub> decreased the activity of the enzyme. The addition of 8% NaCl enhanced the glutaminase activity. L-Glutaminase immobilized on 3.6% agar was stable for up to 3 weeks.Rabia SaleemSafia AhmedMDPI AGarticleL-glutaminase productionoptimizationcharacterizationmolecular identification<i>Achromobacter xylosoxidans</i> RSHG1Chemical technologyTP1-1185ChemistryQD1-999ENCatalysts, Vol 11, Iss 1262, p 1262 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	L-glutaminase production optimization characterization molecular identification <i>Achromobacter xylosoxidans</i> RSHG1 Chemical technology TP1-1185 Chemistry QD1-999
spellingShingle	L-glutaminase production optimization characterization molecular identification <i>Achromobacter xylosoxidans</i> RSHG1 Chemical technology TP1-1185 Chemistry QD1-999 Rabia Saleem Safia Ahmed Characterization of a New L-Glutaminase Produced by <i>Achromobacter xylosoxidans</i> RSHG1, Isolated from an Expired Hydrolyzed L-Glutamine Sample
description	As significant biocatalyst, L-glutaminases find potential applications in various fields, from nourishment to the pharmaceutical industry. Anticancer activity and flavor enhancement are the most promising applications of L-glutaminases. In this study, L-glutaminase was isolated and purified from an old glutamine sample. A selected bacterial isolate was characterized taxonomically by morphological characters, biochemical testing and 16S rDNA sequence homology testing. The taxonomical characterization of the isolate identified it as <i>Achromobacter xylosoxidans</i> strain RSHG1. The isolate showed maximum enzyme production at 30 °C, pH 9, with Sorbitol as a carbon source and L-Glutamine as a nitrogen and inducer source. L-Glutaminsae was purified by using column chromatography on a Sephadex G-75. The enzyme has a molecular weight of 40 KDa, pH optimal 7 and is stable in the pH range of 6–8. The optimum temperature for the catalyst was 40 °C and stable at 35–50 °C. The kinetic studies of the purified L-glutaminase exhibited Km and Vmax of 0.236 mM and 443.8 U/mg, respectively. L-Glutaminase activity was increased when incubated with 20 mM CaCl<sub>2</sub>, BaCl<sub>2</sub>, ZnSO<sub>4</sub>, KCl, MgSO<sub>4</sub> and NaCl, whereas EDTA, CoCl<sub>2</sub>, HgCl, ZnSO<sub>4</sub> and FeSO<sub>4</sub> decreased the activity of the enzyme. The addition of 8% NaCl enhanced the glutaminase activity. L-Glutaminase immobilized on 3.6% agar was stable for up to 3 weeks.
format	article
author	Rabia Saleem Safia Ahmed
author_facet	Rabia Saleem Safia Ahmed
author_sort	Rabia Saleem
title	Characterization of a New L-Glutaminase Produced by <i>Achromobacter xylosoxidans</i> RSHG1, Isolated from an Expired Hydrolyzed L-Glutamine Sample
title_short	Characterization of a New L-Glutaminase Produced by <i>Achromobacter xylosoxidans</i> RSHG1, Isolated from an Expired Hydrolyzed L-Glutamine Sample
title_full	Characterization of a New L-Glutaminase Produced by <i>Achromobacter xylosoxidans</i> RSHG1, Isolated from an Expired Hydrolyzed L-Glutamine Sample
title_fullStr	Characterization of a New L-Glutaminase Produced by <i>Achromobacter xylosoxidans</i> RSHG1, Isolated from an Expired Hydrolyzed L-Glutamine Sample
title_full_unstemmed	Characterization of a New L-Glutaminase Produced by <i>Achromobacter xylosoxidans</i> RSHG1, Isolated from an Expired Hydrolyzed L-Glutamine Sample
title_sort	characterization of a new l-glutaminase produced by <i>achromobacter xylosoxidans</i> rshg1, isolated from an expired hydrolyzed l-glutamine sample
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/35e0479446cc48e59f3978f8edcf3524
work_keys_str_mv	AT rabiasaleem characterizationofanewlglutaminaseproducedbyiachromobacterxylosoxidansirshg1isolatedfromanexpiredhydrolyzedlglutaminesample AT safiaahmed characterizationofanewlglutaminaseproducedbyiachromobacterxylosoxidansirshg1isolatedfromanexpiredhydrolyzedlglutaminesample
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Characterization of a New L-Glutaminase Produced by <i>Achromobacter xylosoxidans</i> RSHG1, Isolated from an Expired Hydrolyzed L-Glutamine Sample

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