Characterization of a Novel L-Asparaginase from <i>Mycobacterium gordonae</i> with Acrylamide Mitigation Potential

L-asparaginase (E.C.3.5.1.1) is a well-known agent that prevents the formation of acrylamide both in the food industry and against childhood acute lymphoblastic leukemia in clinical settings. The disadvantages of L-asparaginase, which restrict its industrial application, include its narrow range of...

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Autores principales:	Huibing Chi, Meirong Chen, Linshu Jiao, Zhaoxin Lu, Xiaomei Bie, Haizhen Zhao, Fengxia Lu
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	L-asparaginase acrylamide <i>Mycobacterium gordonae</i> thermal stability Chemical technology TP1-1185
Acceso en línea:	https://doaj.org/article/2e32c2af18aa4b5387a9d4a1c26bb2d6
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spelling	oai:doaj.org-article:2e32c2af18aa4b5387a9d4a1c26bb2d62021-11-25T17:35:59ZCharacterization of a Novel L-Asparaginase from <i>Mycobacterium gordonae</i> with Acrylamide Mitigation Potential10.3390/foods101128192304-8158https://doaj.org/article/2e32c2af18aa4b5387a9d4a1c26bb2d62021-11-01T00:00:00Zhttps://www.mdpi.com/2304-8158/10/11/2819https://doaj.org/toc/2304-8158L-asparaginase (E.C.3.5.1.1) is a well-known agent that prevents the formation of acrylamide both in the food industry and against childhood acute lymphoblastic leukemia in clinical settings. The disadvantages of L-asparaginase, which restrict its industrial application, include its narrow range of pH stability and low thermostability. In this study, a novel L-asparaginase from <i>Mycobacterium gordonae</i> (GmASNase) was cloned and expressed in <i>Escherichia coli</i> BL21 (DE3). GmASNase was found to be a tetramer with a monomeric size of 32 kDa, sharing only 32% structural identity with <i>Helicobacter pylori</i> L-asparaginases in the Protein Data Bank database. The purified GmASNase had the highest specific activity of 486.65 IU mg<sup>−1</sup> at pH 9.0 and 50 °C. In addition, GmASNase possessed superior properties in terms of stability at a wide pH range of 5.0–11.0 and activity at temperatures below 40 °C. Moreover, GmASNase displayed high substrate specificity towards L-asparagine with Km, kcat, and kcat/Km values of 6.025 mM, 11,864.71 min<sup>−1</sup> and 1969.25 mM<sup>−1</sup>min<sup>−1</sup>, respectively. To evaluate its ability to mitigate acrylamide, GmASNase was used to treat potato chips prior to frying, where the acrylamide content decreased by 65.09% compared with the untreated control. These results suggest that GmASNase is a potential candidate for applications in the food industry.Huibing ChiMeirong ChenLinshu JiaoZhaoxin LuXiaomei BieHaizhen ZhaoFengxia LuMDPI AGarticleL-asparaginaseacrylamide<i>Mycobacterium gordonae</i>thermal stabilityChemical technologyTP1-1185ENFoods, Vol 10, Iss 2819, p 2819 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	L-asparaginase acrylamide <i>Mycobacterium gordonae</i> thermal stability Chemical technology TP1-1185
spellingShingle	L-asparaginase acrylamide <i>Mycobacterium gordonae</i> thermal stability Chemical technology TP1-1185 Huibing Chi Meirong Chen Linshu Jiao Zhaoxin Lu Xiaomei Bie Haizhen Zhao Fengxia Lu Characterization of a Novel L-Asparaginase from <i>Mycobacterium gordonae</i> with Acrylamide Mitigation Potential
description	L-asparaginase (E.C.3.5.1.1) is a well-known agent that prevents the formation of acrylamide both in the food industry and against childhood acute lymphoblastic leukemia in clinical settings. The disadvantages of L-asparaginase, which restrict its industrial application, include its narrow range of pH stability and low thermostability. In this study, a novel L-asparaginase from <i>Mycobacterium gordonae</i> (GmASNase) was cloned and expressed in <i>Escherichia coli</i> BL21 (DE3). GmASNase was found to be a tetramer with a monomeric size of 32 kDa, sharing only 32% structural identity with <i>Helicobacter pylori</i> L-asparaginases in the Protein Data Bank database. The purified GmASNase had the highest specific activity of 486.65 IU mg<sup>−1</sup> at pH 9.0 and 50 °C. In addition, GmASNase possessed superior properties in terms of stability at a wide pH range of 5.0–11.0 and activity at temperatures below 40 °C. Moreover, GmASNase displayed high substrate specificity towards L-asparagine with Km, kcat, and kcat/Km values of 6.025 mM, 11,864.71 min<sup>−1</sup> and 1969.25 mM<sup>−1</sup>min<sup>−1</sup>, respectively. To evaluate its ability to mitigate acrylamide, GmASNase was used to treat potato chips prior to frying, where the acrylamide content decreased by 65.09% compared with the untreated control. These results suggest that GmASNase is a potential candidate for applications in the food industry.
format	article
author	Huibing Chi Meirong Chen Linshu Jiao Zhaoxin Lu Xiaomei Bie Haizhen Zhao Fengxia Lu
author_facet	Huibing Chi Meirong Chen Linshu Jiao Zhaoxin Lu Xiaomei Bie Haizhen Zhao Fengxia Lu
author_sort	Huibing Chi
title	Characterization of a Novel L-Asparaginase from <i>Mycobacterium gordonae</i> with Acrylamide Mitigation Potential
title_short	Characterization of a Novel L-Asparaginase from <i>Mycobacterium gordonae</i> with Acrylamide Mitigation Potential
title_full	Characterization of a Novel L-Asparaginase from <i>Mycobacterium gordonae</i> with Acrylamide Mitigation Potential
title_fullStr	Characterization of a Novel L-Asparaginase from <i>Mycobacterium gordonae</i> with Acrylamide Mitigation Potential
title_full_unstemmed	Characterization of a Novel L-Asparaginase from <i>Mycobacterium gordonae</i> with Acrylamide Mitigation Potential
title_sort	characterization of a novel l-asparaginase from <i>mycobacterium gordonae</i> with acrylamide mitigation potential
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/2e32c2af18aa4b5387a9d4a1c26bb2d6
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Characterization of a Novel L-Asparaginase from <i>Mycobacterium gordonae</i> with Acrylamide Mitigation Potential

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