A Novel L-Asparaginase from Enterobacter sp. Strain M55 from Maras Salterns in Peru

A. Hurtado; J. C. Flores-Santos; C. N. Flores-Fernández; S. Saavedra; J. H.P.M. Santos; A. Pessoa-Júnior; M. E. Lienqueo; M. J. Bayro; A. I. Zavaleta

doi:10.15255/CABEQ.2022.2064

A Novel L-Asparaginase from Enterobacter sp. Strain M55 from Maras Salterns in Peru

A. Hurtado, J. C. Flores-Santos, C. N. Flores-Fernández, S. Saavedra, J. H.P.M. Santos, A. Pessoa-Júnior, M. E. Lienqueo, M. J. Bayro, A. I. Zavaleta

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Resumen

L-Asparaginase (ASNase) is used in medicine for neoplasms treatment and in food industry for mitigation of acrylamide in high-temperature processed food. In medicine, commercial ASNases have exhibited side effects and l-glutaminase (GLNase) activity affecting the clinical treatment. The aim of this work was to study a novel ASNase from Enterobacter sp. M55 isolated from Maras Salters in Peru, which was purified and biochemically characterised. This ASNase exhibited a Km of 5.71 mM and a Vmax of 0.16 µmol mL^–1 min^–1, as well as an optimum temperature and pH of 37 °C and 6, respectively. Moreover, a good activity (80 %) was observed at physiological pH. Likewise, the enzyme increased its activity by around 50% in presence of urea, glutathione, and glucose. Whilst in presence of serum compounds, it kept more that 60 % of activity. In addition, this ASNase showed low GLNase activity.

Idioma original	Inglés
Páginas (desde-hasta)	167-173
Número de páginas	7
Publicación	Chemical and Biochemical Engineering Quarterly
Volumen	36
N.º	2
DOI	https://doi.org/10.15255/CABEQ.2022.2064
Estado	Publicada - 2022

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© 2022 Assoc. of Chemists and Chemical Engineers of Croatia. All rights reserved.

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title = "A Novel L-Asparaginase from Enterobacter sp. Strain M55 from Maras Salterns in Peru",

abstract = "L-Asparaginase (ASNase) is used in medicine for neoplasms treatment and in food industry for mitigation of acrylamide in high-temperature processed food. In medicine, commercial ASNases have exhibited side effects and l-glutaminase (GLNase) activity affecting the clinical treatment. The aim of this work was to study a novel ASNase from Enterobacter sp. M55 isolated from Maras Salters in Peru, which was purified and biochemically characterised. This ASNase exhibited a Km of 5.71 mM and a Vmax of 0.16 µmol mL–1 min–1, as well as an optimum temperature and pH of 37 °C and 6, respectively. Moreover, a good activity (80 %) was observed at physiological pH. Likewise, the enzyme increased its activity by around 50% in presence of urea, glutathione, and glucose. Whilst in presence of serum compounds, it kept more that 60 % of activity. In addition, this ASNase showed low GLNase activity.",

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T1 - A Novel L-Asparaginase from Enterobacter sp. Strain M55 from Maras Salterns in Peru

AU - Hurtado, A.

AU - Flores-Santos, J. C.

AU - Flores-Fernández, C. N.

AU - Saavedra, S.

AU - Santos, J. H.P.M.

AU - Pessoa-Júnior, A.

AU - Lienqueo, M. E.

AU - Bayro, M. J.

AU - Zavaleta, A. I.

PY - 2022

Y1 - 2022

N2 - L-Asparaginase (ASNase) is used in medicine for neoplasms treatment and in food industry for mitigation of acrylamide in high-temperature processed food. In medicine, commercial ASNases have exhibited side effects and l-glutaminase (GLNase) activity affecting the clinical treatment. The aim of this work was to study a novel ASNase from Enterobacter sp. M55 isolated from Maras Salters in Peru, which was purified and biochemically characterised. This ASNase exhibited a Km of 5.71 mM and a Vmax of 0.16 µmol mL–1 min–1, as well as an optimum temperature and pH of 37 °C and 6, respectively. Moreover, a good activity (80 %) was observed at physiological pH. Likewise, the enzyme increased its activity by around 50% in presence of urea, glutathione, and glucose. Whilst in presence of serum compounds, it kept more that 60 % of activity. In addition, this ASNase showed low GLNase activity.

AB - L-Asparaginase (ASNase) is used in medicine for neoplasms treatment and in food industry for mitigation of acrylamide in high-temperature processed food. In medicine, commercial ASNases have exhibited side effects and l-glutaminase (GLNase) activity affecting the clinical treatment. The aim of this work was to study a novel ASNase from Enterobacter sp. M55 isolated from Maras Salters in Peru, which was purified and biochemically characterised. This ASNase exhibited a Km of 5.71 mM and a Vmax of 0.16 µmol mL–1 min–1, as well as an optimum temperature and pH of 37 °C and 6, respectively. Moreover, a good activity (80 %) was observed at physiological pH. Likewise, the enzyme increased its activity by around 50% in presence of urea, glutathione, and glucose. Whilst in presence of serum compounds, it kept more that 60 % of activity. In addition, this ASNase showed low GLNase activity.

KW - Enterobacter

KW - clinical treatment

KW - l-asparaginase

KW - l-glutaminase

KW - saline environments

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DO - 10.15255/CABEQ.2022.2064

M3 - Artículo

AN - SCOPUS:85135838130

SN - 0352-9568

VL - 36

SP - 167

EP - 173

JO - Chemical and Biochemical Engineering Quarterly

JF - Chemical and Biochemical Engineering Quarterly

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A Novel L-Asparaginase from Enterobacter sp. Strain M55 from Maras Salterns in Peru

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