Original scientific paper
https://doi.org/10.15255/CABEQ.2022.2064
A Novel L-Asparaginase from Enterobacter sp. Strain M55 from Maras Salterns in Peru
A. Hurtado
; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima-Peru
J. C. Flores-Santos
; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima-Peru
C. N. Flores-Fernández
orcid.org/0000-0002-6250-201X
; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima-Peru
S. Saavedra
; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima-Peru
J. H. P. M. Santos
; Department of Biochemical and Pharmaceutical Technology, School of Pharmaceutical Sciences, University of São Paulo, São Paulo-Brazil
A. Pessoa-Júnior
; Department of Biochemical and Pharmaceutical Technology, School of Pharmaceutical Sciences, University of São Paulo, São Paulo-Brazil
M. E. Lienqueo
; Centre for Biotechnology and Bioengineering, Universidad de Chile, Santiago-Chile
M. J. Bayro
; Faculty of Natural Sciences, Universidad de Puerto Rico, Puerto Rico
A. I. Zavaleta
; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima-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.
This work is licensed under a Creative Commons Attribution 4.0 International License.
Keywords
l-asparaginase; l-glutaminase; Enterobacter; saline environments; clinical treatment
Hrčak ID:
280943
URI
Publication date:
26.7.2022.
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