A coupled system involving arginase and urease for l-ornithine production

Huang, Kai; Zhang, Tao; Mu, Wanmeng; Miao, Ming

doi:10.1016/j.molcatb.2017.01.018

Cited by 6 publications

(2 citation statements)

References 26 publications

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“…Purified (His-tagged) Bacillus pycnus arginase at pH 6.5 had its highest activity with Ni 2+ , while Mn +2 permitted less than half the activity obtained with Ni 2+ . At pH 9.5, however, the enzyme had maximal activity with Mn 2+ and only a small fraction of this activity with Ni 2+ [53].…”

Section: Discussionmentioning

confidence: 89%

Genetic regulation, biochemical properties and physiological importance of arginase from Sinorhizobium meliloti

et al. 2020

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In bacteria, l-arginine is a precursor of various metabolites and can serve as a source of carbon and/or nitrogen. Arginine catabolism by arginase, which hydrolyzes arginine to l-ornithine and urea, is common in nature but has not been studied in symbiotic nitrogen-fixing rhizobia. The genome of the alfalfa microsymbiont Sinorhizobium meliloti 1021 has two genes annotated as arginases, argI1 (smc03091) and argI2 (sma1711). Biochemical assays with purified ArgI1 and ArgI2 (as 6His-Sumo-tagged proteins) showed that only ArgI1 had detectable arginase activity. A 1021 argI1 null mutant lacked arginase activity and grew at a drastically reduced rate with arginine as sole nitrogen source. Wild-type growth and arginase activity were restored in the argI1 mutant genetically complemented with a genomically integrated argI1 gene. In the wild-type, arginase activity and argI1 transcription were induced several fold by exogenous arginine. ArgI1 purified as a 6His-Sumo-tagged protein had its highest in vitro enzymatic activity at pH 7.5 with Ni2+ as cofactor. The enzyme was also active with Mn2+ and Co2+, both of which gave the enzyme the highest activities at a more alkaline pH. The 6His-Sumo-ArgI1 comprised three identical subunits based on the migration of the urea-dissociated protein in a native polyacrylamide gel. A Lrp-like regulator (smc03092) divergently transcribed from argI1 was required for arginase induction by arginine or ornithine. This regulator was designated ArgIR. Electrophoretic mobility shift assays showed that purified ArgIR bound to the argI1 promoter in a region preceding the predicted argI1 transcriptional start. Our results indicate that ArgI1 is the sole arginase in S. meliloti , that it contributes substantially to arginine catabolism in vivo and that argI1 induction by arginine is dependent on ArgIR.

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Section: Discussionmentioning

confidence: 89%

Genetic regulation, biochemical properties and physiological importance of arginase from Sinorhizobium meliloti

et al. 2020

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“…Arginase (EC 3.5.3.1; L-arginine amidinohydrolase) is found in all five organism kingdoms, from unicellular prokaryotes to multicellular eukaryotes, and it is an enzyme-dependent on divalent manganese metal as a cofactor [ 7 , 8 ]. It catalyzes the hydrolysis of L-arginine irreversibly to urea and L-ornithine in the last step of the urea cycle [ 9 ].…”

Section: Introductionmentioning

confidence: 99%

Fabrication of electrospun cellulose-derived nanofiber membranes with enhanced stability properties of arginase

IŞIK¹,

TEKE²

2022

Turkish Journal of Chemistry

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In this study, cellulose acetate (CA)/polyvinylpyrrolidone (PVP) and CA/PVP/Mn 2+ nanofibers were produced by the electrospinning method, and these cellulose-derived membranes were used as carriers for arginase immobilization for the first time. The structural and morphological analysis of these cellulose-derived nanofibers were determined by attenuated total reflection-Fourier to transform infrared spectroscopy (FTIR), thermogravimetric analysis (TGA), X-ray diffraction (XRD), and scanning electron microscopy (SEM). After the immobilization process, it was observed that the thermal properties of the cellulose-derived nanofibers especially improved. The optimum temperature value for free arginase was found to be 35 °C, and this value was found to be 40 °C for arginase immobilized cellulose-derived nanofibers. When the free arginase retained only about 35% of its activity at 50 °C and 60 °C after 60 min, arginase immobilized nanofibers protected 65% of their activity under the same conditions. In addition, arginase immobilized CA/PVP and CA/PVP/Mn 2+ nanofibers managed to retain 50% of their activity even after 9 and 12 reuses, respectively.

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Thermostable arginase from Sulfobacillus acidophilus with neutral pH optimum applied for high-efficiency l-ornithine production

Huang

Zhang

Guan

et al. 2020

Appl Microbiol Biotechnol

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A coupled system involving arginase and urease for l-ornithine production

Cited by 6 publications

References 26 publications

Genetic regulation, biochemical properties and physiological importance of arginase from Sinorhizobium meliloti

Genetic regulation, biochemical properties and physiological importance of arginase from Sinorhizobium meliloti

Fabrication of electrospun cellulose-derived nanofiber membranes with enhanced stability properties of arginase

Thermostable arginase from Sulfobacillus acidophilus with neutral pH optimum applied for high-efficiency l-ornithine production

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