Characterization of a thermostable arginase from Rummeliibacillus pycnus SK31.001

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

doi:10.1016/j.molcatb.2016.11.020

Cited by 15 publications

(6 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several studies have shown that metal ions might be essential for the activation or improvement of enzyme activity . Hence, the effect of metal ions on ZENG catalytic activity was investigated (Table ).…”

Section: Resultsmentioning

confidence: 72%

“…Several studies have shown that metal ions might be essential for the activation or improvement of enzyme activity. 28 Hence, the effect of metal ions on ZENG catalytic activity was investigated (Table 2). In contrast with the group without the addition of metal ions, the enzyme group with the addition of 1 mmol/L of Ca 2+ and Co 2+ had no obvious effect on ZENG activity and the addition of the same concentrations of Mn 2+ , Mg 2+ , Ni 2+ , and EDTA slightly restrained the catalytic activity.…”

Section: Effects Of Ph On Recombinant Zeng Activity Andmentioning

confidence: 99%

See 1 more Smart Citation

Identification of a Potent Enzyme for the Detoxification of Zearalenone

Zhang

et al. 2019

J. Agric. Food Chem.

Self Cite

View full text Add to dashboard Cite

The occurrence of mycotoxin zearalenone (ZEN) and its derivatives has been a severe global threat to food and animals. In addition to the chemical and physical degradation methods, a powerful biocatalyst is urgently required for the detoxification of ZEN. Here, an efficient ZEN-degrading lactonase from Gliocladium roseum, named ZENG, was identified for the first time. The recombinant ZENG exhibited the highest activity at pH 7.0 and 38 °C. In addition, the recombinant enzyme showed a high degrading performance toward ZEN and its toxic derivatives α-zearalenol (α-ZOL) and α-zearalanol (α-ZAL), with the specific activities as 315, 187, and 117 units/mg, respectively. To meet the industrial demands, attempts were also made to enhance the thermostability of ZENG using a structure-based modification. Three double-site mutants, including H134L/S136L, H134F/S136F, and H134I/S134I, in the position between the cap and core catalytic domain of ZENG were designed. Finally, the thermostability of both H134L/S136L and H134F/S136F displayed a significant improvement compared to the wild-type enzyme.

show abstract

Section: Resultsmentioning

confidence: 72%

Section: Effects Of Ph On Recombinant Zeng Activity Andmentioning

confidence: 99%

Identification of a Potent Enzyme for the Detoxification of Zearalenone

Zhang

et al. 2019

J. Agric. Food Chem.

Self Cite

View full text Add to dashboard Cite

show abstract

“…Some species of Lysinibacillus are positive for catalase and have broad spectrum antimicrobial activity [63]. Rummeliibacillu spycnus was recently shown to produce an arginine metabolic enzyme with high activity [64] and was speculated to promote better arginine absorption by tilapia on a woody diet in this study. Interestingly, Microbacterium foliorum, which produces a cold-active α-amylase [65], was observed in the guts of tilapia fed fermented MOL leaf meal ( Table 3).…”

Section: Plos Onementioning

confidence: 76%

Effects of woody forages on biodiversity and bioactivity of aerobic culturable gut bacteria of tilapia (Oreochromis niloticus)

Chen

Liu

et al. 2020

PLoS ONE

View full text Add to dashboard Cite

The present study investigated the effects of four woody forages (Moringa oleifera Lam (MOL), fermented MOL, Folium mori (FM) and fermented FM) on biodiversity and bioactivity of aerobic culturable gut bacteria of tilapia (Oreochromis niloticus) by a traditional culturedependent method. A total of 133 aerobic culturable isolates were recovered and identified from the gut of tilapia, belonging to 35 species of 12 genera in three bacterial phyla (Firmicutes, Actinobacteria and Proteobacteria). Among them, 6 bacterial isolates of Bacillus baekryungensis, Bacillus marisflavi, Bacillus pumilus, Bacillus methylotrophicus, Proteus mirabilis and Pseudomonas taiwanensis were isolated from all the five experimental groups. The Bray-Curtis analysis showed that the bacterial communities among the five groups displayed obvious differences. In addition, this result of bioactivity showed that approximate 43% of the aerobic culturable gut bacteria of tilapia displayed a distinct anti-bacterial activity against at least one of four fish pathogens Streptococcus agalactiae, Streptococcus iniae, Micrococcus luteus and Vibrio parahemolyticus. Furthermore, Bacillus amyloliquefaciens and Streptomyces rutgersensis displayed strong activity against all four indicator bacteria. These results contribute to our understanding of the intestinal bacterial diversity of tilapia when fed with woody forages and how certain antimicrobial bacteria flourished under such diets. This can aid in the further exploitation of new diets and probiotic sources in aquaculture.

show abstract

“…With Mn 2 it was most active over a broad pH range of 8.5-10.5 and with Co 2+ its highest activity centered at pH 9.0. pH-dependent changes in catalytic activity with different cofactors have been reported in other arginases. The arginase from Rummeliibacillus pycnus, for example, has its highest activity at pH 6.5 in the presence of Ni 2+ and at pH 9.5 in the presence of Mn 2+ [51]. The pH-activity profiles of the H. pylori arginase differed markedly with Co 2+ and Mn 2+ , possibly due to the effect of their different acid equilibrium constants on active site tertiary structure [52].…”

Section: Discussionmentioning

confidence: 99%

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

et al. 2020

View full text Add to dashboard Cite

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.

show abstract

Characterization of a thermostable arginase from Rummeliibacillus pycnus SK31.001

Cited by 15 publications

References 26 publications

Identification of a Potent Enzyme for the Detoxification of Zearalenone

Identification of a Potent Enzyme for the Detoxification of Zearalenone

Effects of woody forages on biodiversity and bioactivity of aerobic culturable gut bacteria of tilapia (Oreochromis niloticus)

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

Contact Info

Product

Resources

About