English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Background  The concentration of urinary oxalate is more influential to the formation of calcium oxalate urolithiasis than is urinary calcium concentration.  YvrK  gene encodes a 43 KD-sized oxalate decarboxylase. We previously developed the recombinant  Escherichia coli (E. coli ) expressing  Yvrk  gene from  Bacillus subtilis  and named it as  pBy . The aim of this study was to purify the recombinant oxalate decarboxylase overexpressed in  E. coli  and evaluate the oxalate-degrading activity of the purified enzyme.    Results  The oxalate-degrading activity of  pBy  was highest when cultured at pH 5. The activity of purified oxalate decarboxylase was determined after incubation with sodium oxalate and the optimal pH and temperature of oxalate decarboxylase were determined. Purified oxalate decarboxylase degraded more than 50% of oxalate when incubated with MnCl 2  and sodium oxalate in atmospheric O 2 . The optimal pH of recombinant oxalate decarboxylase was 5 and the optimal temperature was 28°C. Eight-week-old Sprague–Dawley male rats were used as a transient hyperoxaluric rat model. Suprapubic catheter was inserted into the bladder of each rat and urine was collected hourly before and 3 hours after oral oxalate intake in the absence and presence of homogenates of  pBy  and non-recombinant  E. coli  as the control. After the oral intake of sodium oxalate, the concentration of oxalate in urine increased exponentially for 3 hours. The oxalate concentration in urine was decreased significantly by  pBy  homogenates compared to control.    Conclusions  We constructed the recombinant  E. coli  expressing  YvrK  gene and purified the recombinant oxalate decarboxylase successfully. Purified recombinant oxalate decarboxylase, as well as recombinant  E. coli  named  pBy , showed the oxalate-degrading activity in  in vitro  and  in vivo  model.

Expression of the gene encoding oxalate decarboxylase from Bacillus subtilis and characterization of the recombinant enzyme