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Articles by M.R. Soudi
Total Records ( 3 ) for M.R. Soudi
  S. Ashraf , M.R. Soudi and M. Sadeghizadeh
 

This study was conducted to isolate novel lactose utilizing Xanthomonas campestris mutants. Such a mutant will assist the utilization of whey as the sole carbon source for xanthan gum production, lower costs of fermentation process and set a precise application for whey as a waste. In this study, a mutant strain (NA1) was isolated from Xanthomonas campestris cells exposed to nitrous acid mutagenesis Environmental conditions were optimized and maximum activity of the β-galactosidase enzyme was obtained at pH 5.5 and 38°C following which the β-galactosidase activity in NA1 culture was increased 9.5 folds, compared to that of the wild type culture (336.1 U vs. 35.4 U). Xanthan gum production by NA1 using whey as carbon source was also studied. Using the experimental design of Plackett-Burman and statistical analysis, whey, as the main substrate and pH were the first factors affecting gum production among the seven parameters tested. Gum production using significant factors (such as substrate concentration and pH) was carried out in a lab-scale fermentor and 10 g L-1 xanthan was obtained.

  M. Islami , A. Shabani , M. Saifi-Abolhassan , Sh. Sepehr , M.R. Soudi and S.Z. Mossavi-Nejad
 

Purification and characterization of alcohol dehydrogenase (ADH) from Gluconobacter suboxydans was done in order to biotechnological and industrial application. Solubilization of enzyme from bacterial membrane fraction by Triton X-100 and subsequent fractionation on DEAE-Sephadex A-50 and Hydroxyapatite was successful in enzyme purification. Enzyme assay reaction mixture contained potassium ferricyanide 0.1 M, McIlvaine buffer 0.1 M (pH 5.5), Triton X-100 10%, ethanol 1 M and enzyme solution. The purified ADH Optimum pH activity was 5.5. The enzyme was in maximum stability in pH 5.8. The substrate specificity of the enzyme was determined using the same enzyme assay method as described above, except that various substrates (100 mM) were used instead of ethanol. The relative activity of the ADH for ethanol was higher than the others. The effects of metal ions and inhibitors on the activity of the enzyme were examined by measuring the activity using the same assay method as described above. Activity of purified enzyme was increased in the presence of Ca+2 and was decreased in presence the of ethylenediamine tetra acetic acid (EDTA). Because the proper structure and function of the enzyme is related to structural Ca+2 and EDTA can chelate Ca+2. An apparent Michaelis constant for ethanol were examined to be 1.7x10-3 M for ethanol as substrate.

  P. Ghadam , S. Gharavi , F. Yarian , M.R. Soudi , B. Kazemi and M. Bandehpour
  Among some Bacillus species, a protein highly homologous to HU, classified HB and coded by hbs gene. According to the recent studies, the sequence of hbs gene just in one strain of Bacillus subtilis exists in gene bank (ATCC 23857). In this study, DNA from Bacillus subtilis ATCC 6633 was extracted and investigated by PCR. The PCR product was sequenced and shown to differ in just one nucleotide from B. subtilis ATCC 23857. Hence, it was chosen as reference and for the first time, used for non-radioactive labeled probe preparation. The PCR product in Bacillus subtilis with ATCC 6633 was labeled using non-radioactive DIG-labeled nucleotides and conditions of probe preparation and hybridization were optimized and checked it by Southern blotting.
 
 
 
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