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Articles by B. Mandal
Total Records ( 2 ) for B. Mandal
  P. Chowdhury , R. Hari , B. Chakraborty , B. Mandal , S. Naskar and Nirmalendu Das
  Pleurotus fossulatus (Cooke) Sace is member of oyster mushroom can produced extracellular laccase (benzenediol: oxygen oxidoreductase; EC 1.10.3.2) in submerged fermentation. To analyze the optimum production for laccase P. fossulatus was cultured both in stationary and shaking condition in different media. Partial purification of laccase was done after 0-80% ammonium sulphate precipitation, followed by DEAE (Diethylaminoethyl) Sephadex (A-50) anion exchange chromatography. Potato-sucrose peptone (PSP) medium and Potato-dextrose (PD) medium showed highest laccase production in shaking and stationary conditions, respectively. Though the time required for optimum laccase production in stationary condition was much more than the shaking condition but the amount of laccase was about 2.75t greater in former condition. The laccase produced in stationary condition was more stable than the enzyme produced in shaking condition. The partially purified enzyme showed highest affinity towards o-dianisidine than guaiacol and ABTS (2,2’- Azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) as evidenced by their Km. The physico-chemical properties of the laccase suggested the significance of this enzyme in industrial applications.
  S. Sen , V. Venkata Dasu , K. Dutta and B. Mandal
  Recently, alkaline proteases are of great importance due to their several industrial (detergent, tanning, textile and dairy industries, organic synthesis, peptide synthesis) and environmental applications. The objective of this study was to purify and characterize a novel surfactant and organic solvent stable high-alkaline protease from a new Bacillus pseudofirmus SVB1 (Shampa Venkata Bacillus isolate 1). The potential of the culture broth of a newly isolated Bacillus pseudofirmus SVB1 have evaluated in hydrolyzing natural proteins viz., egg albumin, blood, poultry feather and goat skin hair. An unusually large (85 kDa) serine alkaline protease was purified from the cell supernatant. High stability of the alkaline protease was found in the presence of surfactants, oxidizing agents, heavy metal ions and particularly organic solvents. The maximum activity was observed at an optimal pH of 10.0 and temperature of 40°C. The results obtained in this research study inferred that the purified alkaline protease was a novel surfactant and organic solvent tolerant enzyme with potential applications for various industrial processes.
 
 
 
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