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1.
J Environ Biol ; 2009 Sept; 30(5): 641-646
Article in English | IMSEAR | ID: sea-146251

ABSTRACT

Presence of pathogens in high numbers in waste water is a cause of concern. Techno economic feasibility has restricted the conventional and non conventional treatment approaches for pathogen removal. Despite prolific use, carbon adsorption technology remains an expensive treatment process. The present study investigates the use of rice husk (RH), saw dust (SD), groundnut shells (GS) as natural agro-residues and partially weathered deccan trap basalt (PWDTB) for their sorption capacities and desorption pattern for two indicator organisms viz. Escherichia coli K12 and Staphylococcus aureus. Sorption experiments were carried out at flow-rate of 1.5 bed volumes per hour (bv hr-1) for cell suspension volume of 4, 8, 16 and 32 bed volumes. PWDTB have shown high sorption coefficient and log removal for E. coli K12 whereas GS have shown high sorption coefficient and log removal for S. aureus. PWDTB have shown maximum desorption constant and log retention for E. coli K12 whereas GS have shown maximum desorption constant and log retention for S. aureus during desorption experiment. Retention pattern suggest that adsorption is partially irreversible for almost all the materials used. It suggest that PWDTB in combination with RH and / GS could help in removal of pathogens from waste water.

2.
Indian J Exp Biol ; 2003 Jun; 41(6): 614-9
Article in English | IMSEAR | ID: sea-62421

ABSTRACT

A new extracellular protease having a prospective application in the food industry was isolated from Bacillus sUbtilis NCIM 2711 by (NH4)2SO4 precipitation from the cell broth. It was purified using DEAE-Cellulose and CM-Sephadex C-50 ion-exchange chromatography. With casein as a substrate, the proteolytic activity of the purified protease was found to be optimal at pH 7.0 and temperature 55 degrees C with Km 1.06 mg/ml. The enzyme was stable over a pH range 6.5-8.0 at 30 degrees C for 1 hr in presence of CaCl2 x 2H2O. At 55 degrees C, the enzyme retained 60% activity up to 15 min in presence of CaCl2 x 2H2O. EDTA and o-phenanthroline (OP) completely inhibited the enzyme activity while DFP, PMSF and iodoacetamide were ineffective. The enzyme was completely inhibited by Hg2+ and partially by Cd2+, Cu2+, Ni2+, Pb2+ and Fe2+. The OP inhibited enzyme could be reactivated by Zn2+ and Co2+ up to 75% and 69% respectively. It is a neutral metalloprotease showing a single band of 43 kDa on SDS-PAGE.


Subject(s)
Bacillus subtilis/enzymology , Chromatography, Ion Exchange , Electrophoresis, Polyacrylamide Gel , Endopeptidases/isolation & purification
3.
J Indian Med Assoc ; 1960 Feb; 34(): 92-6
Article in English | IMSEAR | ID: sea-95683
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