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Articles by Khalil-ur-Rehman
Total Records ( 3 ) for Khalil-ur-Rehman
  Hafiz M. Hamid , Khalil-ur-Rehman , M. Anjum Zia and M. Asgher
  The enzyme glucose oxidase was produced by fermentation technology, using Aspergillus niger as fermentation organism and rice polishing as substrate. Maximum production of enzyme (3.42 U mL-1) was recovered at substrate level of 2% after 36 h of submerged fermentation. The pH for the optimal production of enzyme was found to be 4. Addition of salts such as urea (0.3%), CaCO3 (0.04%) and KH2PO4 (0.6%) into the fermentation medium enhanced enzyme production while MGSO4.7H2O was found to inhabit microbial growth and glucose oxidase production by A. niger.
  M. Anjum Zia , Khalil-ur-Rehman , M. Khalid Saeed , Aftab Ahmed and Abdul Ghaffar
  Peroxidase from tomato was extracted and partially purified by means of ammonium sulphate [(NH4)2SO4] precipitation technique and ion exchange chromatography. The crude extract having the specific activity of 0.239U mg-1 was subjected to (NH4)2SO4 precipitation technique for partial purification of peroxidase. The specific activity of (NH4)2SO4 precipitated enzyme was 0.546U mg-1 with protein contents of 0.412mg ml-1. After ion exchange chromatography through DEAE-Cellulose columns, the specific activity was 11.844U mg-1 and the protein contents were decreased to 0.0358mg ml-1 showing that unnecessary proteins have been eliminated. Finally, partially purified enzyme was subjected to SDS-Electrophoresis for confirming the purification. So it was concluded that crude and partially purified enzymes from tomato possess an appreciable enzyme activity.
  Farzana Habib , Khalil-ur-Rehman , M. Anjum Zia , Zia-ur-Rehman and M. Khalid Saeed
  Peroxidase, extracted from soybean seeds and was partially purified by precipitating with ammonium sulfate and 85 % saturation resulted in an increase in the activity of peroxidase up to 1.21 fold. Purification was carried out by diethyl amminoethyl cellulose chromatography and purification fold obtained was 2.62. Then, the enzyme was subjected to 10 % sodium dodecyl sulfate polyacrylamide gel electrophoresis which resulted in a marked decrease in unwanted proteins.
 
 
 
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