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Articles by Niranjan Kumar Sana
Total Records ( 2 ) for Niranjan Kumar Sana
  M. Omar Faruk , M. Ziaul Amin , Niranjan Kumar Sana , Ranajit Kumar Shaha and Kamal Krishna Biswas
  In this study, two varieties (Green and red) of water chestnuts (Trapa sp.) have been selected for their biochemical analysis as well as nutrient composition using standard methods. The proximate composition of green water chestnuts revealed moisture 62.5, ash 1.04, crude fiber 2.13%, total soluble sugar 0.92%, reducing sugar 0.33%, non-reducing sugar 0.59%, starch 8.7%, lipid 0.84%. One hundred gram of green variety contained water soluble protein 0.275 mg, β-Carotene 60 μg, vitamin-C 1.1 mg and total phenol 0.5 mg. The minerals contents of green variety were potassium 5.22%, sodium 0.64%, calcium 0.25%, phosphorus 6.77%, sulpher 0.38%, and iron, copper, manganese and zinc 200, 430, 90 and 600 ppm, respectively. The red variety contained moisture 62.7%, ash 1.30%, crude fiber 2.27%, total soluble sugar 0.90%, reducing sugar 0.30%, non-reducing sugar 0.60%, starch 8.2%, lipid 0.83%. The red variety contained water soluble protein 0.251 mg, β-Carotene 92 μg, vitamin-C 0.9 mg and total phenol 0.60 mg per 100 g. The red variety contained potassium 5.32%, sodium 0.59%, calcium 0.26% phosphorus 6.77%, sulpher 0.32%, Iron 200 ppm, copper 450 ppm, manganese 110 ppm and zinc 650 ppm. The free amino acids, glutamic acid, tryptophan, tyrosine, alanine, lysine and leucine were commonly found in both varieties. In addition, green and red variety contained cysteine, arginine and proline and glutamine and asparagines, respectively. Thus, the present study sheds light on the nutrient contents of the two varieties of water chestnuts and suggests that water chestnuts may play a crucial role in human nutrition.
  Niranjan Kumar Sana , Narayan Roy , Kamal Krishna Biswas and Entazul M. Huque
  The carbohydrate binding protein (Lectin) of the sesame oil seeds have been purified from the seed homogenate by 100% ammonium sulfate precipitation followed by gel filtration on Sephadex G-75 and ion exchange chromatography on DEAE-cellulose. The purified lectin was found to be homogeneous in polyacrylamide gel electrophoresis. The protein has a molecular weight of 25 kDa. Both in the disc and SDS-PAGE analysis only a single band was observed indicating that the protein does not contain any subunit. The protein is agglutinated with erythrocytes of albino rat. The binding of the protein to erythrocytes of albino rat was inhibited by mannose and glucosamine indicating that the protein possesses two binding sites for carbohydrates. The percentage of sugar present in the glycoprotein was found to be about 10%. The reducing sugar in the hydrolysate of the protein was identified to be galactose. The pH stability of the protein was studied. The protein showed its hemagglutination activity in the pH range 6.5 to 8.4.
 
 
 
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