Enzyme activities and degradation of seed storage substances were investigated in BARI-1, BARI-2 and BARI-3 varieties of chickpea (Cicer arietinum L.) seed at different germinating periods. Among the varieties, the highest amylase activity was found in BARI-2 and lowest in BARI-3 during germination at 45 hours in water. The maximum activity of invertase was found in BARI-2 and minimum in BARI-1 at 72 hours of germination. Lipase activity was highest in BARI-2 and lowest in BARI-1. The highest protease activity was found in BARI-2 and lowest in BARI-3. The amount of total protein and water-soluble protein were found to be highest in BARI-1 and BARI-3, respectively. During light germination, carbohydrate depletion starts after initial imbibitions, and was completed in 120-144 hours. The variety BARI-1 was found to contain the highest amount of free sugar while BARI-3 had the lowest amount. BARI-2 was found to contain highest amount of reducing sugar and BARI-1 contained the lowest amount. The highest amount of starch was found in BARI-3 and lowest in BARI-1. The starch content in chickpea seed decreased gradually during germination. Among the varieties, BARI-1 was found to contain the highest amount of lipid while BARI-3 contained the lowest amount. The seed storage substances were found to decrease gradually with the increase of germination time. The results indicate that degradation of reserve seed nutrients accelerate the development of seedling growth during germination.

Context: Determination of the activities of hydrolytic enzymes from germinating wheat seeds and investigation of degraded nutrients from brassica and wheat seeds at different periods of germination are important factors for identification of richest sources of hydrolytic enzymes and nutrients.Objectives: To study the activities of hydrolytic enzymes and degradation of seed storage substances of brassica (Brassica napus L.) and wheat (Triticum aestivum L.) seeds during germination.Materials and Methods:  Three varieties of brassica (Brassica napus L., B. juncea L. and B. campestris L.) and three varieties of wheat (Akbar, Kanchan and Agrani) seeds were analyzed. Amylase, invertase, protease and lipase activities were assayed. Degradation of seed storage nutrients during germination were determined by conventional biochemical methods.Results: The activities of amylase, invertase, protease and lipase varied from 8.02 – 48.69, 2.45 – 15.32, 20.96 – 45.45 and 2.72 – 12.76 units/ ml respectively. Degradation of nutrients in the three species of brassica and wheat seeds was also studied at different periods of germination. The amount of free sugar in brassica and wheat seeds ranged from 0.93 – 4.27% and 3.82 – 4.88%; reducing sugar content from 0.012 - 0.093% and 0.032 - 0.078%; starch from 1.42 – 4.70% and 10.26 – 69.65%; total protein from 3.1 – 25.37% and 2.3 – 18.37%;  water-soluble protein from 1.5 – 14.24% and 1.0 – 6.50%;  and oil content from 2.49 – 43.6% and 1.04 – 1.92% respectively. Conclusion: The results suggest that the extracts from brassica and wheat seeds can be good sources of nutrients and hydrolytic enzymes which are applicable in food industry to improve food quality.Key words: Brassica; Wheat; Carbohydrate; Protein; Lipid; Hydrolytic Enzyme.DOI: 10.3329/jbs.v17i0.7114J. bio-sci. 17: 101-106, 2009

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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.