• Applied Biological Chemistry
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• v.36 no.2
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• pp.121-126
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• 1993

To extract insoluble proteins of sesame meal residue by using microorganism, the sesame meal residue was treated with crude enzyme solution from Bacillus sp. CW-1121. It was found that the solubility reached to maximum at pH 7.5, $45^{\circ}C$. Under optimum condition, the nitrogen solubility with the enzyme solution from Bacillus sp. CW-1121 reached to 60% in 2 hours. Nitrogen solubility of protein from sesame meal showed minimum value at pH 4.5 and significantly increased above pH 6.0. When the protein from sesame meal extracted with Bacillus sp. CW-1121 was subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis, water soluble protein was showed 4 bands and salt soluble protein was showed 2 bands. The amino acid composition of water soluble protein, salt soluble protein and free amino acid indicated relatively high contents of serine (17.24 mg/g), glutamic acid (10.77 mg/g) and glutamic acid (6.55 mg/g). Specially, the contents of essential amino acids were high.

• Journal of the Korean Society of Food Science and Nutrition
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• v.20 no.4
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• pp.388-394
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• 1991

Alkaline protease producing bacteria were isolated from soil and identified as Bacillus sp. CW-1121. It was found that the production of alkaline protease reached to maximum in 5 day of fermentation at 4$0^{\circ}C$. The enzyme was purified by ammonium sulfate precipitation, gel filtration on Sephadex G-150 and DEAE-cellulose ion-exchange chromatography. The homogeneity of the purified enzyme was verified by polyacrylamide gel electrophoresis. The enzyme was purified 5.72 fold and yield of the enzyme purification was 16.71%. When the purified enzyme was applied to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the molecular weight was estimated to be 55, 000.

• Applied Biological Chemistry
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• v.36 no.3
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• pp.172-177
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• 1993

To extract insoluble proteins from sesame meal residue by microorganism, the sesame meal residue was treated with crude enzyme solution of Bacillus sp. CW-1121. The foaming capacity of salt soluble protein was quite lower than that of water soluble protein and the foaming stability of salt soluble protein decreased abruptly in 10 min., while it sustained for 30 min in case of water soluble protein. Emulsion capacities of all the protein fractions showed minimum value near isoelectric point of protein and salt soluble protein had lower emulsion capacities than that of water soluble protein. The emulsion stability of the protein was relatively stable for 30 min at $80^{\circ}C$. Oil and water absorption capacities of salt soluble protein were higher than those of water soluble protein.