On Basic Subunits Dissociated from C (11S) Component of Soybean Proteins with Urea |
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Authors: | Kazuyoshi Ôkubo Mitsuo Asano Yoshikazu Kimura Kazuo Shibasaki |
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Institution: | Department of Food Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan |
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Abstract: | Galactolipase (galactolipid acyl hydrolase, EC 3.1.1.26) was purified 147-fold in good yield (91 %) from rice bran by affinity chromatography, in which the enzyme was adsorbed on a palmitoylated gauze column at pH 5.5 and then was eluted with a buffer solution containing a detergent such as sodium deoxycholate or Triton X–100 at pH 8.0. The preparation obtained was further purified by gel filtration on a Sephadex G–100 column and isoelectric focusing. After electrophoresis, the enzyme separated into four components with different isoelectric points. It seems that galactolipase in rice bran exists in multiple forms. The major component (G–2) with isoelectric point of 7.3, one of them, was purified 268-fold and electrophoretically homogeneous. The enzyme (G–2) hydrolyzed rapidly galactolipid and also slowly phospholipid, but hardly triglyceride. |
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Keywords: | alcohol resistant metalloproteinase marine bacteria Vibrio sp purification |
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