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KMID : 0380619840160030322
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Korean Journal of Food Science and Technology
1984 Volume.16 No. 3 p.322 ~ p.328
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Purification of Glucoamylase Produced by Rhizopus oryzae
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Abstract
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These experiments were conducted to purify the glucoamylase produced by Rhizopus oryzae. Two forms of glucoamylase (GI and GII) from Phizopus oryzae were purified by
(NH₄)₂SO₄ fractionation, acetone fractionation and successive column chromatography on DEAF-cellulose and CM-cellulose. The specific activities of GI and GII toward soluble starch were 157.6 U/㎎. protein (37.5 fold of crude extract), and 164.7 U/㎎. ptrotein (39.2 fold of curde extract), respectively, and the yields of them were 4.3% and 3.8%, respectively. The two purified enzymes have shown a single band by polyacrylamide disc gel electrophoresis and SDS-polyacrylamide gel electrophoresis. The protein bands of their electrophoresis gel were revealed to have glucoamylase activity by iodine staining and were proved to be glycoprotein by periodic acid Schiff´s staining.
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