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KMID : 0380619760080030141
Korean Journal of Food Science and Technology
1976 Volume.8 No. 3 p.141 ~ p.146
Studies on the Lipolytic Enzyme of Molds


Abstract
1) The purified enzyme was obtained with the specific activity 126.5 u/§· protein (about 45 times of the original activity) and the yield of 4.2%, by means of salting out with ammonium sulfate (0.5 saturation) of the crude enzyme solution, desalting by Sephadex G 25, CM cellulose columm chromatography, concentration by Sephadex G 25, and gel filtration by Sephadex G 75.
2) In the acrylamide gel disc electrophoresis of the purified enzyme, the main band and two obscure ones on the both side of the main band appeared, which indicated that the enzyme was considerably purified compared with its crude enzyme solution, even if it is not referred to as a pure protein.
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