The Purification and the Properties of Three Kinds of Lipases from Rhizopus delemer
Mieko Iwai, Yoshio Tsujisaka
Abstract
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Mieko Iwai, Yoshio Tsujisaka
Abstract
Open-access reader
The study was undertaken to clarify whether three kinds of lipases (EC 3.1.1.3) secreted from Rhizopus delemar are originally different or identical with each other. First of all, the purification of those lipases was carried out and their enzymatic properties were examined. Their properties including the stability on heat and pH, precipitabilities at a certain pH, the behaviours on a SE-Sephadex C50 column and on a Sephadex G200 column and so on were compared. From the results, A-lipase is clearly different from the other two lipases. On the other hand, it seems that B- and C-lipases are originally identical.
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The study was undertaken to clarify whether three kinds of lipases (EC 3.1.1.3) secreted from Rhizopus delemar are originally different or identical with each other. First of all, the purification of those lipases was carried out and their enzymatic properties were examined. Their properties including the stability on heat and pH, precipitabilities at a certain pH, the behaviours on a SE-Sephadex C50 column and on a Sephadex G200 column and so on were compared. From the results, A-lipase is clearly different from the other two lipases. On the other hand, it seems that B- and C-lipases are originally identical.
Key concepts: Lipase, Sephadex, Chemistry, Rhizopus, Enzyme, Chromatography, Triacylglycerol lipase, Heat stability