Abstract
Candida rugosa lipose (CRL) was purified to homogeneity from crude powder CRL hydrolyses triocylglycerols without chain length specificity. A specific activity of about 800 U/mg was measured with triolein or tributyrin as substrate at 37degreesC and pH 8. CRL is a true lipose. This enzyme presents the interfacial activation phenomenon when tripropionin was used as substrate. Contrary to many lipases, CRL is able to hydrolyse its substrate in the presence of natural detergents. Synthetic detergents act as potent inhibitors of CRL activity. This effect disappears when bile salt is added to the lipolysis system. The covalent modification of CRL with tetrahydrolipstatine (THL) inactivates the enzyme. This result confirms that CRL is a serine enzyme like all liposes from various origins.