Aggregation behavior of Candida rugosa lipase

Candida rugosa lipase aggregated in aqueous media. The emission maximum wav elengths for both intrinsic tryptophan fluorescence and surface hydrophobic ity, determined using the probe 8-anilino-1-naphthalene sulfonate, were blu e-shifted upon aggregation of CRL. Dynamic light scattering also showed an increase in the molecular weight of CRL as a function of increasing protein concentration. Apparent dissociation constants derived from the three tech niques were 0.48, 3.5 and 1.9 mu g/ml, respectively. The specific activity of aggregated species (3135 U/mg) was higher than the monomer's (860 U/mg). The aggregation state of lipases may influence kinetic properties, specifi city and interfacial behavior. (C) 1999 Canadian Institute of Food Science and Technology. Published by Elsevier Science Ltd. All rights reserved.