Horizon 1 1 17 ACL : Articles dans des revues avec comité de lecture répertoriées par l'AERES Enzyme and Microbial Technology 1042-1050 Rhizopus homothallicus thermophilic and thermotolerant fungi solid state fermentation submerged fermentation lipase purification 2006 fdi:010035742 ENG Enzyme and Microbial Technology 0141-0229 CC:0002396945-0012 5 10.1016/j.enzmictec.2006.02.005 https://www.documentation.ird.fr/hor/fdi:010035742 https://www.documentation.ird.fr/intranet/publi/2006/09/010035742.pdf 39 Horizon (IRD) Extracellular lipases were obtained from solid (SSF) and submerged (SmF) thermotolerant Rhizopus homothallicus fungus cell cultures and purified to homogeneity. The two enzymes are monomers having a molecular mass of 29.5 kDa and an identical protein structure, since the N-terminal sequences and peptide maps were identical. However, some of their properties are different, namely the specific activity on trioctanoin (8600 U/mg with SmF and 10,700 U/mg with SSF), the temperature at which maximum activity occurs (30 degrees C with SmF and 40 degrees C with SSF) and the thermal stability (half-lives at 50 degrees C of 0.44 h with SmF and 0.72 h with SSF). These differences between the kinetic properties suggest that when they were tested, one or both fungal lipases might still have been associated with non-proteic compounds originating from the culture medium. (c) 2006 Elsevier Inc. All rights reserved. 084