%0 Journal Article
%9 ACL : Articles dans des revues avec comité de lecture répertoriées par l'AERES
%A Diaz, J. C. M.
%A Rodriguez, J. A.
%A Roussos, Sevastianos
%A Cordova, J.
%A Abousalham, A.
%A Carriere, F.
%A Baratti, J.
%T Lipase from the thermotolerant fungus Rhizopus homothallicus is more thermostable when produced using solid state fermentation than liquid fermentation procedures
%D 2006
%L fdi:010035742
%G ENG
%J Enzyme and Microbial Technology
%@ 0141-0229
%K Rhizopus homothallicus ; thermophilic and thermotolerant fungi ; solid state fermentation ; submerged fermentation ; lipase ; purification
%M CC:0002396945-0012
%N 5
%P 1042-1050
%R 10.1016/j.enzmictec.2006.02.005
%U https://www.documentation.ird.fr/hor/fdi:010035742
%> https://www.documentation.ird.fr/intranet/publi/2006/09/010035742.pdf
%V 39
%W Horizon (IRD)
%X 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