@article{fdi:010035742,
  title = {{L}ipase from the thermotolerant fungus {R}hizopus homothallicus is more thermostable when produced using solid state fermentation than liquid fermentation procedures},
  author = {{D}iaz, {J}. {C}. {M}. and {R}odriguez, {J}. {A}. and {R}oussos, {S}evastianos and {C}ordova, {J}. and {A}bousalham, {A}. and {C}arriere, {F}. and {B}aratti, {J}.},
  editor = {},
  language = {{ENG}},
  abstract = {{E}xtracellular lipases were obtained from solid ({SSF}) and submerged ({S}m{F}) thermotolerant {R}hizopus homothallicus fungus cell cultures and purified to homogeneity. {T}he two enzymes are monomers having a molecular mass of 29.5 k{D}a and an identical protein structure, since the {N}-terminal sequences and peptide maps were identical. {H}owever, some of their properties are different, namely the specific activity on trioctanoin (8600 {U}/mg with {S}m{F} and 10,700 {U}/mg with {SSF}), the temperature at which maximum activity occurs (30 degrees {C} with {S}m{F} and 40 degrees {C} with {SSF}) and the thermal stability (half-lives at 50 degrees {C} of 0.44 h with {S}m{F} and 0.72 h with {SSF}). {T}hese 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 {E}lsevier {I}nc. {A}ll rights reserved.},
  keywords = {{R}hizopus homothallicus ; thermophilic and thermotolerant fungi ; solid state fermentation ; submerged fermentation ; lipase ; purification},
  booktitle = {},
  journal = {{E}nzyme and {M}icrobial {T}echnology},
  volume = {39},
  numero = {5},
  pages = {1042--1050},
  ISSN = {0141-0229},
  year = {2006},
  DOI = {10.1016/j.enzmictec.2006.02.005},
  URL = {https://www.documentation.ird.fr/hor/fdi:010035742},
}