Investigations have been carried out on an acid protease produced by M
ucor bacilliformis under solid-state fermentation conditions as a mode
l of recovery and purification of a protein from a solid culture mediu
m. The leaching efficiency of sodium chloride solutions to recover the
enzyme from the fermented mass was higher than that of non-ionic dete
rgents (Triton X-100 or Tween 80) or distilled water. Concentration an
d coarse fractionation of the crude extract could be achieved with a h
igh yield of protease by precipitation with ethanol or acetone and by
ultrafiltration and diafiltration in the presence of NaCl. Diafiltrati
on was selected for the prechromatographic treatment of the crude extr
act as it enhances the maximum fraction of enzyme bound to an anion-ex
changer up to 0.9. An overall purification factor of 15.5 was reached,
with a total enzyme recovery of 46%, with the purification procedure
developed by using this methodology. The final product obtained was a
highly purified food-grade protease preparation. (C) 1998 Elsevier Sci
ence B.V. All rights reserved.