Obligately anaerobic ruminal bacteria have been found to possess phytase ac
tivity, in particular, Selenomonas ruminantium. The phytase activity of S.
ruminantium JY35 was produced late in growth and required neither phytate f
or induction nor phosphate limitation for derepression. The activity was co
mpletely cell-associated with a significant fraction extractable by a magne
sium chloride solution. Zymogram analysis suggested that the activity was t
he result of a single gene product of a monomeric nature and approximately
46 kDa in size. The phytase had a temperature optimum of 50-55 degrees C, b
ut; activity dropped off sharply at 60 degrees C. Phytase activity was opti
mal over the pH range of 4.0-5.5, and dependent on the nature of the buffer
used. Activity was inhibited by citric acid buffer and by the addition of
5 mmol l(-1) Fe2+, Fe3+, Cu2+, Zn2+ and Hg2+. The addition of 5 mmol l(-1)
Pb2+ to the enzyme assay appeared to enhance activity of the enzyme.