The activities 01 some phosphorylase enzymes e.g. cellobiose
phosphorylase. cellotriose phosphorylase. maltose phosphorylase and lactose
phospphoryl9se. have bn~n examined in some rumen bacteria e.g. R.flavefae,ens 17,
8.fibrisolvenes OR77. P.bryanlii B,4 and S.DOVis A30 in vitro . The ceuotncse
phosphorylase activity was observed in R.fi8'1e'aCfens 17 and B.fibnsolvenes OR77.
The activity ot cellobiose phosphorylase was detected in R.flavefaciens 17.
B.fibrisolvenes OR77 ar.d P.bryanlii 6,4. Lactose phusphorylase activity was
lound in B.fibrisolvenes OR77, P.bryantii B,4 and S.bovis A30. While maltose
phosphorylase activity was detected only in S bovis A30. The induction of phosphor/'ases by some ca.con sources was investigated.   Cellobiose phosphorylase in R navetaciens 17 and P.bryanlii 8·4 is a constitutive
enzyme but ih B.fibrisolvenes OR77, it is inducible. Maltose has inducerl \he mauose
phosphorylase in S.bovis A30. The time-course experiment revealed that the cell
growth and ~e pattern ot enzyme production in R.flavelaciens 17 occurred WIthin 24
hr incubatioq time. The relationship between endoglucanase and cellotriose
phosphorylase was observed in R.flavefaciens 17 and it was concluded that the
production df celiotriose phosphorylase is paralic: with the production of
endoglucanase. All phosphorytases differ in their affinity and specificity (or substrate
and physiologicsl roles.Tne maximum growth was observed in the period between
1B-21 hr incubation in all carbon sources. The high level 0 f cellotriose £hoshorylaSe activity was p resent in cellulose
medium alter ~4 hr of incubalion at 37 C. Cellobiose phospborylase acli~;tf was found
in ceuoblose.dellodexulns.xyta« or cellulose-grow cells. The high level of activity was
with cellobiose. cellodextrins and xylan.