Sallam,, S., Fahmy, W., Ushida, K. (2003). PHOSPHORILASES INDUCTION BY DIFFERENT CARSON SOURCES IN FOUR PREDOMINANT RUMEN BACTERIA. Journal of Animal and Poultry Production, 28(8), 6039-6054. doi: 10.21608/jappmu.2003.245041
S. M. A. Sallam,; W. G. Fahmy; K. Ushida. "PHOSPHORILASES INDUCTION BY DIFFERENT CARSON SOURCES IN FOUR PREDOMINANT RUMEN BACTERIA". Journal of Animal and Poultry Production, 28, 8, 2003, 6039-6054. doi: 10.21608/jappmu.2003.245041
Sallam,, S., Fahmy, W., Ushida, K. (2003). 'PHOSPHORILASES INDUCTION BY DIFFERENT CARSON SOURCES IN FOUR PREDOMINANT RUMEN BACTERIA', Journal of Animal and Poultry Production, 28(8), pp. 6039-6054. doi: 10.21608/jappmu.2003.245041
Sallam,, S., Fahmy, W., Ushida, K. PHOSPHORILASES INDUCTION BY DIFFERENT CARSON SOURCES IN FOUR PREDOMINANT RUMEN BACTERIA. Journal of Animal and Poultry Production, 2003; 28(8): 6039-6054. doi: 10.21608/jappmu.2003.245041
PHOSPHORILASES INDUCTION BY DIFFERENT CARSON SOURCES IN FOUR PREDOMINANT RUMEN BACTERIA
1Department of Animal Production, Faculty of Agriculture, Alexandria University, Alexandria, A.R.E.
2Kyoto Prefecurill University, Laboratory of Animal Science, Kyoto, Japan.
Abstract
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.
View on SCiNiTO
Top