Yusria Elshiekh Abdalrahim, 2 Isam Mohamed Abu Zeid, 3 Saed A Al-Thobaiti and 1 Emadeldin Hassan Elsaid Konozy
Abstract
Abstract
Background and Objective: Acid phosphatase, an enzyme that acts to liberate phosphate under acidic conditions, is ubiquitous being
detected from bacteria to complex eukaryotic cells. This work was undertaken to isolate and purify acid phosphatase activity.
Materials and Methods: Three acid phosphatase isozymes ACP40, ACP60 and ACP80 were isolated and partially purified from the cassia
occidentalis seeds crude extract by fractional precipitation using salting-out techniques. Kinetics parameters like Km and Vmax were
calculated using p-Nitrophenyl Phosphate (p-NPP) as a substrate. The enzyme's stability was studied with respect to storage at the room,
temperature optima and denaturing agent. Results: The three enzymes shared a common pH optimum at 5.6 however with a wide range
of temperature optima. Cu++ and Zn++were inhibited the enzymes, whereas Mn++, Mg++ and Ca++ stimulated the enzymes. However, they
exhibited different degrees of stability against storage temperature and durability against denaturing agents like urea. Conclusion: The
variations in some biochemical parameters between the ACP's isozymes may indicate variability in their biological functions. In addition
to these, the ability to cope with the high concentration of nitrogen as well as high temperatures may make these enzymes qualified for
the use in biotechnology.
يسرية الشيخ عبدالرحيم عبدالواحد | Yusria Elshiekh Abdalrahim Abdalwahed | 323