Partial Characterization of Protease activity fromRhynchophorus palmarum (Palm Weevil)

Palm weevil (Rhychophorus palmarum) poses treat to cultivated palm trees in central and southern Africa. It is also a natural source of protein in Asia and Africa. It is expected therefore, that protease from this source could have interesting properties and possible industrial applications. Protease produced by R. palmarum was purified by differential centrifugation and partially characterized by their caseinolytic activities. The enzyme optimal in the ranged of pH 8.4 to 9.2 and temperature of 23oC. The Michaelis-Menten’s constant (KM) of the enzyme for its substrate, casein and the maximum attainable velocity (VMax) were 5.51 x 10-2 mM and 45.0μg/min respectively. Metalions such as Sl+, Al3+, Ca2+, Hg2+, Na+, Ba2+ inhibited the activity of the enzyme, with Na+ producing the highest inhibition (32.5%) and Al3+ produced the least inhibition (2.9%). The paper discusses the various possible industrial applications of this protease and concludes that palm weevil can be a source of protease for some industrial applications.