Kinetic parameters of immobilized pectinase enzyme
Saad, S.MM.; Foda, F.F.A.; Abdel-Aleem, LM. and Gamal EleDeen, MS.
Biochem. Dept., Fac. of Agric. Moshtohor, Benha Branch, Egypt
Abstract
. Pectinase (E.C13.2. I .15), pectinex ultra SP-L enzymefrom Aspergillus aculearus has been immobilized Ofl
different supports materials i.e. porous glass beads, chain, chicken bone, sand and calcium alginate also the
kinetic parameters of immobilized forms were determined. The retention activities of bounded enzyme
preparations were found to be 8 1 86, 74h07, 78.39, 75.85 and 77.09% for the above mentioned supports,
rcspcctivr!y. The ortimum pH was 4.8 for immobilized forms on sand and ra-niginate gel heads, hut it was 4.8
tor chitin enzyme complex. ‘Ihe other preparations of pectinex ultra SP-L on glass beads and chicken bone had
the maximum activity at pH’s 51 and 5.0, respectively. On the other hand, optimum temperature reached 55° for
immobilized enzyme on chicken bone, 50°C for immobilized enzyme on activated sand and Ca-alginate but
immobilized forms on glass beads andactivateci chitin were found to be at 60°C.
Kinetic behaviors of the immobilized enzyme with different supports were determined. The tree enzyme
showed Km value of 0.74 1 00 g pectin which was increased after immobilization to 0.8 1 , O79 and 1 .0 1 g! I 00
g pectin for immobilized pectinex ultra SP-L on glass beads, activated chitin and Ca-alginate, respectively. A
decrease in Vnux values occurred upon enzyme immobilized for all supports. Also, the immobilized enzyme on
the above mentioned supports can be used 4 times with only lost about 5.52, 9.23, 5.8 1 , 6.36 and I 1 . 1 1 % of its
original activity. Enzymatic saccharification processes were 90.75, 86.78, 88. 10, 82.84 and 7495%. respectively
for immobilized pectinase enzyme on glass beads, chitin, chicken bone, sand and Ca-alginate, respectively.
Key word: Pectinase enzyme — Immobilization - Aspergitlus aculeatus - Pectinex ultra SP-L Enzyme - (ilass
beads — Chitin - Chicken bone - Sand - Calcium alginate. |
