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Artificial Cells, Blood Substitutes, and Biotechnology Volume 40, 2012 - Issue 6
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Research Article

Purification and characterization of prophenoloxidase from Galleria mellonella L.

Dudu DemirBalikesir University, Science & Art Faculty, Department of Chemistry 10100 Balikesir / TURKEY
,
Nahit GençerBalikesir University, Science & Art Faculty, Department of Chemistry 10100 Balikesir / TURKEYCorrespondence[email protected]
&
Aylin ErBalikesir University, Science & Art Faculty, Department of Biology 10100 Balikesir /TURKEY
Pages 391-395 | Received 05 Mar 2012, Accepted 03 May 2012, Published online: 10 Jul 2012
 
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Abstract

Prophenoloxidase (PPO) was purified from Galleria mellonella L. A 67-fold purification of the proenzyme with 352% yield was achieved by using a Sepharose 4B-L-tyrosine-p-amino benzoic acid affinity column. The purified enzyme was migrated as a single band on SDS-polyacrylamide gel electrophoresis. Km and Vmax values were 0.017 M and 1430.45 EU for catechol. Inhibition of PPO was investigated with inhibitors such as p-aminobenzoic acid, etyleneglycol, and ascorbic acid. Among them, ascorbic acid showed the strongest inhibitory activity with IC50 value of 2.94 μM. The current paper represents new strategies for the biological control of the Galleria mellonella L. insect.

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