Purification and Characterization of Lignin Peroxidase Isozymes from Humicola grisea (Traaen) and Its Application in Bioremediation of Textile Dyes

Document Type : Regular issue (Original Article)

Authors

1 Botany & Microbiology Department, Faculty of Science, Cairo University, Cairo, Egypt

2 botany and microbioogy department, faculty of science, cairo university

3 Faculty of Science,Fayoum University,Fayoum, Egypt

4 phD candidate

Abstract

PEROXIDASES have numerous important applications in industries and biodegradation of organopollutants , so there is a need to explore more and more sources of enzymes with different characteristics. In the present study, lignin peroxidases (LiPs) producing by fungus Humicola grisea were extracted and purified using gel filtration and ion exchange chromatography. Protein and heme protein were eluted in different peaks about 6 of these peaks had LiP activity and this is an indication that LiP in H. grisea was isoenzymes. Four of these isoenzymes were characterized regarding their molecular mass, optimum temperature and optimum pH for activity, substrate concentration and effect of some metal ions. The four purified isoenzymes have maximum activities at different temperatures, where optimum temperature for H2 and H4 isoenzyme were at 60 ºC, and the optimum temperatures for H1 and H3 were at 40 ºC and 30 ºC, respectively. The maximum activities of the four isoenzymes were within the acidic range. The different LiP isoenzymes showed different Km and Vmax values representing the varied affinity of the four isoenzymes using veratryl alcohol as a substrate. Km values for H1, H2, H3 and H4 were 5.26, 5.0, 1.3 and 1.4, respectively. While Vmax values for the same isoenzymes were 1.25, 0.8, 0.87 and 1.1, respectively.

Keywords

Egyptian Journal of Botany
Volume 57, Issue 2
August 2017
Pages 335-343

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