Open AccessPeroxidase from infected fruit of Solanum sp. grown in Nsukka
Author(s) -
Omeje Ko,
Sabinus Oscar Onyebuchi Eze,
Ferdinand C. Chilaka
Publication year - 2019
Publication title -
bangladesh journal of scientific and industrial research
Language(s) - English
Resource type - Journals
eISSN - 2224-7157
pISSN - 0304-9809
DOI - 10.3329/bjsir.v54i2.41669
Subject(s) - peroxidase , ammonium sulfate precipitation , enzyme , chemistry , ion chromatography , size exclusion chromatography , substrate (aquarium) , ammonium , enzyme assay , chromatography , ammonium sulfate , biochemistry , biology , organic chemistry , ecology
In this study, we characterized the activity of peroxidase a quality control enzyme from the infected fruit of Solanum sp. Peroxidase was purified to homogeneity by ammonium sulfate precipitation, dialysis, ion exchange chromatography and size exclusion chromatography. The molecular weight of the native enzyme was 63000 da. The enzyme was shown to have two iso-enzymes with distinct optimum pH of 4.5 and 7.0 and optimum temperature of 40 and 70⁰C. The purified enzyme had broad substrate specificity with o-dianisidine being the ideal substrate. Na+, Ca2+, Mg2+, Mn2+, Cu2+, Al3+ were shown to be activators of the enzyme, while the peroxidase activity was severely inhibited by Co2+.
Bangladesh J. Sci. Ind. Res.54(2), 131-138, 2019