Abstract:
:Analysis of peroxidase activity by native polyacrylamide gel electrophoresis (PAGE) from a garlic bulb (Allium sativum L) extract showed two major activities (designated POX1 and POX2). The POX2 isoenzyme was purified to homogeneity by ammonium sulfate precipitation, gel filtration, and cation-exchange chromatography. The purified enzyme was found to be monomeric with a molecular mass of 36.5 kDa, as determined by sodium dodecyl sulfate-PAGE. The optimum temperature ranged from 25 to 40 degrees C and optimum pH was about 5.0. The apparent Km values for guaiacol and H2O2 were 9.5 and 2 mM, respectively. POX2 appeared highly stable since 50% of its activity was conserved at 50 degrees C for 5 h. Moreover POX2 was stable over a pH range of 3.5-11.0. Immobilization of POX2 was achieved by covalent binding of the enzyme to an epoxy-Sepharose matrix. The immobilized enzyme showed great stability toward heat and storage when compared with soluble enzyme. These properties permit the use of this enzyme as a biosensor to detect H2O2 in some food components such as milk or its derivatives.
journal_name
Appl Biochem Biotechnoljournal_title
Applied biochemistry and biotechnologyauthors
Marzouki SM,Limam F,Smaali MI,Ulber R,Marzouki MNdoi
10.1385/abab:127:3:201subject
Has Abstractpub_date
2005-12-01 00:00:00pages
201-14issue
3eissn
0273-2289issn
1559-0291pii
ABAB:127:3:201journal_volume
127pub_type
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