Articles
SOME PROPERTIES OF PEROXIDASE EXTRACTED FROM PULP OF STAR FRUIT (OXALIDACIA AVERRHOA)
Article number
864_57
Pages
415 – 421
Language
English
Abstract
The soluble and ionically bound peroxidase (EC. 1.11.1.7) was extracted from the star fruit in different stages of maturation.
The extracts were prepared using solution 100 mM sodium phosphate buffer at pH 7.0 and the enzymatic activity of those extracts were measured.
The maturation degree did not show an influence in the activity of soluble peroxidase; however the same change in the activity for the ionic bound peroxidase was observed.
For the study of the thermal stability of the peroxidase, the crude extracts were submitted at temperatures of 60, 65, 70, 75, 80 and 85°C and the enzymatic activity was carried out in intervals of 0, 2, 4, 6, 8 and 10 minutes.
It was observed that the enzyme lost activity with increased of the time and the temperature.
In the purification step, the concentrated extract of the soluble peroxidase was dialyzed, using a solution of 10 mM of the sodium phosphate buffer pH 7.0, after the sample was applied in a chromatographic column (16 mm i.d. × 70 cm) packed with Sephacryl HS100 with flow rate of 30 ml/h.
The results of electrophoresis show a presence of one pattern of the anionic isoenzyme.
The extracts were prepared using solution 100 mM sodium phosphate buffer at pH 7.0 and the enzymatic activity of those extracts were measured.
The maturation degree did not show an influence in the activity of soluble peroxidase; however the same change in the activity for the ionic bound peroxidase was observed.
For the study of the thermal stability of the peroxidase, the crude extracts were submitted at temperatures of 60, 65, 70, 75, 80 and 85°C and the enzymatic activity was carried out in intervals of 0, 2, 4, 6, 8 and 10 minutes.
It was observed that the enzyme lost activity with increased of the time and the temperature.
In the purification step, the concentrated extract of the soluble peroxidase was dialyzed, using a solution of 10 mM of the sodium phosphate buffer pH 7.0, after the sample was applied in a chromatographic column (16 mm i.d. × 70 cm) packed with Sephacryl HS100 with flow rate of 30 ml/h.
The results of electrophoresis show a presence of one pattern of the anionic isoenzyme.
Authors
C. Laurenti, E. Clemente
Keywords
pulp fruit, maturation stage, enzymatic activity, thermal stability, isoenzyme
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