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Characterization of partially purified and immobilized partially purified protease extracted from silver catfish (pangasius sutchi) viscera
Siti Noorsyarafana Sahimi1, Normah Ismail2.
ABSTRACT
Viscera is known as one of the richest sources of proteolytic enzymes.
However, the biggest problem regarding enzyme is the rapid deterioration
and lose in functional properties due to inefficient treatment and improper
storage condition. Therefore, in this study, protease from silver catfish
viscera have been extracted, partially purified by acetone precipitation
method and immobilized in the calcium alginate beads. Concentrations
of 2.99 % (w/v) sodium alginate and 0.30 M calcium chloride were used
to produce the immobilized partially purified protease. Then, the partially
purified and immobilized partially purified protease were characterized in
different range of pH, temperature and storage period in order to establish
a greater protease stability during storage and increase in its efficiency.
Proteolytic activity of the partially purified and immobilized partially
purified protease in the alginate beads were measured by using casein as a
substrate. The highest proteolytic activity for partially purified protease was
recorded at pH 4 (5709.76 CDU/mg) and 40 °C (6061.14 CDU/mg) and for
immobilized partially purified protease at pH 5 (3987.85 CDU/mg) and 50
°C (4956.54 CDU/mg). For storage stability, the partially purified protease
has optimum storage temperature at – 40 °C while the immobilized partially
purified protease at 4 °C. of 17.44 and 24.50 %, respectively for 6th days
of storage. At optimum storage condition, the partially purified protease
and immobilized partially purified protease have storage efficiency of 17.44
and 24.50 %, respectively for 6th days of storage.
Affiliation:
- Universiti Teknologi MARA (UiTM), Shah Alam, Selangor, Malaysia
- Universiti Teknologi MARA (UiTM), Shah Alam, Selangor, Malaysia
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