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Isolation, purification and characterization of a protease from the seeds of Artocarpus heterophyllus

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Title Isolation, purification and characterization of a protease from the seeds of Artocarpus heterophyllus
 
Creator Pandey, Monika
Hajela, Krishnan
 
Subject Artocarpus heterophyllus
BAPNA
CD spectra
Dynamic light scattering
Proteases
Serine endopeptidase
 
Description 690-702
Proteases are being widely used in various industries like detergent, leather, food and pharmaceuticals.Protease was
purified to homogeneity from the seeds of Artocarpus heterophyllus. The enzyme was found to be a tetramer having
molecular mass of 74 kDa. Gelatin zymography showed a clear band of proteolysis. The enzyme isolated and purified was a
serine protease, as indicated by its inhibition with PMSF. The enzyme was stable at broad pH and temperature ranges with
pH and temperature optima at 8.5 and 50°C, respectively. The presence of some divalent ions enhanced the activity. With
the addition of calcium, change in absorption and emission spectra was observed in spectrofluorometric analysis. The Km
and Vmax for the enzyme was found to be 0.229 μM and 0.014 μM min1, respectively, using BAPNA as a substrate. The
enzyme consisted 4.44% alpha helix and 44.17% beta sheets when measured by CD spectra. Dynamic light scattering of the
protease for particle size distribution revealed the mono-dispersity of the sample. Easy purification and paramount stability
of protease makes it a good candidate for industrial and pharmaceutical applications.
 
Date 2023-09-20T05:16:10Z
2023-09-20T05:16:10Z
2023-09
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://nopr.niscpr.res.in/handle/123456789/62533
https://doi.org/10.56042/ijbb.v60i9.4053
 
Language en
 
Publisher NIScPR-CSIR,India
 
Source IJBB Vol.60(09) [September 2023]