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Extraction, Purification And Characterization Of Artocarpus Altilis Latex Protease As A Fibrino(Geno)lytic Agent

The harvesting of Artocarpus altilis (breadfruit) in plantations involves the process of draining the latex to avoid staining of the epicarp. The exudate is not fully utilized and it has no commercial value. Ethnopharmacological applications of the latex in wound healing imply its action on blood co...

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Main Author: Zulfigar, Siti Balqis
Format: Thesis
Language:English
Published: 2019
Subjects:
T1-995 Technology(General)
Online Access:http://eprints.usm.my/55846/1/SITI%20BALQIS24.pdf
http://eprints.usm.my/55846/
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spelling my.usm.eprints.55846 http://eprints.usm.my/55846/ Extraction, Purification And Characterization Of Artocarpus Altilis Latex Protease As A Fibrino(Geno)lytic Agent Zulfigar, Siti Balqis T1-995 Technology(General) The harvesting of Artocarpus altilis (breadfruit) in plantations involves the process of draining the latex to avoid staining of the epicarp. The exudate is not fully utilized and it has no commercial value. Ethnopharmacological applications of the latex in wound healing imply its action on blood coagulation and fibrinolysis. Partial purification of A. altilis latex through HiTrapTM SP Sepharose chromatography had purified a 72 kDa protease by 3.1-fold with 24% recovery and the specific activity of 4.87 U/mg. This serine protease was inhibited by phenylmethanesulfonyl fluoride (PMSF) (1 mM and 10 mM) with 89% and 27% of residual activities respectively. The protease showed maximal activity at pH 10 with casein and bovine serum albumin (BSA) as substrates. The protease’s apparent optimal temperature after 30 minutes of incubation was 80C. The Km and Vmax values on casein were 0.453 ± 0.026 mM and 0.022 ± 0.001 μmol/min, respectively. The protease was stable at a broad pH range (pH 4-11) with no significant reductions were detected after 24h. Thermodynamic parameters like the enthalpy (ΔH), free energy change (ΔG) and entropy (ΔS) of the protease’s inactivation at the temperature of 55-75C were estimated to be in the range of 80.10-80.27 kJ/mol, 108.34-109.32 kJ/mol and 83.97-85.58 J/mol respectively. The energy of inactivation (Ed) was 82.9 kJ/mol. A. altilis protease (0.125 U) had a comparable fibrinogen clotting capacity with thrombin (0.25 U) during the first 75 min of incubation. 2019-10 Thesis NonPeerReviewed application/pdf en http://eprints.usm.my/55846/1/SITI%20BALQIS24.pdf Zulfigar, Siti Balqis (2019) Extraction, Purification And Characterization Of Artocarpus Altilis Latex Protease As A Fibrino(Geno)lytic Agent. PhD thesis, Universiti Sains Malaysia..
institution Universiti Sains Malaysia
building Hamzah Sendut Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Sains Malaysia
content_source USM Institutional Repository
url_provider http://eprints.usm.my/
language English
topic T1-995 Technology(General)
spellingShingle T1-995 Technology(General)
Zulfigar, Siti Balqis
Extraction, Purification And Characterization Of Artocarpus Altilis Latex Protease As A Fibrino(Geno)lytic Agent
description The harvesting of Artocarpus altilis (breadfruit) in plantations involves the process of draining the latex to avoid staining of the epicarp. The exudate is not fully utilized and it has no commercial value. Ethnopharmacological applications of the latex in wound healing imply its action on blood coagulation and fibrinolysis. Partial purification of A. altilis latex through HiTrapTM SP Sepharose chromatography had purified a 72 kDa protease by 3.1-fold with 24% recovery and the specific activity of 4.87 U/mg. This serine protease was inhibited by phenylmethanesulfonyl fluoride (PMSF) (1 mM and 10 mM) with 89% and 27% of residual activities respectively. The protease showed maximal activity at pH 10 with casein and bovine serum albumin (BSA) as substrates. The protease’s apparent optimal temperature after 30 minutes of incubation was 80C. The Km and Vmax values on casein were 0.453 ± 0.026 mM and 0.022 ± 0.001 μmol/min, respectively. The protease was stable at a broad pH range (pH 4-11) with no significant reductions were detected after 24h. Thermodynamic parameters like the enthalpy (ΔH), free energy change (ΔG) and entropy (ΔS) of the protease’s inactivation at the temperature of 55-75C were estimated to be in the range of 80.10-80.27 kJ/mol, 108.34-109.32 kJ/mol and 83.97-85.58 J/mol respectively. The energy of inactivation (Ed) was 82.9 kJ/mol. A. altilis protease (0.125 U) had a comparable fibrinogen clotting capacity with thrombin (0.25 U) during the first 75 min of incubation.
format Thesis
author Zulfigar, Siti Balqis
author_facet Zulfigar, Siti Balqis
author_sort Zulfigar, Siti Balqis
title Extraction, Purification And Characterization Of Artocarpus Altilis Latex Protease As A Fibrino(Geno)lytic Agent
title_short Extraction, Purification And Characterization Of Artocarpus Altilis Latex Protease As A Fibrino(Geno)lytic Agent
title_full Extraction, Purification And Characterization Of Artocarpus Altilis Latex Protease As A Fibrino(Geno)lytic Agent
title_fullStr Extraction, Purification And Characterization Of Artocarpus Altilis Latex Protease As A Fibrino(Geno)lytic Agent
title_full_unstemmed Extraction, Purification And Characterization Of Artocarpus Altilis Latex Protease As A Fibrino(Geno)lytic Agent
title_sort extraction, purification and characterization of artocarpus altilis latex protease as a fibrino(geno)lytic agent
publishDate 2019
url http://eprints.usm.my/55846/1/SITI%20BALQIS24.pdf
http://eprints.usm.my/55846/
_version_ 1751537283854499840
score 13.211869

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