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

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
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id	my-usm-ep.55846
record_format	uketd_dc
spelling	my-usm-ep.558462022-11-30T17:33:16Z Extraction, Purification And Characterization Of Artocarpus Altilis Latex Protease As A Fibrino(Geno)lytic Agent 2019-10 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 http://eprints.usm.my/55846/ http://eprints.usm.my/55846/1/SITI%20BALQIS24.pdf application/pdf en public phd doctoral Universiti Sains Malaysia. Pusat Pengajian Teknologi Industri
institution	Universiti Sains Malaysia
collection	USM Institutional Repository
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
qualification_name	Doctor of Philosophy (PhD.)
qualification_level	Doctorate
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
granting_institution	Universiti Sains Malaysia.
granting_department	Pusat Pengajian Teknologi Industri
publishDate	2019
url	http://eprints.usm.my/55846/1/SITI%20BALQIS24.pdf
_version_	1776101118813667328

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

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