Purification And Characterization Of Protease From Artocarpus Integer Leaf

The presence of a protease in Artocarpus integer leaves, which can be used as a meat tenderiser, was verified by the presence of a band at 69 kDa, using caseinolytic zymography and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS PAGE). Purification by temperature-phase partitioning w...

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Main Author:	Zulfigar,, Siti Balqis
Format:	Thesis
Language:	English
Published:	2012
Subjects:	T1-995 Technology(General)
Online Access:	http://eprints.usm.my/44895/1/SITI%20BALQIS%20BINTI%20ZULFIGAR.pdf
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id	my-usm-ep.44895
record_format	uketd_dc
spelling	my-usm-ep.448952019-07-05T08:15:58Z Purification And Characterization Of Protease From Artocarpus Integer Leaf 2012-07 Zulfigar,, Siti Balqis T1-995 Technology(General) The presence of a protease in Artocarpus integer leaves, which can be used as a meat tenderiser, was verified by the presence of a band at 69 kDa, using caseinolytic zymography and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS PAGE). Purification by temperature-phase partitioning with 6 % (v/v) Triton X-114, 44 % (w/v) ammonium sulphate precipitation and gel filtration chromatography yielded a preparation with a 12-fold increase in enzyme purity and a final specific activity of 76.67 U/mg. The purified protease was maximally active at 40ºC and at pH 10.0. 2012-07 Thesis http://eprints.usm.my/44895/ http://eprints.usm.my/44895/1/SITI%20BALQIS%20BINTI%20ZULFIGAR.pdf application/pdf en public masters 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 Purification And Characterization Of Protease From Artocarpus Integer Leaf
description	The presence of a protease in Artocarpus integer leaves, which can be used as a meat tenderiser, was verified by the presence of a band at 69 kDa, using caseinolytic zymography and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS PAGE). Purification by temperature-phase partitioning with 6 % (v/v) Triton X-114, 44 % (w/v) ammonium sulphate precipitation and gel filtration chromatography yielded a preparation with a 12-fold increase in enzyme purity and a final specific activity of 76.67 U/mg. The purified protease was maximally active at 40ºC and at pH 10.0.
format	Thesis
qualification_level	Master's degree
author	Zulfigar,, Siti Balqis
author_facet	Zulfigar,, Siti Balqis
author_sort	Zulfigar,, Siti Balqis
title	Purification And Characterization Of Protease From Artocarpus Integer Leaf
title_short	Purification And Characterization Of Protease From Artocarpus Integer Leaf
title_full	Purification And Characterization Of Protease From Artocarpus Integer Leaf
title_fullStr	Purification And Characterization Of Protease From Artocarpus Integer Leaf
title_full_unstemmed	Purification And Characterization Of Protease From Artocarpus Integer Leaf
title_sort	purification and characterization of protease from artocarpus integer leaf
granting_institution	Universiti Sains Malaysia
granting_department	Pusat Pengajian Teknologi Industri
publishDate	2012
url	http://eprints.usm.my/44895/1/SITI%20BALQIS%20BINTI%20ZULFIGAR.pdf
_version_	1747821421433716736

Purification And Characterization Of Protease From Artocarpus Integer Leaf

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