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...

Full description

Bibliographic Details
Main Author: Zulfigar,, Siti Balqis
Format: Thesis
Language:English
Published: 2012
Subjects:
Online Access:http://eprints.usm.my/44895/
http://eprints.usm.my/44895/1/SITI%20BALQIS%20BINTI%20ZULFIGAR.pdf
_version_ 1848880183683055616
author Zulfigar,, Siti Balqis
author_facet Zulfigar,, Siti Balqis
author_sort Zulfigar,, Siti Balqis
building USM Institutional Repository
collection Online Access
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.
first_indexed 2025-11-15T17:59:05Z
format Thesis
id usm-44895
institution Universiti Sains Malaysia
institution_category Local University
language English
last_indexed 2025-11-15T17:59:05Z
publishDate 2012
recordtype eprints
repository_type Digital Repository
spelling usm-448952019-07-05T08:15:58Z http://eprints.usm.my/44895/ Purification And Characterization Of Protease From Artocarpus Integer Leaf 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 NonPeerReviewed application/pdf en http://eprints.usm.my/44895/1/SITI%20BALQIS%20BINTI%20ZULFIGAR.pdf Zulfigar,, Siti Balqis (2012) Purification And Characterization Of Protease From Artocarpus Integer Leaf. Masters thesis, Universiti Sains Malaysia.
spellingShingle T1-995 Technology(General)
Zulfigar,, Siti Balqis
Purification And Characterization Of Protease From Artocarpus Integer Leaf
title 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_short Purification And Characterization Of Protease From Artocarpus Integer Leaf
title_sort purification and characterization of protease from artocarpus integer leaf
topic T1-995 Technology(General)
url http://eprints.usm.my/44895/
http://eprints.usm.my/44895/1/SITI%20BALQIS%20BINTI%20ZULFIGAR.pdf