Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis

Lipase from a newly isolated strain of Rhizopus rhizopodifonnis was partially purified and characterized. By acetone fractionation, the enzyme was purified to about 2.8 fold, with 62.5% recovery and with specific activity of 3.2 U/mg. By gel filtration through Sephadex G-100, the enzyme was further...

Full description

Bibliographic Details
Main Authors: Salleh, Abu Bakar, Abdul Razak, Che Nyonya, Abd Samad, Mohd Yusoff, Ampon, Kamaruzaman, Wan Yunus, Wan Md. Zin, Basri, Mahiran
Format: Article
Language:English
Published: Penerbit Universiti Kebangsaan Malaysia 1996
Online Access:http://psasir.upm.edu.my/id/eprint/22573/
http://psasir.upm.edu.my/id/eprint/22573/1/Partial%20purification%20and%20characterization%20of%20lipases%20from%20thermophilic%20Rhizopus%20rhizopodiformis.pdf
_version_ 1848844521475932160
author Salleh, Abu Bakar
Abdul Razak, Che Nyonya
Abd Samad, Mohd Yusoff
Ampon, Kamaruzaman
Wan Yunus, Wan Md. Zin
Basri, Mahiran
author_facet Salleh, Abu Bakar
Abdul Razak, Che Nyonya
Abd Samad, Mohd Yusoff
Ampon, Kamaruzaman
Wan Yunus, Wan Md. Zin
Basri, Mahiran
author_sort Salleh, Abu Bakar
building UPM Institutional Repository
collection Online Access
description Lipase from a newly isolated strain of Rhizopus rhizopodifonnis was partially purified and characterized. By acetone fractionation, the enzyme was purified to about 2.8 fold, with 62.5% recovery and with specific activity of 3.2 U/mg. By gel filtration through Sephadex G-100, the enzyme was further purified to 9.7 fold and had a specific activity of 11.1 U/mg. By polyacrylamide gel electrophoresis, five protein bands were observed after acetone fractionation, white two protein bands were observed after the preparation was passed through Sephadex G-100. It has a pH optimum at 6.0 and a temperature optimum at 45°C. The enzyme is most stable at pH 7.0 and temperature of 50°C. The enzyme has a preference for short chain triglycerides and can also hydrolyse some methyl esters. The lipase is specific for 1,3 positions.
first_indexed 2025-11-15T08:32:15Z
format Article
id upm-22573
institution Universiti Putra Malaysia
institution_category Local University
language English
last_indexed 2025-11-15T08:32:15Z
publishDate 1996
publisher Penerbit Universiti Kebangsaan Malaysia
recordtype eprints
repository_type Digital Repository
spelling upm-225732016-02-02T04:03:43Z http://psasir.upm.edu.my/id/eprint/22573/ Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis Salleh, Abu Bakar Abdul Razak, Che Nyonya Abd Samad, Mohd Yusoff Ampon, Kamaruzaman Wan Yunus, Wan Md. Zin Basri, Mahiran Lipase from a newly isolated strain of Rhizopus rhizopodifonnis was partially purified and characterized. By acetone fractionation, the enzyme was purified to about 2.8 fold, with 62.5% recovery and with specific activity of 3.2 U/mg. By gel filtration through Sephadex G-100, the enzyme was further purified to 9.7 fold and had a specific activity of 11.1 U/mg. By polyacrylamide gel electrophoresis, five protein bands were observed after acetone fractionation, white two protein bands were observed after the preparation was passed through Sephadex G-100. It has a pH optimum at 6.0 and a temperature optimum at 45°C. The enzyme is most stable at pH 7.0 and temperature of 50°C. The enzyme has a preference for short chain triglycerides and can also hydrolyse some methyl esters. The lipase is specific for 1,3 positions. Penerbit Universiti Kebangsaan Malaysia 1996 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/22573/1/Partial%20purification%20and%20characterization%20of%20lipases%20from%20thermophilic%20Rhizopus%20rhizopodiformis.pdf Salleh, Abu Bakar and Abdul Razak, Che Nyonya and Abd Samad, Mohd Yusoff and Ampon, Kamaruzaman and Wan Yunus, Wan Md. Zin and Basri, Mahiran (1996) Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis. Sains Malaysiana, 25 (4). pp. 131-141. ISSN 0126-6039 http://www.ukm.my/jsm/english_journals/vol25num4_1996/vol25num4_96page131-141.html
spellingShingle Salleh, Abu Bakar
Abdul Razak, Che Nyonya
Abd Samad, Mohd Yusoff
Ampon, Kamaruzaman
Wan Yunus, Wan Md. Zin
Basri, Mahiran
Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis
title Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis
title_full Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis
title_fullStr Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis
title_full_unstemmed Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis
title_short Partial purification and characterization of lipases from thermophilic Rhizopus rhizopodiformis
title_sort partial purification and characterization of lipases from thermophilic rhizopus rhizopodiformis
url http://psasir.upm.edu.my/id/eprint/22573/
http://psasir.upm.edu.my/id/eprint/22573/
http://psasir.upm.edu.my/id/eprint/22573/1/Partial%20purification%20and%20characterization%20of%20lipases%20from%20thermophilic%20Rhizopus%20rhizopodiformis.pdf