Physiochemical properties and specificity of mycelium-bound lipase from a locally isolated strain of Aspergillus flavus link

The properties of mycelium-bound lipase of Aspergillus flavus Link obtained after 3 days growth in palm olein were studied. The mycelium-bound lipase has an optimum activity at a temperature range of 50–55°C and once extracted, the activity was optimum at a temperature range of 25–35 °C. The extract...

Full description

Saved in:
Bibliographic Details
Main Authors: Long, Kamariah, Mohd Ghazali, Hasanah, Ariff, Arbakariya, Bucke, Christopher
Format: Article
Language:English
Published: Malaysian Agricultural Research and Development Institute (MARDI) 2000
Online Access:http://psasir.upm.edu.my/id/eprint/36849/1/Physiochemical%20properties%20and%20specificity%20of%20mycelium-bound%20lipase%20from%20a%20locally%20isolated%20strain%20of%20Aspergillus%20flavus%20Link.pdf
http://psasir.upm.edu.my/id/eprint/36849/
http://ejtafs.mardi.gov.my/index.php/publication/issues/archive/87-2000/volume-28-no2/593-280210
Tags: Add Tag
No Tags, Be the first to tag this record!
id my.upm.eprints.36849
record_format eprints
spelling my.upm.eprints.368492016-05-17T06:56:14Z http://psasir.upm.edu.my/id/eprint/36849/ Physiochemical properties and specificity of mycelium-bound lipase from a locally isolated strain of Aspergillus flavus link Long, Kamariah Mohd Ghazali, Hasanah Ariff, Arbakariya Bucke, Christopher The properties of mycelium-bound lipase of Aspergillus flavus Link obtained after 3 days growth in palm olein were studied. The mycelium-bound lipase has an optimum activity at a temperature range of 50–55°C and once extracted, the activity was optimum at a temperature range of 25–35 °C. The extracted lipase was stable at alkaline pH and heat labile, thus lost 14% of its activity after being exposed to 30°C for 4 h. Ca2+ enhanced the lipase activity while EDTA (1 mM) had no effect. The enzyme hydrolysed coconut oil faster than other vegetable oils and tributyrin was not hydrolysed by the extracted lipase. The apparent Km values obtained for mycelium-bound lipase (11.76 mg/mL) was three times higher than the extracted lipase (3.92 mg/mL) suggesting that there was a diffusion limitation of the substrate in reaching the bound lipase. The extracted lipase displayed 1,3 positional specificity. Malaysian Agricultural Research and Development Institute (MARDI) 2000 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/36849/1/Physiochemical%20properties%20and%20specificity%20of%20mycelium-bound%20lipase%20from%20a%20locally%20isolated%20strain%20of%20Aspergillus%20flavus%20Link.pdf Long, Kamariah and Mohd Ghazali, Hasanah and Ariff, Arbakariya and Bucke, Christopher (2000) Physiochemical properties and specificity of mycelium-bound lipase from a locally isolated strain of Aspergillus flavus link. Journal of Tropical Agriculture and Food Science, 28 (2). pp. 135-142. ISSN 1394-9829; ESSN: 2289-9650 http://ejtafs.mardi.gov.my/index.php/publication/issues/archive/87-2000/volume-28-no2/593-280210
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
description The properties of mycelium-bound lipase of Aspergillus flavus Link obtained after 3 days growth in palm olein were studied. The mycelium-bound lipase has an optimum activity at a temperature range of 50–55°C and once extracted, the activity was optimum at a temperature range of 25–35 °C. The extracted lipase was stable at alkaline pH and heat labile, thus lost 14% of its activity after being exposed to 30°C for 4 h. Ca2+ enhanced the lipase activity while EDTA (1 mM) had no effect. The enzyme hydrolysed coconut oil faster than other vegetable oils and tributyrin was not hydrolysed by the extracted lipase. The apparent Km values obtained for mycelium-bound lipase (11.76 mg/mL) was three times higher than the extracted lipase (3.92 mg/mL) suggesting that there was a diffusion limitation of the substrate in reaching the bound lipase. The extracted lipase displayed 1,3 positional specificity.
format Article
author Long, Kamariah
Mohd Ghazali, Hasanah
Ariff, Arbakariya
Bucke, Christopher
spellingShingle Long, Kamariah
Mohd Ghazali, Hasanah
Ariff, Arbakariya
Bucke, Christopher
Physiochemical properties and specificity of mycelium-bound lipase from a locally isolated strain of Aspergillus flavus link
author_facet Long, Kamariah
Mohd Ghazali, Hasanah
Ariff, Arbakariya
Bucke, Christopher
author_sort Long, Kamariah
title Physiochemical properties and specificity of mycelium-bound lipase from a locally isolated strain of Aspergillus flavus link
title_short Physiochemical properties and specificity of mycelium-bound lipase from a locally isolated strain of Aspergillus flavus link
title_full Physiochemical properties and specificity of mycelium-bound lipase from a locally isolated strain of Aspergillus flavus link
title_fullStr Physiochemical properties and specificity of mycelium-bound lipase from a locally isolated strain of Aspergillus flavus link
title_full_unstemmed Physiochemical properties and specificity of mycelium-bound lipase from a locally isolated strain of Aspergillus flavus link
title_sort physiochemical properties and specificity of mycelium-bound lipase from a locally isolated strain of aspergillus flavus link
publisher Malaysian Agricultural Research and Development Institute (MARDI)
publishDate 2000
url http://psasir.upm.edu.my/id/eprint/36849/1/Physiochemical%20properties%20and%20specificity%20of%20mycelium-bound%20lipase%20from%20a%20locally%20isolated%20strain%20of%20Aspergillus%20flavus%20Link.pdf
http://psasir.upm.edu.my/id/eprint/36849/
http://ejtafs.mardi.gov.my/index.php/publication/issues/archive/87-2000/volume-28-no2/593-280210
_version_ 1643831846695337984
score 13.211869