Functional Properties of Sweet Lupin Protein Isolated and Tested at Various pH Levels

Lupin has the potential to be a new source of vegetable protein due to its similar protein content to soy, the common source of vegetable protein used in the food industry. Investigation of its functional properties is essential to validate the potential application in the food industry. Lupin prote...

Full description

Bibliographic Details
Main Authors: Jayasena, Vijay, Chih, Hui Jun, Nasar-Abbas, Syed
Format: Journal Article
Published: American-Eurasian Network for Scientific Information 2010
Subjects:
Online Access:http://hdl.handle.net/20.500.11937/19417
_version_ 1848750027655086080
author Jayasena, Vijay
Chih, Hui Jun
Nasar-Abbas, Syed
author_facet Jayasena, Vijay
Chih, Hui Jun
Nasar-Abbas, Syed
author_sort Jayasena, Vijay
building Curtin Institutional Repository
collection Online Access
description Lupin has the potential to be a new source of vegetable protein due to its similar protein content to soy, the common source of vegetable protein used in the food industry. Investigation of its functional properties is essential to validate the potential application in the food industry. Lupin protein isolates were prepared by alkaline extraction at pH 9.0 followed by acidic precipitation at eight different pH levels i.e. 4.0, 4.2, 4.4, 4.5, 4.6, 4.8, 5.0 and 5.5. The range of pH employed here covered the isoelectric points of major legume proteins. The emulsifying and foaming properties of lupin protein isolate (LPI) samples were evaluated and compared with those of soy protein isolate (SPI). Lupin protein isolates prepared by precipitating at a pH range of 4.4 to 5.0 had no significant difference in their emulsifying and foaming properties. Emulsifying activity and emulsion stability of LPI samples were comparable to those of SPI. All LPI samples exhibited greater emulsifying activity and emulsion stability than SPI at pH 4.0. Foaming capacity and foam stability of LPI tested at a range of pH levels was also higher than that of SPI. The study provides a base for more flexible and economical process for making LPI at commercial level.
first_indexed 2025-11-14T07:30:18Z
format Journal Article
id curtin-20.500.11937-19417
institution Curtin University Malaysia
institution_category Local University
last_indexed 2025-11-14T07:30:18Z
publishDate 2010
publisher American-Eurasian Network for Scientific Information
recordtype eprints
repository_type Digital Repository
spelling curtin-20.500.11937-194172017-01-30T12:13:44Z Functional Properties of Sweet Lupin Protein Isolated and Tested at Various pH Levels Jayasena, Vijay Chih, Hui Jun Nasar-Abbas, Syed Lupinus angustifolius lupin functional properties protein isolates Lupin has the potential to be a new source of vegetable protein due to its similar protein content to soy, the common source of vegetable protein used in the food industry. Investigation of its functional properties is essential to validate the potential application in the food industry. Lupin protein isolates were prepared by alkaline extraction at pH 9.0 followed by acidic precipitation at eight different pH levels i.e. 4.0, 4.2, 4.4, 4.5, 4.6, 4.8, 5.0 and 5.5. The range of pH employed here covered the isoelectric points of major legume proteins. The emulsifying and foaming properties of lupin protein isolate (LPI) samples were evaluated and compared with those of soy protein isolate (SPI). Lupin protein isolates prepared by precipitating at a pH range of 4.4 to 5.0 had no significant difference in their emulsifying and foaming properties. Emulsifying activity and emulsion stability of LPI samples were comparable to those of SPI. All LPI samples exhibited greater emulsifying activity and emulsion stability than SPI at pH 4.0. Foaming capacity and foam stability of LPI tested at a range of pH levels was also higher than that of SPI. The study provides a base for more flexible and economical process for making LPI at commercial level. 2010 Journal Article http://hdl.handle.net/20.500.11937/19417 American-Eurasian Network for Scientific Information fulltext
spellingShingle Lupinus angustifolius
lupin
functional properties
protein isolates
Jayasena, Vijay
Chih, Hui Jun
Nasar-Abbas, Syed
Functional Properties of Sweet Lupin Protein Isolated and Tested at Various pH Levels
title Functional Properties of Sweet Lupin Protein Isolated and Tested at Various pH Levels
title_full Functional Properties of Sweet Lupin Protein Isolated and Tested at Various pH Levels
title_fullStr Functional Properties of Sweet Lupin Protein Isolated and Tested at Various pH Levels
title_full_unstemmed Functional Properties of Sweet Lupin Protein Isolated and Tested at Various pH Levels
title_short Functional Properties of Sweet Lupin Protein Isolated and Tested at Various pH Levels
title_sort functional properties of sweet lupin protein isolated and tested at various ph levels
topic Lupinus angustifolius
lupin
functional properties
protein isolates
url http://hdl.handle.net/20.500.11937/19417