Efficient isolation of lupin protein

The increasing demand for low cost and non-genetically modified vegetable proteins has pushed the food industry to explore alternate sources of protein. Lupin has been found to have similar protein content and amino acid profile to that of soy. In particular, the Australian Sweet Lupin (Lupinus angu...

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Main Authors: Jayasena, Vijay, Chih, Hui Jun, Nasar-Abbas, Syed
Format: Journal Article
Published: Australian Institute of Food Science and Technology Inc. 2011
Subjects:
Online Access:http://www.aifst.asn.au/
http://hdl.handle.net/20.500.11937/22645
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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 The increasing demand for low cost and non-genetically modified vegetable proteins has pushed the food industry to explore alternate sources of protein. Lupin has been found to have similar protein content and amino acid profile to that of soy. In particular, the Australian Sweet Lupin (Lupinus angustifolius), a low alkaloid variety of lupin, is high in protein and fibre and low in fat, making it an ideal food ingredient for health and well being. Concentrated form of lupin protein with protein content of 90% was prepared by alkaline extraction at pH 9.0 followed by acidic precipitation at eight different pH levels (4.0, 4.2, 4.4, 4.5, 4.6, 4.8, 5.0 and 5.5). The range of pH employed covered the isoelectric points of major legume proteins. The results revealed that there was no significant difference in protein content and yield of lupin protein isolates precipitated at pH 4.4, 4.5, 4.6, 4.8 and 5.0. The finding indicated that instead of using pH 4.5 for lupin protein precipitation, a higher pH such as 5.0 can be used that would result in decreased acid usage, thus providing a more economical approach to protein isolate production.
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format Journal Article
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institution Curtin University Malaysia
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publishDate 2011
publisher Australian Institute of Food Science and Technology Inc.
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spelling curtin-20.500.11937-226452019-03-28T07:42:35Z Efficient isolation of lupin protein Jayasena, Vijay Chih, Hui Jun Nasar-Abbas, Syed chemical properties protein isolates recovery The increasing demand for low cost and non-genetically modified vegetable proteins has pushed the food industry to explore alternate sources of protein. Lupin has been found to have similar protein content and amino acid profile to that of soy. In particular, the Australian Sweet Lupin (Lupinus angustifolius), a low alkaloid variety of lupin, is high in protein and fibre and low in fat, making it an ideal food ingredient for health and well being. Concentrated form of lupin protein with protein content of 90% was prepared by alkaline extraction at pH 9.0 followed by acidic precipitation at eight different pH levels (4.0, 4.2, 4.4, 4.5, 4.6, 4.8, 5.0 and 5.5). The range of pH employed covered the isoelectric points of major legume proteins. The results revealed that there was no significant difference in protein content and yield of lupin protein isolates precipitated at pH 4.4, 4.5, 4.6, 4.8 and 5.0. The finding indicated that instead of using pH 4.5 for lupin protein precipitation, a higher pH such as 5.0 can be used that would result in decreased acid usage, thus providing a more economical approach to protein isolate production. 2011 Journal Article http://hdl.handle.net/20.500.11937/22645 http://www.aifst.asn.au/ Australian Institute of Food Science and Technology Inc. fulltext
spellingShingle chemical properties
protein isolates
recovery
Jayasena, Vijay
Chih, Hui Jun
Nasar-Abbas, Syed
Efficient isolation of lupin protein
title Efficient isolation of lupin protein
title_full Efficient isolation of lupin protein
title_fullStr Efficient isolation of lupin protein
title_full_unstemmed Efficient isolation of lupin protein
title_short Efficient isolation of lupin protein
title_sort efficient isolation of lupin protein
topic chemical properties
protein isolates
recovery
url http://www.aifst.asn.au/
http://hdl.handle.net/20.500.11937/22645