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Guava seed storage protein: Fractionation and characterization
In the present work, guava seed storage proteins have been fractionated and characterized. Glutelins (86–90 g/100 g) and globulins (≈10 g/100 g) are the main components of the protein extract. Albumins and prolamins are minor components (≈2 g/100 g). Guava seed glutelin extracts, like rice and amara...
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Published in: | Food science & technology 2006-01, Vol.39 (8), p.902-910 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | In the present work, guava seed storage proteins have been fractionated and characterized. Glutelins (86–90
g/100
g) and globulins (≈10
g/100
g) are the main components of the protein extract. Albumins and prolamins are minor components (≈2
g/100
g). Guava seed glutelin extracts, like rice and amaranth glutelins, are legumine-like proteins that, due to their solubility properties, have to be extracted using extreme pH (borate buffer, pH 10, Gt-Bo; NaOH pH 12 Gt-Na), denaturing (borate buffer plus sodium dodecyl sulfate, Gt-BoSDS) or reducing conditions (borate buffer plus 2-mercaptoethanol, Gt-BoME; borate buffer plus sodium dodecyl sulfate and 2-mercaptoethanol, Gt-BoSDSME). The highest yield was obtained with SDS extraction, suggesting that proteins in the seeds form aggregates stabilized mainly by non-covalent interactions. Glutelins are mainly composed of 65 and 67
kD subunits, with a lower proportion of 55
kD subunits. These subunits are formed by disulfide bond-linked polypeptides with molecular masses 40–45
kD, 22–27
kD and 23–25
kD, respectively. The guava seeds protein isolate (GSI) exhibited a polypeptide profile very similar to that of the glutelin fraction.
The guava seed could be an alternative source of protein for human and animal consume, additional to this to solve at least in part the pollution problem that fruit processing industry has for discarding this material. |
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ISSN: | 0023-6438 1096-1127 |
DOI: | 10.1016/j.lwt.2005.06.006 |