Please use this identifier to cite or link to this item: http://earsiv.odu.edu.tr:8080/xmlui/handle/11489/3470
Title: Sesame seed as an alternative plant protein source: A comprehensive physicochemical characterisation study for alkaline, salt and enzyme-assisted extracted samples
Authors: Koysuren, Begum
Oztop, Mecit Halil
Mazi, BG.
Ordu Üniversitesi
0000-0001-6414-8942
0000-0003-3478-6243
0000-0001-5065-0990
Keywords: RICE BRAN PROTEIN; FUNCTIONAL-PROPERTIES; EMULSIFYING PROPERTIES; IONIC-STRENGTH; WHEY; IDENTIFICATION; SOLUBILITY; ALLERGENS; WATER; OIL
alkaline; salt; enzyme-assisted extraction; SDS-PAGE; sesame seed meal; TD-NMR relaxometry
Issue Date: 2021
Publisher: WILEY HOBOKEN
Citation: Koysuren, B., Oztop, MH., Mazi, BG. (2021). Sesame seed as an alternative plant protein source: A comprehensive physicochemical characterisation study for alkaline, salt and enzyme-assisted extracted samples. International Journal of Food Science and Technology, 56(11), 5471-5484.Doi:10.1111/ijfs.15229
Abstract: Sesame seed is mostly utilised for its oil but also the waste of the oil processing; the seed meal has also significant potential to be used as an alternative protein source. In this study, the goal is to produce sesame seed protein by using three different techniques; alkaline, salt and enzyme-assisted extraction. A comprehensive physicochemical characterisation of the extracts was performed. Total and soluble protein contents, emulsification activity & emulsion stability, FTIR spectroscopy, hydration behaviour and gelling ability experiments by TD-NMR were conducted for all extracted proteins. Also, SDS-PAGE experiments were performed to observe the effect of extraction conditions on protein folding. Overall, the aqueous phase of enzyme-assisted extracted proteins (E-ACP) had the highest protein content and solubility, which resulted in other improved physicochemical properties. Salt extracted samples were 'salted-out', therefore, had poor physicochemical properties. TD-NMR experiments further confirmed the solubility and gelling ability results by measuring the change in the T-2 spin relaxation times. Additionally, FTIR spectroscopy confirmed the most critical peaks for the proteins; Amide I (C=O stretching) and Amide II (N-H bending). In summary, depending on the physicochemical property of interest, different extraction methods yielded proteins with different properties.
Description: WoS Categories : Food Science & Technology Web of Science Index : Science Citation Index Expanded (SCI-EXPANDED) Research Areas : Food Science & Technology
URI: http://dx.doi.org/10.1111/ijfs.15229
https://www.webofscience.com/wos/woscc/full-record/WOS:000673995800001
http://earsiv.odu.edu.tr:8080/xmlui/handle/11489/3470
ISBN: 0950-5423
1365-2621
Appears in Collections:Gıda Mühendisliği

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