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Hempseed meal protein isolates prepared by different isolation techniques. Part I. physicochemical properties

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dc.contributor.author Hadnađev, Miroslav
dc.contributor.author Dapčević-Hadnađev, Tamara
dc.contributor.author Lazaridou, A.
dc.contributor.author Moschakis, T.
dc.contributor.author Michaelidou, A.M.
dc.contributor.author Popović, Sanja
dc.contributor.author Biliaderis, C.G
dc.date info:eu-repo/date/embargoEnd/2019-06-30
dc.date.accessioned 2019-01-23T18:12:22Z
dc.date.available 2019-01-23T18:12:22Z
dc.date.issued 2018-06-30
dc.identifier.citation Hadnađev, M., Dapčević-Hadnađev, T., Lazaridou, A., Moschakis, T., Michaelidou, A. M., Popović, S., & Biliaderis, C. G. (2018) Hempseed meal protein isolates prepared by different isolation techniques. Part I. Physicochemical properties. Food Hydrocolloids, 79, 526-533. DOI: https://doi.org/10.1016/j.foodhyd.2017.12.015 en_US
dc.identifier.issn 0268-005X
dc.identifier.uri http://oa.fins.uns.ac.rs/handle/123456789/114
dc.description - en_US
dc.description.abstract Protein isolates from hemp seed meal were prepared using alkaline extraction/isoelectric precipitation (HPI) and micellization (HMI) procedures and compared in terms of their physicochemical properties and functionality. The micellization technique resulted in lower protein recovery than the isoelectric precipitation technique. Both HPI and HMI proteins had protein contents higher than 90%. The HMI protein powders were lighter in colour than the corresponding HPI isolates due to higher content of co-extracted polyphenols for the latter. The electrophoretic mobility and subunit composition, as well as amino acid composition of the isolates were not affected by the extraction procedure, indicative of similar protein composition. The HPI exhibited minimum protein solubility at pH 5.0, while for HMI it was shifted to pH 6.0. Differential scanning calorimetry indicated that highly alkaline conditions during HPI extraction led to partial protein denaturation which is reflected in lower transition enthalpy of HPI than HMI. FTIR spectra have also confirmed changes in HPI protein secondary structure, i.e. lower intensity of the peak (1634 cm−1) corresponding to native protein structural elements such as intramolecular β-sheets and higher intensities of peaks (1618 cm−1, 1683 cm−1 and 1694 cm−1) indicating enhanced protein aggregation compared to HMI. Protein conformational changes during alkali extraction resulted in higher water retention capacities of HPI in comparison to HMI. en_US
dc.description.sponsorship This research is a part of the project funded by Provincial Secretariat for Higher Education and Scientific Research [Project No. 142-451-2516/2017-01/02]. The results of this research represent experimental work of the postdoctoral study of Tamara Dapčević Hadnađev and Miroslav Hadnađev performed at the Department of Food Science and Technology, Aristotle University of Thessaloniki under the supervision of professor Costas G. Biliaderis. Financial assistance for the postdoctoral fellowships was provided by the Ministry of Education, Science and Technological Development, Republic of Serbia. en_US
dc.language.iso en en_US
dc.publisher ELSEVIER en_US
dc.relation info:eu-repo/grantAgreement/EC/H2020/692276/eu//
dc.rights info:eu-repo/semantics/embargoedAccess
dc.subject Hemp protein en_US
dc.subject alkaline extraction en_US
dc.subject micellization en_US
dc.subject denaturation en_US
dc.subject solubility en_US
dc.subject electrophoretic mobility en_US
dc.title Hempseed meal protein isolates prepared by different isolation techniques. Part I. physicochemical properties en_US
dc.title.alternative - en_US
dc.type Article en_US


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