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dc.contributor.authorHadnađev, M.
dc.contributor.authorDapčević-Hadnađev, T.
dc.contributor.authorLazaridou, A.
dc.contributor.authorMoschakis, T.
dc.contributor.authorMichaelidou, A.M.
dc.contributor.authorPopović, S.
dc.contributor.authorBiliaderis, C.G
dc.dateinfo:eu-repo/date/embargoEnd/2019-06-30
dc.date.accessioned2019-01-23T18:12:22Z
dc.date.available2019-01-23T18:12:22Z
dc.date.issued2018-06-30
dc.identifier.citationHadnađev, 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.2017.12.015en_US
dc.identifier.issn0268-005X
dc.identifier.urihttp://oa.fins.uns.ac.rs/handle/123456789/114
dc.description-en_US
dc.description.abstractProtein 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.sponsorshipThis 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.isoenen_US
dc.publisherELSEVIERen_US
dc.relationinfo:eu-repo/grantAgreement/EC/H2020/692276/eu//
dc.rightsinfo:eu-repo/semantics/embargoedAccess
dc.subjectHemp proteinen_US
dc.subjectalkaline extractionen_US
dc.subjectmicellizationen_US
dc.subjectdenaturationen_US
dc.subjectsolubilityen_US
dc.subjectelectrophoretic mobilityen_US
dc.titleHempseed meal protein isolates prepared by different isolation techniques. Part I. physicochemical propertiesen_US
dc.title.alternative-en_US
dc.typeArticleen_US


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