dc.contributor.author | Ivanova, Petya | |
dc.contributor.author | Chalova, Vesela | |
dc.contributor.author | Kalaydzhiev, Hristo | |
dc.contributor.author | Perifanova-Nemska, Mariana | |
dc.contributor.author | Rustad, Turid | |
dc.contributor.author | Koleva, Lidia | |
dc.date.accessioned | 2018-06-20T08:34:06Z | |
dc.date.available | 2018-06-20T08:34:06Z | |
dc.date.created | 2017-09-21T11:40:08Z | |
dc.date.issued | 2017 | |
dc.identifier.citation | Food technology and biotechnology. 2017, 55 (3), 420-428. | nb_NO |
dc.identifier.issn | 1330-9862 | |
dc.identifier.uri | http://hdl.handle.net/11250/2502229 | |
dc.description.abstract | The utilization of industrial sunflower meal to produce protein-rich products for the food industry is an alternative approach for better and more efficient use of this agricultural by-product. Sunflower meal proteins possess specific functional properties, which however need improvement to broaden their potential as supplements for delivering high-quality products for human nutrition. The aim of the study is to evaluate the combined influence of low-degree pepsin hydrolysis and transglutaminase (TG) modification on industrial sunflower meal protein isolate functionality at pH=2 to 10. Three TG-modified pepsin hydrolysates with the degree of hydrolysis of 0.48, 0.71 and 1.72 % were produced and named TG-PH1, TG-PH2 and TG-PH3, respectively. All three TG-modifi ed pepsin hydrolysates exhibited improved solubility at pH between 3.5 and 5.5 as the highest was observed of TG-PH3 at protein isoelectric point (pI=4.5). Sunflower meal protein isolate and TG-modified sunflower meal protein isolate had greater solubility than the three TG-modified hydrolysates at pH<3 and >7. Significant improvement of foam making capacity (p<0.05) was achieved with all three TG-modifi ed pepsin hydrolysates in the entire pH area studied. Pepsin hydrolysis of the protein isolate with the three degrees of hydrolysis did not improve foam stability. Improved thermal stability was observed with TG-PH3 up to 80 °C compared to the protein isolate (pH=7). At 90 °C, TG modification of the protein isolate alone resulted in the highest thermal stability. Pepsin hydrolysis followed by a treatment with TG could be used to produce sunflower protein isolates with improved solubility, foam making capacity and thermal stability for use in the food industry. | nb_NO |
dc.language.iso | eng | nb_NO |
dc.publisher | University of Zagreb, Faculty of Food Technology and Biotechnology, Croatia | nb_NO |
dc.rights | Navngivelse-Ikkekommersiell 4.0 Internasjonal | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc/4.0/deed.no | * |
dc.title | Pepsin-Assisted Transglutaminase Modification of Functional Properties of a Protein Isolate Obtained from Industrial Sunflower Meal | nb_NO |
dc.type | Journal article | nb_NO |
dc.type | Peer reviewed | nb_NO |
dc.description.version | publishedVersion | nb_NO |
dc.source.pagenumber | 420-428 | nb_NO |
dc.source.volume | 55 | nb_NO |
dc.source.journal | Food technology and biotechnology | nb_NO |
dc.source.issue | 3 | nb_NO |
dc.identifier.doi | 10.17113/ftb.55.03.17.5061 | |
dc.identifier.cristin | 1496375 | |
dc.description.localcode | © The Author(s). 2017 Food Technology and Biotechnology applies the Creative Commons Attribution Non-Commercial 4.0 CC BY-NC license to all published papers, which permits use, distribution, reproduction and archiving in any medium, provided the original work is properly cited and is not used for commercial purposes. Copyright of published papers is retained by the authors, who grant the Faculty of Food Technology and Biotechnology, University of Zagreb, Croatia, a license to publish the manuscript as the original publisher. Authors also grant any third party the right to use the article freely and for non-commercial purposes, as long as its integrity is maintained and its original authors, citation details and publisher are clearly stated. | nb_NO |
cristin.unitcode | 194,66,15,0 | |
cristin.unitname | Institutt for bioteknologi og matvitenskap | |
cristin.ispublished | true | |
cristin.fulltext | original | |
cristin.qualitycode | 1 | |