getpdf
   


Pepsin-Assisted Transglutaminase Modification of Functional Properties of a Protein Isolate
Obtained from Industrial Sunflower Meal



Petya Ivanova1small orcid_display_4pp, Vesela I. Chalova1*small orcid_display_4pp, Hristo Kalaydzhiev1small orcid_display_4pp, Mariana Perifanova-Nemska2small orcid_display_4pp, Turid Rustad3small orcid_display_4pp
and Lidia Koleva1small orcid_display_4pp



1University of Food Technologies, Department of Biochemistry and Molecular Biology, 26 Maritsa Bulv., BG-4002 Plovdiv,
  Bulgaria
2University of Food Technologies, Department of Technology of Tobacco, Sugar, Vegetable and Essential Oils, 26 Maritsa
  Bulv., BG-4002 Plovdiv, Bulgaria
3Norwegian University of Science and Technology, Department of Biotechnology and Food Science, Sem Salandsvei 6/8,
  NO-7491 Trondheim, Norway



Article history:
Received: November 15, 2016
Accepted: May 4, 2017



Key words:
industrial sunflower meal, pepsin, protein hydrolysates, transglutaminase modification, functional properties



Summary:
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-modified 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-modified 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.



*Corresponding author:  tel3  +359 32 603 855
                                           fax2  +359 32 644 102
                                            email3  This e-mail address is being protected from spambots. You need JavaScript enabled to view it.

We use cookies to improve our website and your experience when using it. Cookies used for the essential operation of the site have already been set. To find out more about the cookies we use and how to delete them, see our privacy policy.

I accept cookies from this site.

EU Cookie Directive Module Information