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

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...

Full description

Saved in:
Bibliographic Details
Published in:Food technology and biotechnology 2017-07, Vol.55 (3), p.420-428
Main Authors: Ivanova, Petya, Chalova, Vesela I, Kalaydzhiev, Hristo, Perifanova-Nemska, Mariana, Rustad, Turid, Koleva, Lidia
Format: Article
Language:English
Subjects:
Agricultural land
Dairy industry
Dietary supplements
Food
Food industry
Food processing industry
Food production
functional properties
Human nutrition
Hydrogen ions
Hydrolysates
Hydrolysis
industrial sunflower meal
Nutrition
Nutritional aspects
Pepsin
Petroleum production
pH effects
Physiological aspects
Protein hydrolysates
Proteins
Scientific Notes
Seeds
Solubility
Sunflower seeds
Thermal stability
transglutaminase modification
Vegetable oils
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
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 pH7. Significant improvement of foam making capacity (p
ISSN:1330-9862
1334-2606
DOI:10.17113/ftb.55.03.17.5061