Evidence map›Paper›PMID 29089856›Full record

ArticleFood technology and biotechnology2017

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

Petya Ivanova, Vesela I Chalova, Hristo Kalaydzhiev, Mariana Perifanova-Nemska, Turid Rustad, Lidia Koleva

Open access · diamondAbstract read
In one paragraph

Article in Food technology and biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.6field-weighted citation impact, top 27% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 5 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Petya IvanovaUniversity of Food Technologies, Department of Biochemistry and Molecular Biology, 
26 Maritsa Bulv., BG-4002 Plovdiv, Bulgaria.ORCID 0000-0001-6790-0298
Vesela I ChalovaUniversity of Food Technologies, Department of Biochemistry and Molecular Biology, 
26 Maritsa Bulv., BG-4002 Plovdiv, Bulgaria.ORCID 0000-0001-5139-5389
Hristo KalaydzhievUniversity of Food Technologies, Department of Biochemistry and Molecular Biology, 
26 Maritsa Bulv., BG-4002 Plovdiv, Bulgaria.ORCID 0000-0002-3589-4134
Mariana Perifanova-NemskaUniversity of Food Technologies, Department of Technology of Tobacco, Sugar, 
Vegetable and Essential Oils, 26 Maritsa Bulv., BG-4002 Plovdiv, Bulgaria.ORCID 0000-0002-5763-3891
Turid RustadNorwegian University of Science and Technology, Department of Biotechnology and Food Science, 
Sem Sælandsvei 6/8, NO-7491 Trondheim, Norway.ORCID 0000-0002-8972-6347
Lidia KolevaUniversity of Food Technologies, Department of Biochemistry and Molecular Biology, 
26 Maritsa Bulv., BG-4002 Plovdiv, Bulgaria.ORCID 0000-0002-7368-9908
University of Food Technologies · BGNorwegian University of Science and Technology · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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-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.

Indexed as

functional propertiesindustrial sunflower mealpepsinprotein hydrolysatestransglutaminase modification

Identifiers

PMID29089856
PMCPMC5654420
OpenAlexW2613251215

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.