Evidence map›Paper›PMID 39693694›Full record

ArticleUltrasonics sonochemistry2025

Ultrasound-assisted modification of oat protein isolates: Structural and functional enhancements.

Hamad Rafique, Pai Peng, Xinzhong Hu, Kanza Saeed, Muhammad Zubair Khalid, Waseem Khalid, Sonia Morya, Tawfiq Alsulami, Robert Mugabi, Gulzar Ahmad Nayik

Abstract read
In one paragraph

Article in Ultrasonics sonochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

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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

10 authors.

Hamad RafiqueCollege of Food Engineering and Nutritional Science, Shaanxi Normal University, Xi'an, Shaanxi 710119, China.
Pai PengCollege of Food Engineering and Nutritional Science, Shaanxi Normal University, Xi'an, Shaanxi 710119, China.
Xinzhong HuCollege of Food Engineering and Nutritional Science, Shaanxi Normal University, Xi'an, Shaanxi 710119, China. Electronic address: hxinzhong@snnu.edu.cn.
Kanza SaeedFaculty of Food Technology and Nutrition Sciences, University of Biological and Applied Sciences, Lahore, 53400, Pakistan.
Muhammad Zubair KhalidDepartment of Food Science, Faculty of Life Sciences, Government College University, Faisalabad, Punjab, Pakistan.
Waseem KhalidDepartment of Organic Chemistry, Faculty of Chemical Sciences and Technologies, University of Castilla, La Mancha, 13071 Ciudad Real, Spain; Department of Molecular Food Chemistry and Food Development, Institute of Food and One Health, Gottfried Wilhelm Leibniz University Hannover, Hannover, Germany.
Sonia MoryaDepartment of Food Technology and Nutrition, School of Agriculture, Lovely Professional University, Phagwara, 144411, Punjab, India.
Tawfiq AlsulamiDepartment of Food Science & Nutrition, College of Food and Agricultural Sciences, King Saud University, Riyadh 11451, Saudi Arabia.
Robert MugabiDepartment of Food Technology and Nutrition, Makerere University, Kampala, Uganda. Electronic address: mugabi2011@gmail.com.
Gulzar Ahmad NayikMarwadi University Research Centre, Department of Microbiology, Marwadi University, Rajkot, Gujarat 360003, India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Escalating global protein demand necessitates the commercialization of protein rich products. Oat is a promising high-quality protein source but it requires structural and functional modifications to diversify its application. The current investigation was focused on the impact of different powers of ultrasonic waves (200, 400, and 600 W) on structural and functional characteristics of oat protein isolates to improve its techno-functional properties. Higher strength ultrasound waves generated flat sheet structures which were observed while analyzing microstructure of oat protein isolate (OPI). However, non-significant variation in molecular weight distribution were observed in different treatments. At 600 W power of ultrasonic waves the protein fragments show local accumulation, increased α-helix content. Due to uncoiling of protein structure decrease in β-sheets and β-turns was also observed at 600 W. Protein turbidity decreased significantly under low power ultrasonic treatment (200 W) which significantly increased at higher power. Moderate ultrasonic treatment (400 W) promoted protein dissolution, and maintained a good balance between β-sheets (71.04 ± 0.08), α-helix (16.27 ± 0.02) and β-turns (12.68 ± 0.03), exhibiting optimized flexibility and structural integrity. Whereas, higher strength (600 W) significantly destroyed protein structure. The amino acid content decreased significantly with increasing ultrasonic power. The thermal characteristics of OPI remained unaffected after ultrasound treatment. In conclusion, modifications of secondary and tertiary structure induced by moderate ultrasonic treatment (400 W) improved functional properties of OPI. The 400 W treatment resulted in highest essential amino acid content (EAA) i.e., 22.75 ± 0.82 mg/100 mg and total amino acid content (TAA) i.e., 64.94 ± 2.7 mg/100 mg, which are significantly higher than WHO and FAO standards, suggesting best total and essential amino acid production in comparison to other treatments.

Indexed as

AvenaPlant ProteinsUltrasonic WavesProtein Structure, SecondaryPlant ProteinsCircular dichroism spectrophotometerFourier transform infra-red spectroscopy (FTIR)Micro-structureOat protein isolateUltrasound

Identifiers

PMID39693694
PMCPMC11721227

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Registered trials

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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.