Details
Original language | English |
---|---|
Article number | 107204 |
Number of pages | 8 |
Journal | Ultrasonics Sonochemistry |
Volume | 112 |
Early online date | 16 Dec 2024 |
Publication status | Published - Jan 2025 |
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.
Keywords
- Circular dichroism spectrophotometer, Fourier transform infra-red spectroscopy (FTIR), Micro-structure, Oat protein isolate, Ultrasound
ASJC Scopus subject areas
- Environmental Science(all)
- Environmental Chemistry
- Chemical Engineering(all)
- Chemical Engineering (miscellaneous)
- Medicine(all)
- Radiology Nuclear Medicine and imaging
- Physics and Astronomy(all)
- Acoustics and Ultrasonics
- Chemistry(all)
- Organic Chemistry
- Chemistry(all)
- Inorganic Chemistry
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In: Ultrasonics Sonochemistry, Vol. 112, 107204, 01.2025.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Ultrasound-assisted modification of oat protein isolates
T2 - Structural and functional enhancements
AU - Rafique, Hamad
AU - Peng, Pai
AU - Hu, Xinzhong
AU - Saeed, Kanza
AU - Khalid, Muhammad Zubair
AU - Khalid, Waseem
AU - Morya, Sonia
AU - Alsulami, Tawfiq
AU - Mugabi, Robert
AU - Nayik, Gulzar Ahmad
N1 - Publisher Copyright: © 2024 The Author(s)
PY - 2025/1
Y1 - 2025/1
N2 - 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.
AB - 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.
KW - Circular dichroism spectrophotometer
KW - Fourier transform infra-red spectroscopy (FTIR)
KW - Micro-structure
KW - Oat protein isolate
KW - Ultrasound
UR - http://www.scopus.com/inward/record.url?scp=85212186650&partnerID=8YFLogxK
U2 - 10.1016/j.ultsonch.2024.107204
DO - 10.1016/j.ultsonch.2024.107204
M3 - Article
C2 - 39693694
AN - SCOPUS:85212186650
VL - 112
JO - Ultrasonics Sonochemistry
JF - Ultrasonics Sonochemistry
SN - 1350-4177
M1 - 107204
ER -