Amino Acid and Secondary Structure Integrity of Sonicated Milk Proteins

Pathak, Rachana; Leong, Thomas; Martin, Gael M.; Ashokkumar, Muthupandian

doi:10.1071/ch19372

Cited by 15 publications

(5 citation statements)

References 34 publications

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“…The samples were prepared in duplicate and the image data were collected over triplicate experiments. ImageJ was also used for gel densitometry analysis for NR-SDS-PAGE (Carter et al 2013 ; Pathak et al 2020 ).…”

Section: Methodsmentioning

confidence: 99%

Ultrasound-induced protein restructuring and ordered aggregation to form amyloid crystals

et al. 2022

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Amyloid crystals, a form of ordered protein aggregates documented relatively recently, have not been studied as extensively as amyloid fibres. This study investigates the formation of amyloid crystals with low frequency ultrasound (20 kHz) using β-lactoglobulin, as a model protein for amyloid synthesis. Acoustic cavitation generates localised zones of intense shear, with extreme heat and pressure that could potentially drive the formation of amyloid structures at ambient bulk fluid temperatures (20 ± 1 °C). Thioflavin T fluorescence and electron microscopy showed that low-frequency ultrasound at 20 W/cm3 input power induced β-stacking to produce amyloid crystals in the mesoscopic size range, with a mean length of approximately 22 µm. FTIR spectroscopy indicated a shift towards increased intermolecular antiparallel β-sheet content. An increase in sonication time (0–60 min) and input power (4–24 W/cm3) increased the mean crystal length, but this increase was not linearly proportional to sonication time and input power due to the delayed onset of crystal growth. We propose that acoustic cavitation causes protein unfolding and aggregation and imparts energy to aggregates to cross the torsion barrier, to achieve their lowest energy state as amyloid crystals. The study contributes to a further understanding of protein chemistry relating to the energy landscape of folding and aggregation. Ultrasound presents opportunities for practical applications of amyloid structures, presenting a more adaptable and scalable approach for synthesis. Graphical abstract

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Section: Methodsmentioning

confidence: 99%

Ultrasound-induced protein restructuring and ordered aggregation to form amyloid crystals

et al. 2022

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“…In a study conducted by Ashokkumar et al . [70], the impact of both low‐frequency (20 kHz) and medium‐frequency (414 kHz) ultrasound on the amino acid content and the secondary structural integrity of dairy proteins ( α ‐s1/ α ‐s2/ β /κ‐Caseins, BSA, α / β ‐lactoglobulins, lactoferrin) was explored. It was found that both treatment conditions did not influence the protein's primary structure, even under prolonged and extreme processing conditions (6 h at 355 kHz).…”

Section: Effects Of Mechanical Energy Generated By Us On the Protein ...mentioning

confidence: 99%

“…Ashokkumar et al . [70] showed that low‐frequency (20 kHz) ultrasound treatment of hydrolyzed sonicated skim milk proteins (lactoglobulins, caseins, see Table 1) increased β ‐sheet content with a predominance of antiparallel structures accompanied by a protein surface hydrophobicity increase [76,77], causing unfolding and partial denaturation of native protein folding.…”

Section: Effects Of Mechanical Energy Generated By Us On the Protein ...mentioning

confidence: 99%

Effects of sound energy on proteins and their complexes

Kozell,

Solomonov,

Shimanovich

2023

FEBS Letters

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Mechanical energy in the form of ultrasound, and protein complexes intuitively have been considered as two distinct unrelated topics. However, in the past few years, increasingly more attention has been paid to the ability of ultrasound to induce chemical modifications on protein molecules that further change protein‐protein interaction and protein self‐assembling behavior. Despite efforts to decipher the exact structure and the behavior‐modifying effects of ultrasound on proteins, our current understanding of these aspects remains limited. The limitation arises from the complexity of both phenomena. Ultrasound produces multiple chemical, mechanical, and thermal effects in aqueous media. Proteins are dynamic molecules with diverse complexation mechanisms. This review provides an exhaustive analysis of the progress made in better understanding the role of ultrasound in protein complexation. It describes in detail how ultrasound affects an aqueous environment and the impact of each effect separately and when combined with the protein structure and fold, the protein‐protein interaction, and finally the protein self‐assembly. It specifically focuses on modifying role of ultrasound in amyloid self‐assembly, where the latter is associated with multiple neurodegenerative disorders.

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“…Specific compounds within the milk matrices may underlie this effect on target (antioxidant and enzymatic marker) activities. Ultrasonication treatment is known to alter protein structural conformations (Chandrapala et al, 2011, Pathak et al, 2019, Gharibzahedi and Smith, 2020 and at high power, may also cause hydrolysis of peptide bonds (Urbizo-Reyes et al, 2019;Koirala et al, 2021), resulting in release of peptides that potentially influence activities against these specific markers or assays to different levels. The milk samples tested were control (raw milk), pasteurized (heat-treated), and US-treated milk samples without any modification in the composition of the samples.…”

Section: Effects Of Us Treatment On Bioactive Propertiesmentioning

confidence: 99%

Ultrasonication as a novel processing alternative to pasteurization for camel milk: Effects on microbial load, protein profile, and bioactive properties

Mudgil

Alkaabi

Maqsood

2022

Journal of Dairy Science

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Ultrasonic technology presents a promising novel tool in the food industry for the processing of milk and dairy products. In this study, we investigated the effects of ultrasonication (US) as an alternative to thermal pasteurization for stabilization of the bioactive properties of camel milk. Camel and bovine milk samples were subjected to US at 6 different power levels (US1-US6), and 1 set of each type of milk was concurrently subjected to flash heat pasteurization (FHP) for comparative analysis (100 mL; n = 4). The microbiological and bioactive parameters of the samples were analyzed during 7 d of storage at 4°C. In both milk types subjected to US ≥ 140 W (US3), the bacterial load was reduced by almost 4 log cycles and complete reduction of microbial load was achieved with US = 170 W and US = 210 W (US5 and US6 treatments, respectively). No significant changes in protein patterns were observed with either FHP or US treatment. In addition, bioactive properties (cholesteryl esterase and pancreatic lipase inhibition) were either enhanced or retained at US3 or higher. 2,2′-Azino-bis-3-ethylbenzthiazoline-6-sulfonic acid and ferric reducing antioxidant power activities in camel milk were decreased after FHP treatment but increased or retained upon US, particularly at US3 and US4 (160 W). Overall, under our experimental conditions, US4 was effective in completely reducing the microbial count, while concomitantly retaining different bioactive properties of both camel and bovine milk. These outcomes highlight the potential of US at 160 W as an efficient nonthermal alternative processing method for milk.

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Amino Acid and Secondary Structure Integrity of Sonicated Milk Proteins

Cited by 15 publications

References 34 publications

Ultrasound-induced protein restructuring and ordered aggregation to form amyloid crystals

Ultrasound-induced protein restructuring and ordered aggregation to form amyloid crystals

Effects of sound energy on proteins and their complexes

Ultrasonication as a novel processing alternative to pasteurization for camel milk: Effects on microbial load, protein profile, and bioactive properties

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