Whey Protein Structure and Denaturation and Interactions with Other Food Components

Wang, Cuina; Guo, Mingruo

doi:10.1002/9781119256052.ch4

Cited by 5 publications

(6 citation statements)

References 157 publications

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“…Since whey proteins have different molecular properties, structures, and denaturations, these factors change when they are found together. For example, when α-LA and β-LG are together, denaturation temperature and aggregate sizes are affected [39]. The quaternary structure of β-LG, consisting of 162 amino acids, varies with low concentration (<10 mg/mL) and high pH at temperature (<10°C).…”

Section: Extraction Of Bioactive Peptidesmentioning

confidence: 99%

“…With increasing temperature (65°C≤), β-LG denatures and Extraction of Bioactive Peptides from Whey Proteins by Conventional and Novel Technologies DOI: http://dx.doi.org/10.5772/intechopen.1005645 aggregation of oligomers causes irreversible aggregation, releasing free sulfhydryl. However, in skimmed milk with a high water content, β-LG denatures to 75-100°C at higher temperatures [39]. α-LA (about 14 kDa), on the other hand, is less sensitive to pH changes [8].…”

Section: Extraction Of Bioactive Peptidesmentioning

confidence: 99%

“…The novel/ conventional technologies UAE-EH Change of peptide profile [48] Shortening of hydrolysis time [48,49] Low molecular weight peptide extraction [48,49] Increase in bioactivity [48] Reducing the amount of enzymes required [48] Increasing substrate sensitivity [39,41] HHP-EH Increased number of bioactive peptides [50] Enhancement of physiological properties [51] Enzyme to improve substrate accessibility [41] After HPP pretreatment, protein/peptide interaction may occur again [3] MAE-EH Obtaining low molecular weight peptides [41] Enables rapid and efficient hydrolysis [2,52] OH-EH Enhancing bioactive properties [48] Table 1.…”

Section: Advantages Disadvantagesmentioning

confidence: 99%

“…Similarly, the conditions of an application before enzymatic hydrolysis (pepsin and papain) with an ultrasonic sonicator (300-400 W, 20 kHz, 2-4 min) and the degrees of hydrolysis vary according to the enzyme used [49]. β-LG, high-intensity ultrasound (frequency of 20 kHz, 60 Wcm −2 ) has been reported to increase the sensitivity of pepsin and trypsin to proteolysis [39].…”

Section: Ultrasound-assisted Extractionmentioning

confidence: 99%

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Extraction of Bioactive Peptides from Whey Proteins by Conventional and Novel Technologies

Kilic

2024

Food Science and Nutrition

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Bioactive peptides show physiological properties in systems such as digestive, cardiovascular, and vascular. Bioactive compounds are found in animal and plant proteins. However, peptides obtained from milk proteins have better biological activity in terms of amino acid composition and sequence. It is important to industrially evaluate bioactive peptides after proper extraction, purification, and identification. There are conventional (enzymatic hydrolyzation and fermentation) and novel methods (ohmic heating, ultrasound and microwave) for the extraction of bioactive peptides. Novel extraction methods increase the degree of hydrolysis of peptides, making them more efficient, and peptides with high activity are obtained. The extraction method of bioactive peptides to be extracted from whey is important, and the method to be chosen must be evaluated in all its aspects. This chapter includes literature data on the importance of whey proteins, bioactive peptides, and extraction methods of bioactive peptides from whey.

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Section: Extraction Of Bioactive Peptidesmentioning

confidence: 99%

Section: Extraction Of Bioactive Peptidesmentioning

confidence: 99%

Section: Advantages Disadvantagesmentioning

confidence: 99%

Section: Ultrasound-assisted Extractionmentioning

confidence: 99%

See 2 more Smart Citations

Extraction of Bioactive Peptides from Whey Proteins by Conventional and Novel Technologies

Kilic

2024

Food Science and Nutrition

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“…Low‐intensity ultrasound is commonly employed in non‐destructive applications. In contrast, high‐intensity ultrasound (HIUS) is widely utilized for the physical, chemical, and biological modification of food materials, including proteins, carbohydrates, and others (Farjami et al., 2021; Wang & Guo, 2019). The modification process involves diverse mechanisms depending on the specific application.…”

Section: Mechanisms Of Ultrasound‐assisted Ionic Liquids On Proteinmentioning

confidence: 99%

How does ultrasound‐assisted ionic liquid treatment affect protein? A comprehensive review of their potential mechanisms, safety evaluation, and physicochemical and functional properties

Zhang,

Boateng,

2023

Comp Rev Food Sci Food Safe

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Proteins are essential to human health with enormous food applications. Despite their advantages, plant and animal proteins often exhibit limited molecular flexibility and poor solubility due to hydrogen bonds, hydrophobic interactions, and ionic interactions within their molecular structures. Thus, there is an urgent need to modify the rigid structure of proteins to enhance their stability and functional properties. Ultrasound‐assisted ionic liquid (UA‐IL) treatment for developing compound modification and producing proteins with excellent functional properties has received interest. However, no review specifically addresses the interactions between UA‐ILs and proteins. Hence, this review focused on recent research advancements concerning the effects and potential reaction mechanisms of UA‐ILs on the physicochemical properties (including particle size; primary, secondary, and tertiary structure; and surface morphology) as well as the functionality (such as solubility, emulsifying properties, and foaming ability) of proteins. Moreover, the safety evaluation of modified proteins was also discussed from various perspectives, such as acute and chronic toxicity, genotoxicity, cytotoxicity, and environmental and microbial toxicity. This review demonstrated that UA‐IL treatment‐induced protein structural changes significantly impact the functional characteristics of proteins. This treatment approach efficiently promotes protein structure stretching and spatial rearrangement through cavitation, thermal effects, and ionic interactions. As a result, the functional properties of modified proteins exhibited an obvious enhancement, thereby bringing more opportunities to utilize modified protein products in the food industry. Potential future directions for protein modification using UA‐ILs were also proposed.

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The Scope of Biopolymers in Food Industry

Gupta

Ghosal

Goswami

et al. 2022

Springer Series on Polymer and Composite Materials

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Whey Protein Structure and Denaturation and Interactions with Other Food Components

Cited by 5 publications

References 157 publications

Extraction of Bioactive Peptides from Whey Proteins by Conventional and Novel Technologies

Extraction of Bioactive Peptides from Whey Proteins by Conventional and Novel Technologies

How does ultrasound‐assisted ionic liquid treatment affect protein? A comprehensive review of their potential mechanisms, safety evaluation, and physicochemical and functional properties

The Scope of Biopolymers in Food Industry

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