Effects of α-casein and β-casein on the stability, antioxidant activity and bioaccessibility of blueberry anthocyanins with an in vitro simulated digestion

Lang, Yuxi; Li, Bin; Gong, Ersheng; Shu, Chi; Si, Xu; Gao, Ningxuan; Zhang, Weijia; Cui, Hong; Meng, Xianjun

doi:10.1016/j.foodchem.2020.127526

Cited by 86 publications

(54 citation statements)

References 36 publications

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“…Arroyo-Maya et al (2016) studied the binding properties of β-LG, whey proteins, and sodium caseinate with pelargonidin, and found that hydrophobic effect promoted pelargonidin binding to CM proteins. Lang et al (2021) confirmed that α-CA and β-CA could interact with ACNs and improve the stability of ACNs in the gastrointestinal tract. Similar to caseins, He et al (2016) found that β-LG improved the heat, oxygen, and light resistance capacity of malvidin-3-O-glucoside (M3G) and hydrophobic interaction was the main binding force between M3G and β-LG.…”

Section: Introductionmentioning

confidence: 57%

“…(2016) studied the binding properties of β‐LG, whey proteins, and sodium caseinate with pelargonidin, and found that hydrophobic effect promoted pelargonidin binding to CM proteins. Lang et al (2021) confirmed that α‐CA and β‐CA could interact with ACNs and improve the stability of ACNs in the gastrointestinal tract. Similar to caseins, He et al.…”

Section: Introductionmentioning

confidence: 96%

“…β‐LG is a natural carrier protein which can bind to hydrophobic ligands and transfer to the cell surface to interact with receptors (Flower et al., 2000; Goers et al., 2002; Schlehuber & Skerra, 2005). Many studies have evaluated the ACNs carrying capacity of CM proteins (Arroyo‐Maya et al., 2016; He et al., 2016; Lang et al, 2019, 2021). Arroyo‐Maya et al.…”

Section: Introductionmentioning

confidence: 99%

“…β-LG is a natural carrier protein which can bind to hydrophobic ligands and transfer to the cell surface to interact with receptors (Flower et al, 2000;Goers et al, 2002;Schlehuber & Skerra, 2005). Many studies have evaluated the ACNs carrying capacity of CM proteins (Arroyo-Maya et al, 2016;He et al, 2016;Lang et al, 2019Lang et al, , 2021. Arroyo-Maya et al (2016) studied the binding properties of β-LG, whey proteins, and sodium caseinate with pelargonidin, and found that hydrophobic effect promoted pelargonidin binding to CM proteins.…”

Section: Introductionmentioning

confidence: 99%

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A molecular docking and molecular dynamics simulation study on the interaction between cyanidin ‐ 3 ‐O ‐glucoside and major proteins in cow's milk

Pan

Zhao

et al. 2020

J. Food Biochem.

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The objective of this study was to investigate the molecular interaction and complex stability of four major cow's milk (CM) proteins (α-LA, β-LG, α s1-CA, and β-CA) with cyanidin-3-O-glucoside (C3G) using computational methods. The results of molecular docking analysis revealed that hydrogen bond and hydrophobic interaction were the main binding forces to maintain the stability of the C3G-CM protein complexes. Molecular dynamics simulation results showed that all complexes except for C3Gα s1-CA were found to reach equilibrium within 50 ns of simulation. α s1-CA and β-CA switched to a more compact conformation after binding with C3G. Additionally, the radius of gyration, number of hydrogen bond, radial distribution function, and interaction energy showed that β-CA is the best C3G carrier protein among the four CM proteins. This study can provide valuable information for CM proteins to serve as C3G delivery carriers. Practical applications Anthocyanins (ACNs) are flavonoid-based pigments that play an important functional role in regulating human's health. Cow's milk (CM) proteins are the most representative protein-based carriers that can improve the short-term bioavailability and stability of ACNs. Thus, it is important to study the interactions between ACNs and CM proteins at the molecular level for the development of effective ACNs delivery carriers. Our study showed that caseins (α s1-CA and β-CA) had more hydrophobic and hydrogen-bonding sites with cyanidin-3-O-glucoside (C3G) than whey proteins using computational methods. Among the four CM proteins, β-CA was the best C3G carrier protein showing the best interaction stability with C3G. Thus, it is helpful for us to screen effective ACNs carriers from multiple protein sources by computational methods.

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Section: Introductionmentioning

confidence: 57%

Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

A molecular docking and molecular dynamics simulation study on the interaction between cyanidin ‐ 3 ‐O ‐glucoside and major proteins in cow's milk

Pan

Zhao

et al. 2020

J. Food Biochem.

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“…(2019) stated that casein protected blueberry anthocyanins through common processing conditions. The authors also reported that casein has the potential to protect anthocyanins through the human digestive system (Lang et al., 2021).…”

Section: Introductionmentioning

confidence: 99%

Combination of rehydrated sodium caseinate aqueous solution with blackcurrant concentrate and the formation of encapsulates via spray drying and freeze drying: Alterations to the functional properties of protein

Hui

Brennan

et al. 2021

J Food Process Preserv

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Protein and Peptide‐Based Nanotechnology for Enhancing Stability, Bioactivity, and Delivery of Anthocyanins

Zhang

Yao

Zhao

et al. 2023

Adv Healthcare Materials

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Anthocyanin, a unique natural polyphenol, is abundant in plants and widely utilized in biomedicine, cosmetics, and the food industry due to its excellent antioxidant, anticancer, antiaging, antimicrobial, and anti‐inflammatory properties. However, the degradation of anthocyanin in an extreme environment, such as alkali pH, high temperatures, and metal ions, limits its physiochemical stabilities and bioavailabilities. Encapsulation and combining anthocyanin with biomaterials could efficiently stabilize anthocyanin for protection. Promisingly, natural or artificially designed proteins and peptides with favorable stabilities, excellent biocapacity, and wide sources are potential candidates to stabilize anthocyanin. This review focuses on recent progress, strategies, and perspectives on protein and peptide for anthocyanin functionalization and delivery, i.e., formulation technologies, physicochemical stability enhancement, cellular uptake, bioavailabilities, and biological activities development. Interestingly, due to the simplicity and diversity of peptide structure, the interaction mechanisms between peptide and anthocyanin could be illustrated. This work sheds light on the mechanism of protein/peptide–anthocyanin nanoparticle construction and expands on potential applications of anthocyanin in nutrition and biomedicine.

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Effects of α-casein and β-casein on the stability, antioxidant activity and bioaccessibility of blueberry anthocyanins with an in vitro simulated digestion

Cited by 86 publications

References 36 publications

A molecular docking and molecular dynamics simulation study on the interaction between cyanidin ‐ 3 ‐O ‐glucoside and major proteins in cow's milk

A molecular docking and molecular dynamics simulation study on the interaction between cyanidin ‐ 3 ‐O ‐glucoside and major proteins in cow's milk

Combination of rehydrated sodium caseinate aqueous solution with blackcurrant concentrate and the formation of encapsulates via spray drying and freeze drying: Alterations to the functional properties of protein

Protein and Peptide‐Based Nanotechnology for Enhancing Stability, Bioactivity, and Delivery of Anthocyanins

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