The dose-dependent effects of polyphenols and malondialdehyde on the emulsifying and gel properties of myofibrillar protein-mulberry polyphenol complex

Cheng, Jingrong; Tang, Daobang; Yang, Huaigu; Wang, Xuping; Zhu, Ming‐Jun; Liu, Xueming

doi:10.1016/j.foodchem.2021.130005

Cited by 42 publications

(24 citation statements)

References 40 publications

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“…The polyphenol concentration governs the retardation of lipid oxidation in MPE-treated SMS, and excessive phenolics are detrimental to the improvement of the SMS antioxidant activity. This was consistent with Cheng et al [ 46 ], who noticed a remarkable upward trend in inhibiting lipid oxidation as mulberry polyphenolic addition increased from 0% to 1.0%, followed by a rapid decline once the addition exceeded 2.5%, with the highest lipid oxidation at 10% mulberry polyphenols added in myofibrillar protein emulsion. It could be explained that excessive polyphenols interacted with myofibrillar protein, causing a change in myofibrillar protein molecular structure at the interface.…”

Section: Resultssupporting

confidence: 92%

“…It could be explained that excessive polyphenols interacted with myofibrillar protein, causing a change in myofibrillar protein molecular structure at the interface. A high concentration of phenolics may also serve as a deterrent, preventing the formation of a continuous protein layer around oil droplets, thereby preventing the formation of high-elastic emulsion [ 46 ]. The high dose of phenolic compounds promotes the production of amino-quinone and thiol-quinone adducts, which may prevent intermolecular interactions from forming between proteins at the emulsion interface.…”

Section: Resultsmentioning

confidence: 99%

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Glochidion wallichianum Leaf Extract as a Natural Antioxidant in Sausage Model System

Wongnen

Ruzzama

Chaijan

et al. 2022

Foods

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This study highlighted the role of an 80% ethanolic Mon-Pu (Glochidion wallichianum) leaf extract (MPE), a novel natural antioxidative ingredient, in controlling the oxidative stability and physicochemical properties of a cooked sausage model system (SMS). MPE had a total extractable phenolic content of 16 mg/100 g, with DPPH● scavenging activity, ABTS●+ scavenging activity, and ferric reducing antioxidant power of 2.3, 1.9, and 1.2 mmole Trolox equivalents (TE)/g, respectively. The effects of different concentrations of MPE (0.01–10%, w/w) formulated into SMS on lipid oxidation, protein oxidation, and discoloration were compared to synthetic butylated hydroxyl toluene (BHT; 0.003%, w/w) and a control (without antioxidant). The peroxide value (PV), thiobarbituric acid reactive substances (TBARS), and protein carbonyl contents of SMS tended to increase with increasing MPE concentration (p < 0.05), indicating that high MPE excipient has a pro-oxidative effect. The lowest lipid oxidation (PV and TBARS) and protein carbonyl contents were observed when 0.01% MPE was used to treat SMS (p < 0.05), which was comparable or even greater than BHT-treated SMS. High concentrations (1–10%) of MPE incorporation led to increases in the discoloration of SMS (p < 0.05) with a negligible change in pH of SMS. The water exudate was reduced when MPE was incorporated into SMS compared to control (p < 0.05). Furthermore, MPE at 0.01% significantly reduced lipid oxidation in cooked EMS during refrigerated storage. According to the findings, a low amount of MPE, particularly at 0.01%, in a formulation could potentially maintain the oxidative stability and physicochemical qualities of cooked SMS that are comparable to or better than synthetic BHT.

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Section: Resultssupporting

confidence: 92%

Section: Resultsmentioning

confidence: 99%

Glochidion wallichianum Leaf Extract as a Natural Antioxidant in Sausage Model System

Wongnen

Ruzzama

Chaijan

et al. 2022

Foods

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“…The occurrence of secondary carbonylation has also been found to affect protein functionality though the effect depends on the nature of the lipid-derived carbonyl and its concentration. Cheng et al ( 2021a , b ) recently observed that 5–20 mM MDA improved the WHC and rheological properties of gels from myofibrillar proteins while at even higher MDA concentrations (40 mM), the emulsion gel was completely lost. It is worth clarifying that these experimental MDA concentrations are out of the range found in processed or digested food products (Steppeler et al 2016 ).…”

Section: Concise Update On the Biological Consequences Of Protein Car...mentioning

confidence: 99%

“…According to recent literature, the carbonylation of proteins via the Maillard reaction (Luna and Estévez 2019 ; Wu et al 2021 ) or via introduction of secondary lipid carbonyls such as MDA (Niu et al 2019 ; Li et al 2021a , b ) have a deleterious impact on the digestibility of meat, dairy and cereal proteins. Recent studies have also established plausible connections between the extent of protein carbonylation and a reduced digestibility of proteins in a variety of foods such as egg white (Cheng et al 2021a , b ), whey isolate (Niu et al 2019 ), ready-to-eat chicken patties (Ferreira et al 2018 ), fish fillets (Semedo Tavares et al 2018 ) and air-dried yak meat (Ma et al 2021 ), among many others.…”

Section: Concise Update On the Biological Consequences Of Protein Car...mentioning

confidence: 99%

Protein carbonylation in food and nutrition: a concise update

2021

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Protein oxidation is a topic of indisputable scientific interest given the impact of oxidized proteins on food quality and safety. Carbonylation is regarded as one of the most notable post-translational modifications in proteins and yet, this reaction and its consequences are poorly understood. From a mechanistic perspective, primary protein carbonyls (i.e. α-aminoadipic and γ-glutamic semialdehydes) have been linked to radical-mediated oxidative stress, but recent studies emphasize the role alternative carbonylation pathways linked to the Maillard reaction. Secondary protein carbonyls are introduced in proteins via covalent linkage of lipid carbonyls (i.e. protein-bound malondialdehyde). The high reactivity of protein carbonyls in foods and other biological systems indicates the intricate chemistry of these species and urges further research to provide insight into these molecular mechanisms and pathways. In particular, protein carbonyls are involved in the formation of aberrant and dysfunctional protein aggregates, undergo further oxidation to yield carboxylic acids of biological relevance and establish interactions with other biomolecules such as oxidizing lipids and phytochemicals. From a methodological perspective, the routine dinitrophenylhydrazine (DNPH) method is criticized not only for the lack of accuracy and consistency but also authors typically perform a poor interpretation of DNPH results, which leads to misleading conclusions. From a practical perspective, the biological relevance of protein carbonyls in the field of food science and nutrition is still a topic of debate. Though the implication of carbonylation on impaired protein functionality and poor protein digestibility is generally recognized, the underlying mechanism of such connections requires further clarification. From a medical perspective, protein carbonyls are highlighted as markers of protein oxidation, oxidative stress and disease. Yet, the specific role of specific protein carbonyls in the onset of particular biological impairments needs further investigations. Recent studies indicates that regardless of the origin (in vivo or dietary) protein carbonyls may act as signalling molecules which activate not only the endogenous antioxidant defences but also implicate the immune system. The present paper concisely reviews the most recent advances in this topic to identify, when applicable, potential fields of interest for future studies.

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“…On the one hand, it will affect the solubility and taste of polyphenols food (Chen et al, 2015; Hasni et al, 2011; Niseteo et al, 2012; Qie et al, 2020). On the other hand, it will affect the structural characteristics and physiological functions of the proteins themselves (Chen et al, 2019; Cheng et al, 2021; Diaz et al, 2021; Duarte & Farah, 2011; Pham et al, 2019). Therefore, the scientific researches on polyphenol–protein interactions play an important role in understanding the physiological activities and pharmacological effects of polyphenols.…”

Section: Introductionmentioning

confidence: 99%

Insights into interactions between food polyphenols and proteins: An updated overview

Wang

Xie

Wang

et al. 2022

Food Processing Preservation

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Polyphenols are widely distributed natural products, investigated intensively due to their health-beneficial effects and prevention of several human diseases. It is well known that polyphenols can easily form complexes with proteins in food processing and human digestion, leading to changes in the conformation and functionality of polyphenols and proteins. On the basis of dividing the common polyphenols into flavonoids, phenolic acids, and tannins, this paper reviews the progress and application of polyphenol-protein interactions during the past decade. Accordingly, this review might provide a better understanding on the mechanism of polyphenol-protein interactions, which is expected to provide guidance for food processing and studying on health effects of polyphenol compounds in the future. Novelty impact statementThe interactions of flavonoids, phenolic acids, and tannins with proteins were reviewed.Reversible interactions are the main form of polyphenol-protein interactions, which are mainly attributed to hydrogen and hydrophobic bonding. Besides, the health effects of polyphenol-protein complexes mainly include the inhibition of protease and toxic protein aggregation.

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The dose-dependent effects of polyphenols and malondialdehyde on the emulsifying and gel properties of myofibrillar protein-mulberry polyphenol complex

Cited by 42 publications

References 40 publications

Glochidion wallichianum Leaf Extract as a Natural Antioxidant in Sausage Model System

Glochidion wallichianum Leaf Extract as a Natural Antioxidant in Sausage Model System

Protein carbonylation in food and nutrition: a concise update

Insights into interactions between food polyphenols and proteins: An updated overview

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