Functional modification of grain proteins by dual approaches: Current progress, challenges, and future perspectives

Kamani, Mohammad Hassan; Semwal, Jyoti; Khaneghah, Amin Mousavi

doi:10.1016/j.colsurfb.2021.112306

Cited by 15 publications

(5 citation statements)

References 97 publications

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“…Moreover, the coordination complexes formed between zinc ions and the succinylated protein further stabilizes its structure, contributing to its improved ability to hold and retain water [59]. Furthermore, WHC of USCP-Zn signifcantly increased (p < 0.05) from 3.41 ± 0.29 to 4.73 ± 0.32 as compared to SCP-Zn, this can be attributed to the fact that ultrasonication induces mechanical energy that disrupts protein aggregates and unfolds the protein, while succinylation introduces hydrophilic groups and prevents aggregation [60]. Tese combined modifcations optimize the protein's structure and surface properties, making it more accessible to water molecules and allowing it to form stronger interactions with water [61].…”

Section: Water and Oil-holding Capacity (Whc And Ohc)mentioning

confidence: 93%

“…Tis improved solubility allows the succinylated protein to form a more uniform and stable emulsion. In addition, the modifcation alters the protein's surface properties, leading to increased adsorption at the oil-water interface and better stabilization of the emulsion [60]. Te succinylation process also promotes stronger protein-protein interactions through cross-linking, further contributing to the emulsion's stability [69].…”

Section: Emulsifying Capacity and Stability (Ec And Es)mentioning

confidence: 99%

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Enhancing Zinc Uptake through Dual-Modification of Cicer arietinum Protein

Patil,

Bains,

Sridhar

et al. 2023

Journal of Food Biochemistry

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Zinc is crucial for physiological processes; however, deficiency persists globally. Binding zinc to plant proteins enhances absorption, minimizing toxicity risks and offering a potential solution for deficiency. Mineral binding efficiency of the unmodified protein is limited; hence, dual modification (succinylation and ultrasonication) is potentially used to achieve higher binding efficiency. Enhancing zinc uptake is crucial for cellular health due to its vital roles in various biological processes including enzymatic activity, DNA repair, immune function, antioxidant defense, hormone regulation, brain function, signaling, growth, gene expression, and reproduction. Therefore, this research aimed to develop a chickpea protein-zinc complex and to evaluate the influence of dual modification on their physiochemical, bioavailability, and cellular mineral uptake attributes. Succinylation exhibited significant improvements in the water-holding capacity by 28.73%, oil-holding capacity by 34.09%, and solubility by 5.46% of the chickpea protein-zinc complex as compared to the native complex. Mineral bioavailability increased by 8.32%, and there were notable increases in cellular uptake of zinc by 2.10%, retention by 5.80%, and transport by 3.96%, respectively. Furthermore, the dual modification approach resulted in a notable decrease in the particle size of the chickpea protein-zinc complex, with a substantial reduction of 73.25% and an increased zeta potential value of −21 mV compared to the succinylated complex. As well, dual modification concurrently led to a substantial decline of 48.04% in the sulfhydryl (SH) content, coupled with a marked increase of 21.92% in the surface hydrophobicity. In addition, zinc bioavailability, cellular uptake, retention, and transport were further enhanced by 1.89, 3.34, and 4.8% through dual modification. Our findings highlight that the dual modification of the chickpea protein-zinc complex shows a promising strategy for enhancing the techno-functional characteristics, bioavailability, and cellular uptake of zinc, which could be a better platform for developing vegan foods.

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Section: Water and Oil-holding Capacity (Whc And Ohc)mentioning

confidence: 93%

Section: Emulsifying Capacity and Stability (Ec And Es)mentioning

confidence: 99%

Enhancing Zinc Uptake through Dual-Modification of Cicer arietinum Protein

Patil,

Bains,

Sridhar

et al. 2023

Journal of Food Biochemistry

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“…It is noteworthy that, with the help of an external agent (e.g., heating), kafirin can hydrate more compared to non-heat-treated kafirin. Heating does not change the amino acid content of kafirin, but some conformational changes like the conversion of α-helices into β-sheets due to the effect of heating might result in more water absorption [63].…”

Section: Hydrophobicitymentioning

confidence: 99%

Advances in Extraction, Structure, and Physiochemical Properties of Sorghum Kafirin for Biomaterial Applications: A Review

Shah,

Bhattarai,

Al-Salami

et al. 2024

JFB

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Kafirin is an endosperm-specific hydrophobic protein found in sorghum grain and the waste by-product from sorghum biorefineries known as sorghum dried distillers’ grain with solubles (DDGS). Because of kafirin’s poor nutritional profile (negative nitrogen balance, slow digestibility, and lack of some essential amino acids), its direct human use as a food is restricted. Nevertheless, increased focus on biofuel production from sorghum grain has triggered a new wave of research to use sorghum DDGS kafirin as a food-grade protein for biomaterials with diverse applications. These applications result from kafirin’s unique chemical nature: high hydrophobicity, evaporation-induced self-assembling capacity, elongated conformation, water insolubility, and low digestibility. Aqueous alcohol mixtures have been widely used for the extraction of kafirin. The composition, structure, extraction methodologies, and physiochemical properties of kafirin, emphasising its biomaterial functionality, are discussed in detail in this review. The literature survey reveals an in-depth understanding of extraction methodologies and their impact on structure functionality, which could assist in formulating materials of kafirin at a commercial scale. Ongoing research continues to explore the potential of kafirin and optimise its utilisation as a functional biomaterial, highlighting its valuable structural and physicochemical properties. Further studies should focus on covering gaps in the research as some of the current structural understanding comes from data on zein protein from maize.

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“…Studies have shown that both HPH ( Ong, et al, 2022 ) and US ( Mozafarpour et al, 2022 ) have an impact on the physicochemical and functional properties of pea protein. The combined use of modification methods may be more effective in improving protein characteristics ( Kamani et al, 2021 ). Zhao et al's study shows that the combination of HPH and US-assisted Maillard reaction can improve multiple functional properties of pea protein ( Zhao, et al, 2022 ).…”

Section: Introductionmentioning

confidence: 99%