Effect of ultrasonic treatment on the structure and functional properties of mantle proteins from scallops (Patinopecten yessoensis)

Ding, Qiuyue; Tian, Guifang; Wang, Xianghong; Deng, Wenyi; Mao, Kemin; Sang, Yaxin

doi:10.1016/j.ultsonch.2021.105770

Cited by 42 publications

(33 citation statements)

References 53 publications

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“…In addition, mild heating (70 °C) promoted the denaturation of the protein, leading to a change in the position of tryptophan residues and consequently to its fluorescence emission [ 20 ]. Attenuated tryptophan fluorescence by overheating (100 °C, 30 min) was observed in myosin, implying that a relatively high heating temperature accelerated the aggregation of protein [ 21 ]. These results revealed the essential role of processing temperature in modifying the stable structure of myosin.…”

Section: Resultsmentioning

confidence: 99%

Effect of Thermal Processing on the Conformational and Digestive Properties of Myosin

Zhang

Zhu

et al. 2023

Foods

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Heat treatment affects the structural properties of meat proteins, which in turn leads to changes in their sensitivity to digestive enzymes, further affecting the nutritional value of meat and meat products. The mechanism of changes in the structure and digestive properties of myosin under different heating conditions were studied. An increase in heating temperature led to the exposure of internal groups to a polar environment, but to a decrease in the sturdy α-helix structure of myosin (p < 0.05). The results of tryptophan fluorescence verified that the tertiary structure of the protein seemed to be unfolded at 70 °C. Higher protein denaturation after overheating, as proven by the sulfhydryl contents and turbidity, caused irregular aggregate generation. The excessive heating mode of treatment at 100 °C for 30 min caused myosin to exhibit a lower degree of pepsin digestion, which increased the Michaelis constant (Km value) of pepsin during the digestion, but induced the production of new peptides with longer peptide sequences. This study elucidates the effects of cooking temperature on the conformation of myosin and the change in digestibility of pepsin treatment during heating.

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Section: Resultsmentioning

confidence: 99%

Effect of Thermal Processing on the Conformational and Digestive Properties of Myosin

Zhang

Zhu

et al. 2023

Foods

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“…The precipitate was redissolved in 50 mL of 60% (v/v) isopropanol solution and was subjected to lyophilization to obtain fraction 3 (F3, containing β-coixin). The lyophilization samples were weighted, and the extraction rates of prolamin components were calculated according to the following formula (Ding, Tian, et al, 2021;Ding, Ma, et al, 2021):…”

Section: Extraction and Separation Of Coixin Fractionsmentioning

confidence: 99%

“…Then the samples were centrifuged at 5000g/min for 15 min to remove the supernatant. The water holding capacity (WHC) and oil holding capacity (OHC) were calculated using the following formulae (Ding, Tian, et al, 2021;Ding, Ma, et al, 2021): where M represents total protein content in the sample, M 1 represents the total mass of the centrifugal tube and the sample(g), M 2 represents the total mass of the centrifugal tube and the deposit with water(g), and M 3 represents the total mass of the centrifugal tube and the deposit with oil (g).…”

Section: Water Holding Capacity (Whc) and Oil Holding Capacity (Ohc)mentioning

confidence: 99%

Difference analysis of the structure and functional properties among coix seed prolamin fractions (α‐, β‐, and γ‐coixin)

Zhou

et al. 2023

Journal of Food Science

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The differences in proteins in structural characteristics are reported to affect their physicochemical and functional properties. In this study, three types of prolamins (γ‐, α‐, and β‐coixin) derived from coix seed separately distributed among fractions 1–3 extracts. They were studied respecting molecular weight, amino acid composition, secondary structure, microstructure, surface hydrophobicity, solubility, water holding capacity, and oil holding capacity. Results showed that the molecular weights of those three fractions were between 10 and 40 kDa. The secondary structure of those fractions was almost the same, mainly based on β‐sheet and irregular structure. The microstructure of α‐ and γ‐coixin presented an irregular shape, whereas β‐coixin presented a regular spherical shape. Those three fractions exhibited species of abundant essential amino acids with the same amino acid composition but different contents. The β‐coixin fraction had the highest content of hydrophobic amino acids (238.39 mg/g) followed by the α‐coixin fraction (235.05 mg/g), whereas the γ‐coixin fraction had the lowest content (33.27 mg/g). The γ‐coixin fraction has the maximum surface hydrophobicity, whereas the β‐coixin fraction has the highest solubility. In addition, the good amphiphilicity of β‐coixin fraction made it possible to be used as a surfactant. The excellent functional properties of the β‐coixin fraction presented in this research would widen the applications of coix seed prolamins. Practical Application The molecular weights of those three fractions were between 10 and 40 kDa. The secondary structure was almost the same, mainly based on β‐sheet and irregular structure. Those three fractions exhibited species of abundant essential amino acids with the same amino acid composition but different contents. The WHC and OHC of β‐coixin were the best, indicating its potential as a surfactant and forming stable lotion.

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“…Specifically, MAE improves the emulsification, oil‐absorption, water‐holding and binding capacities, and digestibility (especially the release of peptides with low molecular weights) of proteins which also impacts on the bioactivities of the proteins when hydrolyzed (Görgüç et al, 2020; Li et al, 2020; Zhang et al, 2022). In addition, ultrasound‐assisted extraction (UAE) is another eco‐friendly technology used in protein extraction to improve the functional properties of proteins such as digestibility, solubility, and binding capacity as well as bioactive properties, similar to MAE (Ding et al, 2021; Habinshuti et al, 2020; Melchior et al, 2020; Ngo & Shahidi, 2021; Vanga et al, 2021). Recently, a combination of MAE and UAE are being explored and findings showed that the combinatorial effect of the two technologies are better than their individual effects in relation to altering the structural properties of the proteins that are needed to improve their post‐extraction functionalities (Jiang et al, 2020; Muñoz‐Almagro et al, 2021; Nasrabadi et al, 2021).…”

Section: Sources and Isolation Of Food Proteins And Peptides With Ost...mentioning

confidence: 99%

Osteo‐modulatory dietary proteins and peptides: A concise review

Okagu

Aham

Ezeorba

et al. 2022

Journal of Food Biochemistry

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Effect of ultrasonic treatment on the structure and functional properties of mantle proteins from scallops (Patinopecten yessoensis)

Abstract: Highlights Effect of ultrasound was wholly studied on various protein functions of scallop mantle. Ultrasound regulated functions by modifying the structure of scallop mantle protein. Ultrasound can modify structure of scallop mantle protein except primary structure.

Cited by 42 publications

References 53 publications

Effect of Thermal Processing on the Conformational and Digestive Properties of Myosin

Effect of Thermal Processing on the Conformational and Digestive Properties of Myosin

Difference analysis of the structure and functional properties among coix seed prolamin fractions (α‐, β‐, and γ‐coixin)

Osteo‐modulatory dietary proteins and peptides: A concise review

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