Consequences of phosphorylation on the structural and foaming properties of ovalbumin under wet-heating conditions

Sheng, Long; Ye, Siqi; Han, Kui; Zhu, Guilan; Ma, Meihu; Cai, Zhaoxia

doi:10.1016/j.foodhyd.2019.01.023

Cited by 101 publications

(42 citation statements)

References 45 publications

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“…Therefore, improving the functional properties of OVA, such as improving its foaming ability (FA), emulsifying ability, heat stability, and gelation behavior, will help to further the utilization of EWP in the food industry. [2] Despite the excellent functional properties displayed by OVA, while in order to meet the complex needs of manufactured food products, several effective methods of improving functionalities of OVA were developed, e.g., wet-heating phosphorylated to improve functional properties, [3] pH-induced to the molten globule state, [4] Maillard reaction to generate protein-polysaccharide conjugates. [5] Moreover, high-pressure pulsation, high hydrostatic pressures, and high-intensity ultrasound (HIU) were also used to modify the solubility and gelling ability of protein.…”

Section: Introductionmentioning

confidence: 99%

Enzymolysis kinetics and structural-functional properties of high-intensity ultrasound-assisted alkali pretreatment ovalbumin

Liu

Hao

Dai

et al. 2020

International Journal of Food Properties

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This research investigated the enzymolysis kinetics of high-intensity ultrasound (HIU)-assisted alkali pretreatment Ovalbumin (OVA) through using Alcalase, and its structural and functional properties. The structural characteristics of OVA were performed with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), surface hydrophobicity, Fourier Transform Infrared, and differential scanning calorimetry. SDS-PAGE analysis indicated that the pretreatment sample showed proportion of lower molecular mass components (14.3-20.1 kDa). There was an increase in the intensity of fluorescence spectrum and changes in functional groups after the pretreatment on OVA compared with the control (without treatment), which might be the reason for the significantly enhancing efficiency of the enzymatic hydrolysis. The thermal denaturation temperature of enzymatic hydrolysis of OVA after pretreatment was 95.1°C, which was 17.5°C higher than that of control. As compared to OVA (control), the enzymatic hydrolysis with HIU-assisted alkali pretreatment was found to significantly improve protein solubility, emulsifying properties, foaming ability (FA) and foam stability, oil, and water absorption capacity (WAC). Especially emulsifying activity index, FA, WAC, and oil absorption capacity were increased by 228.7%, 88.5%, 102.6%, and 67.4%, respectively (P< 0.05). A simplified kinetic equation for the enzymolysis model was deduced to successfully describe the enzymatic hydrolysis of pretreated OVA. The results proved the effects of the pretreatment on the substrate enhanced the enzymolysis process and this influence had relation to the structure changes. Furthermore, the enzymatic hydrolysis process for other proteins demonstrated the applicability of the model.

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Section: Introductionmentioning

confidence: 99%

Enzymolysis kinetics and structural-functional properties of high-intensity ultrasound-assisted alkali pretreatment ovalbumin

Liu

Hao

Dai

et al. 2020

International Journal of Food Properties

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“…The complicated procedure, with an attendant limited improvement in phosphorus level, is unwarranted for a large‐scale application on a practical and economical basis. Compared to the long incubation (≥24 hr) dry‐heating phosphorylation where relatively high temperature (usually ≥85 °C) may exceed the thermal denaturation range of some proteins, wet‐heating phosphorylation in the presence of sodium tripolyphosphate (Figure 5b‐3) seemed to be more applicable for industrial application (Sheng et al., 2019). Accordingly, some literatures have thrown light on the conformational changes in proteins after phosphorylation (Li, Enomoto, et al., 2010; Sheng et al., 2019; Yang et al., 2019).…”

Section: Chemical Modificationmentioning

confidence: 99%

“…Compared to the long incubation (≥24 hr) dry‐heating phosphorylation where relatively high temperature (usually ≥85 °C) may exceed the thermal denaturation range of some proteins, wet‐heating phosphorylation in the presence of sodium tripolyphosphate (Figure 5b‐3) seemed to be more applicable for industrial application (Sheng et al., 2019). Accordingly, some literatures have thrown light on the conformational changes in proteins after phosphorylation (Li, Enomoto, et al., 2010; Sheng et al., 2019; Yang et al., 2019). Some studies claimed that the application of sodium tripolyphosphate allowed the phosphate groups to be covalently attached to the ‒OH or ‒NH 2 of amino acid residues, regardless of dry‐ or wet‐heating systems (Wang, Zhang, et al., 2019; Xiong et al., 2016).…”

Section: Chemical Modificationmentioning

confidence: 99%

Modification of pulse proteins for improved functionality and flavor profile: A comprehensive review

Zha

Rao

Chen

2021

Comp Rev Food Sci Food Safe

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Consumers’ preference to have a healthy eating pattern has led to an increasing demand for more nutrient‐dense and healthier plant‐based foods. Pulse proteins are exceptional quality ingredients with potential nutritional benefits, and might act as health‐promoting agents for addressing the new‐generation foods. However, the utilization of pulse protein in foods has been hampered by its relatively poor functionality and unpleasant flavor. Protein structure modification has been proved to be a useful means to improve the functionality and flavor profile of pulse protein. This paper begins with a brief introduction of hierarchical structure of pulse protein materials to better understand the structure characteristics. A comprehensive review is presented on the current techniques including chemical and enzymatic modifications and molecular breeding on pulse protein structure and functionality/flavor. The mechanism and the limitations and the toxicological concerns of these approaches are discussed. We conclude that understanding protein structure‒functionality relationship is extremely valuable in tailoring proteins for specific functional outcomes and expanding the availability of pulse proteins. Furthermore, selective protein modification is a valuable in‐depth toolkit for generating novel protein constructs with preferable functional attributes and flavor profiles. Innovative structure modification with special focus on the molecular basis for the exquisite protein designs is a pillar of pulse protein access to the desired functionality.

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“…Protein phosphorylation modification has been proved to significantly improved the functional properties of ovalbumin (Sheng et al., 2019; Xiong, Zhang, & Ma, 2016), rice bran protein (Hu, Qiu, Sun, Xiong, & Ogra, 2019), soybean protein (Wang & Chi, 2012), in terms of emulsification, foamability, heat stability, solubility, gelation, and so on. Phosphorylation of food proteins can increase the electronegativity and decrease the isoelectric point of phosphorylated proteins, thereby changing the functional properties (Zhang, 2006).…”

Section: Introductionmentioning

confidence: 99%

Effects of different drying methods on the structures and functional properties of phosphorylated Antarctic krill protein

Lin

Liu

et al. 2020

Journal of Food Science

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Antarctic krill protein (AKP) was extracted from Antarctic krill by an alkali dissolution‐isoelectric precipitation method and then it was phosphorylated with sodium tripolyphosphate. The phosphorylated Antarctic krill protein (P‐AKP) powder was obtained by spray‐drying (SD), freeze‐drying (FD), and hot‐air drying (AD), and the effects of these drying methods on the structures and functional properties of proteins were investigated. The P‐AKP powder dried by SD had the best sensory performance, and its particle size was much smaller than that of FD and AD. Scanning electron microscope displayed a uniform particle size of SD powder and the particles were uniformly dispersed. X‐ray diffraction analysis showed a higher crystallinity of SD sample than AD and FD. Differential scanning calorimeter analysis revealed that SD sample had the best thermal stability and less protein denaturation (ΔH = 210.80 J/g), followed by FD (ΔH = 80.48 J/g) and AD (ΔH = 73.94 J/g; P < 0.05). Fourier transform infrared showed that SD sample contained more protein secondary structure. Compared with SD, the phosphorylated group‐related chemical bonds in FD and AD samples were partially destroyed. SD sample had the highest protein solubility, oil absorption capacity, emulsifying, and foaming activities than FD and AD (P < 0.05). Although FD had the highest water absorption capacity, sample prepared with AD had the worst functional performance. Therefore, different drying methods used for preparation of the P‐AKP can affect its physicochemical and associated functional properties, and SD could be an appropriate drying method for the industrial mass production of P‐AKP powders with better functionalities. Practical Application The optimal drying method for preparing the phosphorylated Antarctic krill protein (P‐AKP) powder was proved to be spray‐drying (SD), because the physicochemical and functional properties were better for P‐AKP dried by SD than the other drying methods. Hence, SD was recommended for the industrial mass production of P‐AKP powders with better functionalities. This research can provide theoretical guidance for the further processing and utilization of P‐AKP, and offer technical reference for food processing and preservation.

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Consequences of phosphorylation on the structural and foaming properties of ovalbumin under wet-heating conditions

Cited by 101 publications

References 45 publications

Enzymolysis kinetics and structural-functional properties of high-intensity ultrasound-assisted alkali pretreatment ovalbumin

Enzymolysis kinetics and structural-functional properties of high-intensity ultrasound-assisted alkali pretreatment ovalbumin

Modification of pulse proteins for improved functionality and flavor profile: A comprehensive review

Effects of different drying methods on the structures and functional properties of phosphorylated Antarctic krill protein

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