Modification of whey−soybean mixed protein by sequential high-pressure homogenization and transglutaminase treatment

Han, Xiue; Liang, Zhiqiang; Tian, Songfan; Liu, Lu; Wang, Song

doi:10.1016/j.lwt.2022.114217

Cited by 6 publications

(2 citation statements)

References 44 publications

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“…All samples exhibited a higher proportion of β‐sheet content compared to α‐helix, similar to a previous study (Han et al . 2022). This phenomenon can be attributed to the fact that α‐helix structures are primarily formed within proteins to enhance their stability, while β‐sheet structures are typically employed to form stable secondary domains that regulate protein functions.…”

Section: Resultsmentioning

confidence: 99%

Physicochemical, structural, and emulsifying properties of stable blended whey and soy protein colloidal dispersion prepared by pH‐shifting and ultrasound

Liu,

Gao,

Xia

et al. 2024

Int J of Dairy Tech

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This study investigated physiochemical, structural, and emulsifying properties of whey and soy protein blends (4%, w/v), which were combined at various proportions by pH‐shifting and ultrasound. The mixed dispersions exhibited small particle sizes (below 200 nm), with the smallest value observed at a sample with WPC to SPI ratio of 50:50. Reducing whey protein gave the blend lower surface hydrophobicity and higher α‐helix structure. More soy protein resulted in larger droplet size, lower surface charge, and greater flocculation of fabricated emulsions. Emulsions with soy protein lower than 50% were acceptable due to the nano‐scale size and small flocculation index.

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Section: Resultsmentioning

confidence: 99%

Physicochemical, structural, and emulsifying properties of stable blended whey and soy protein colloidal dispersion prepared by pH‐shifting and ultrasound

Liu,

Gao,

Xia

et al. 2024

Int J of Dairy Tech

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“…The surface hydrophobicity (H0) of a protein indicates the relative content of hydrophobic residues on its surface, and changing the protein tertiary structure by MTG affects the H0 value [27]. The surface hydrophobicity of CTL (2.25 ± 0.11 × 10 5 ) was significantly higher than that of MBPI (1.48 ± 0.10 × 10 5 ) (Figure 2).…”

Section: Surface Hydrophobicity (H0)mentioning

confidence: 99%

Effect of Microbial Transglutaminase Treatment on the Techno-Functional Properties of Mung Bean Protein Isolate

Moon

Cho

2023

Foods

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The purpose of this study was to investigate the improvement in techno-functional properties of mung bean protein isolate (MBPI) treated with microbial transglutaminase (MTG), including water- and oil-holding capacity, gelling properties, and emulsifying capacity. MBPI dispersions were incubated with MTG (5 U/g of protein substrate) at 45 °C with constant stirring for 4 h (MTM4) or 8 h (MTM8). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that MTG treatment for different durations increased the amount of high-molecular-weight proteins in MBPI, and most of the cross-linking by MTG was terminated at 8 h. Improved water-holding capacity, gelling properties, emulsifying capacity, and stability were observed after MTG treatment, and decreased protein solubility and surface hydrophobicity were observed. Furthermore, the texture of the heat-induced gels made from MTG-treated MBPI was evaluated using a texture analyzer. MTG treatment increased the hardness, gumminess, chewiness, and adhesiveness of the heat-induced gels. Field-emission scanning electron microscopy demonstrated the enhanced hardness of the gels. This research reveals that MTG-catalyzed cross-linking may adjust the techno-functional properties of MBPI, allowing it to be used as a soy protein alternative in food products, such as plant-based and processed meats.

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Pecan (Carya illinoinensis (Wangenh.) K. Koch) nuts as an emerging source of protein: extraction, physicochemical and functional properties

Cao,

Shi,

Wang

et al. 2024

J Sci Food Agric

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BACKGROUNDThe increasing demand for sustainable alternatives to traditional protein sources, driven by population growth, underscores the importance of protein in a healthy diet. Pecan (Carya illinoinensis (Wangenh.) K. Koch) nuts are currently underutilized as plant‐based proteins but hold great potential in the food industry. However, there is insufficient information available on pecan protein, particularly its protein fractions. This study aimed to explore the physicochemical and functional properties of protein isolate and the main protein fraction glutelin extracted from pecan nuts.RESULTSThe results revealed that glutelin (820.67 ± 69.42 g kg−1) had a higher crude protein content compared to the protein isolate (618.43 ± 27.35 g kg−1), while both proteins exhibited amino acid profiles sufficient for adult requirements. The isoelectric points of protein isolate and glutelin were determined to be pH 4.0 and pH 5.0, respectively. The denaturation temperature of the protein isolate (90.23 °C) was higher than that of glutelin (87.43 °C), indicating a more organized and stable conformation. This is further supported by the fact that the protein isolate had a more stable main secondary structure than glutelin. Both proteins demonstrated improved solubility, emulsifying, and foaming properties at pH levels deviating from their isoelectric points in U‐shaped curves. Compared to the protein isolate, glutelin displayed superior water and oil absorption capacity along with enhanced gelling ability.CONCLUSIONThe protein isolate and glutelin from pecan nuts exhibited improved stability and competitive functional properties, respectively. The appropriate utilization of these two proteins will support their potential as natural ingredients in various food systems. © 2024 Society of Chemical Industry.

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Modification of whey−soybean mixed protein by sequential high-pressure homogenization and transglutaminase treatment

Cited by 6 publications

References 44 publications

Physicochemical, structural, and emulsifying properties of stable blended whey and soy protein colloidal dispersion prepared by pH‐shifting and ultrasound

Physicochemical, structural, and emulsifying properties of stable blended whey and soy protein colloidal dispersion prepared by pH‐shifting and ultrasound

Effect of Microbial Transglutaminase Treatment on the Techno-Functional Properties of Mung Bean Protein Isolate

Pecan (Carya illinoinensis (Wangenh.) K. Koch) nuts as an emerging source of protein: extraction, physicochemical and functional properties

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