Kinetic and thermodynamic analysis of ultra-high pressure and heat-induced denaturation of bovine serum albumin by surface plasmon resonance

Wang, Wei; Zhu, Yiwu; Chen, Tianhao; Zhou, Guanghong

doi:10.4314/tjpr.v16i8.29

Cited by 11 publications

(5 citation statements)

References 20 publications

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“…The aggregation may be due to high pressure causing protein unfolding and/or aggregation. By forming new disulfide bonds, complex aggregates are formed, resulting in aggregation of protein subunits [32], which is consistent with the changing trend of flexibility.…”

Section: Effect Of Homogenization Pressures On Particle Size Distribusupporting

confidence: 67%

Effects of homogenization on the molecular flexibility and emulsifying properties of soy protein isolate

Guo-Rong²,

Wang

et al. 2018

Food Sci Biotechnol

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The sensitivity of soy protein isolate (SPI) to trypsin was characterized by its flexibility. The effects of different homogenization conditions on soy protein isolate flexibility and emulsifying properties were investigated. Set the homogenization pressure was 120 MPa (megapascal) and the homogenous number of times is 0-4 times, the flexibility increases with the increase of the homogenization times (0-3 times), the change trend of flexibility is not obvious (3-4 times). When the homogenization times was 0-3 times, the emulsifying activity increases, and the emulsifying activity was the strongest at 3 times, after homogenization 3 times, the change trend of emulsifying activity is not obvious, the trend of emulsification stability and emulsification activity were similar. The surface hydrophobicity increases with the increase of homogenization times, while the turbidity decreases. The other structural indicators such as Ultraviolet scanning and endogenous tryptophan fluorescence spectroscopy suggest that the structure of SPI becomes more stretch as the flexibility increases.

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Section: Effect Of Homogenization Pressures On Particle Size Distribusupporting

confidence: 67%

Effects of homogenization on the molecular flexibility and emulsifying properties of soy protein isolate

Guo-Rong²,

Wang

et al. 2018

Food Sci Biotechnol

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“…A pressure range of 100–400 MPa led to the exposure of the SH group and the loss of tertiary structure in BSA. Pressures of 800 MPa and a prolonged holding time caused the aggregation of BSA by SS bonds via SS–SH interchange, resulting in the α‐helix being replaced with disordered structures, turns, and intermolecular β‐sheet aggregates (De Maria et al., 2016; Huppertz et al., 2019; W. Wang et al., 2017).…”

Section: Effect Of Hhp On the Modification Of Wpsmentioning

confidence: 99%

Factors affecting the modification of bovine milk proteins in high hydrostatic pressure processing: An updated review

Gharbi

Marciniak

Doyen

2022

Comp Rev Food Sci Food Safe

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High hydrostatic pressure (HHP) treatment induces structural changes in bovine milk proteins depending on factors such as the temperature, pH, concentration, decompression rate, cycling, composition of the medium and pressure level and duration. An in-depth understanding of the impact of these factors is important for controlling HHP-induced modification of milk proteins and the interactions within or between them, which can be applied to prevent undesired aggregation, gelation, and precipitation during HHP processing or to obtain specific milk protein modifications to attain specific protein properties. In this regard, understanding the influences of these factors can provide insight into the modulation and optimization of HHP conditions to attain specific milk protein structures. In recent years, there has been a great research attention on HHP-induced changes in milk proteins influenced by factors such as pH, temperature, concentration, cycling, decompression condition, and medium composition. Hence, to provide insight into how these factors control milk protein structures under HHP treatment and to understand if their effects depend on HHP parameters and environmental conditions, this review discusses recent findings on how various factors (pH, temperature, cycling, decompression rate, medium composition, and concentration) affect HHP-induced bovine milk protein modification. K E Y W O R D Sbovine milk proteins, high hydrostatic pressure, structural changes Practical Application: The information provided in this review will be very useful to anticipate the challenges related to the formulation and development of pressure-treated milk and dairy products.

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“…However, because high pressure and shear forces cause violent collisions, which makes the particles in the system more regular, 37 when the homogenization pressure was increased to 90 and 120 MPa, the particle size distribution of the SPI returned to multimodal distributions, respectively. Thus, the higher homogenization pressure caused the protein to aggregate, which makes the complex particle size increase 38 …”

Section: Resultsmentioning

confidence: 99%

“…Thus, the higher homogenization pressure caused the protein to aggregate, which makes the complex particle size increase. 38 As shown in Fig. 1(C), after SPI undergoes HPH, the SPI-lutein nanocomplexes were negatively charged.…”

Section: Average Particle Size and ζ-Potential Analysesmentioning

confidence: 89%

Characteristics and structure of a soy protein isolate–lutein nanocomplex produced via high‐pressure homogenization

Yang

Xie

et al. 2022

J Sci Food Agric

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BACKGROUND In recent years, nanocarriers for transporting active substances have attracted attention. This study was to explore the soy protein isolate (SPI) after high‐pressure homogenization (HPH) (0, 30, 60, 90 and 120 MPa) as potential lutein carriers. RESULTS The load amount (LA) and encapsulation efficiency (EE) of the SPI–lutein nanocomplexes at a homogenization pressure of 60 MPa were the highest (2.32 mg mL−1 and 92.85%, respectively), and the average particle size and ζ‐potential of the SPI–lutein nanocomplexes were 192.1 nm and −30.06 mV, respectively. The DPPH (2,2‐diphenyl‐1‐picrylhydrazyl) and hydroxyl‐antioxidant activities of the complex increased from 12.4% and 23.3% to 52.7% and 61.07%, respectively, after the protein was treated with HPH. The surface hydrophobicity of the SPI and the SPI–lutein nanocomplexes increased with increasing homogenization pressure treatment. Fourier transform‐infrared spectrophotometry analyses suggested that the homogenization treatments resulted in partial unfolding of the protein molecules, and the addition of lutein can also lead to the change of protein secondary structure. The fluorescence emission of SPI was quenched by lutein through the static quenching mechanism. Fluorescence experiments revealed that SPI and lutein had the strongest binding ability through hydrophobic interaction at a homogenization pressure of 60 MPa. CONCLUSION After HPH, the combination of SPI and lutein was beneficial, and the stability of lutein also improved after the combination. This study is conducive to expanding the application of soybean protein in the food industry. © 2022 Society of Chemical Industry.

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Kinetic and thermodynamic analysis of ultra-high pressure and heat-induced denaturation of bovine serum albumin by surface plasmon resonance

Cited by 11 publications

References 20 publications

Effects of homogenization on the molecular flexibility and emulsifying properties of soy protein isolate

Effects of homogenization on the molecular flexibility and emulsifying properties of soy protein isolate

Factors affecting the modification of bovine milk proteins in high hydrostatic pressure processing: An updated review

Characteristics and structure of a soy protein isolate–lutein nanocomplex produced via high‐pressure homogenization

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