Improving albumen thermal stability using succinylation reaction with octenyl succinic anhydride

Kulchaiyawat, Charlwit; Wang, Tong; Zhengkang, Han

doi:10.1016/j.lwt.2016.07.003

Cited by 16 publications

(3 citation statements)

References 36 publications

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“…This result suggests that succinylation can prevent the ion-induced aggregation of EWP. This phenomenon is similar to the result for succinylated albumin that was reported by previous research [6].…”

Section: Resultssupporting

confidence: 93%

“…According to previous study [5], high-pressure treatment (550 MPa) for 20 min can inhibit the formation of insoluble aggregates in the EWP solution, while high-pressure treatment can have negative effects on rheological properties and color. As reported by Kulchaiyawat, Wang, and Han [6], succinylation by octenyl succinic anhydride can improve the thermal stability of albumen; however, the reason for the improvement of thermal stability has not been further investigated. The succinylation process the advantages of high efficiency and, with the method of high pressure treatment, succinylation will be more practicable and effective when compared with the addition of arginine.…”

Section: Introductionmentioning

confidence: 99%

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Succinylation Improves the Thermal Stability of Egg White Proteins

Tong

2019

Molecules

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Succinylation can improve the thermal stability of various proteins. In this study, succinylated egg white protein (SEWP) samples with different succinylation degrees were prepared by adding various succinic anhydride additives to egg white protein (EWP). The thermal stability of SEWP and the conformational structure under various succinylation degrees were investigated. With the increase in succinylation degree, the turbidity of heated SEWP solution (90 °C for 30 min) markedly declined. The heated SEWP solution with high succinylation degree (37.63%, 66.57%, and 72.37%) was transparent. Moreover, the result of differential scanning calorimetry confirmed that the thermal stability of succinylated EWP increased. The results of intrinsic fluorescence spectra and Fourier-transform infrared spectroscopy illustrate that succinylation changed the conformational structure of EWP. Succinylation increased the electrostatic repulsion and decreased the surface hydrophobicity, and it changed the aggregation morphology of EWP. Cross-linked spherical aggregates of low succinylation degree transformed to thready aggregates of a high succinylation degree. Thus, succinylation improved the thermal stability of EWP.

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Section: Resultssupporting

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Succinylation Improves the Thermal Stability of Egg White Proteins

Tong

2019

Molecules

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“…Recently, octenyl succinic anhydride-modified fish skin gelatin was synthesized and applied to form a stable emulsion for the delivery of lipophilic bioactive substances [ 20 ]. An increase in the chain length of the alkenyl derivatives could impart greater thermal stability [ 22 ], surface activity and mechanical properties of the films [ 23 ] to proteins. Additionally, through the formation of a linear amphiphile to stabilize the interface of the oil–water system, the hydrophobic modification of hydrophilic biomacromolecules might also form a self-aggregate through the aid of hydrophobic interaction in the water system [ 24 ].…”

Section: Introductionmentioning

confidence: 99%

Curcumin-Loaded Self-Assembly Constructed by Octenylsuccinate Fish (Cyprinus carpio L.) Scale Gelatin: Preparation and Characterization

Mustapha

et al. 2022

Foods

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Curcumin loaded octenylsuccinate fish scale gelatin (OFSG) was prepared in this study, to explore the potential of FSG for delivering hydrophobic nutrients. The effects of molecule weight (Mw, 22,677–369 g/mol) and degree of substitution (DS, 0–0.116) on the curcumin loading efficiency (CLE, μg/mL) of OFSG (6.98–26.85 mg/mL) were evaluated. The expose of interior hydrophobic groups in FSG and increased intermolecular hydrophobic area contributed to the loading of curcumin in two phases, respectively. The interaction between OFSG and curcumin showed a decreased absorption in FTIR and an increased crystallinity in XRD. The loading of curcumin into OFSG caused a significant decrease of the particle size (from 350–12,070 to 139–214 nm), PDI (from 0.584–0.659 to 0.248–0.347) and ζ-potential (−12.2 or −11.4 to −21.0 or −20.3). OFSG showed a significantly higher stability and lower release of curcumin than FSG at the end of the simulated gastrointestinal digestion. Thus, OFSG showed great potential in the construction of a carrier for hydrophobic nutrients.

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Investigation into the chemical modification of α-amylase using octenyl succinic anhydride: enzyme characterisation and stability studies

Danait-Nabar

2023

Bioprocess Biosyst Eng

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Improving albumen thermal stability using succinylation reaction with octenyl succinic anhydride

Cited by 16 publications

References 36 publications

Succinylation Improves the Thermal Stability of Egg White Proteins

Succinylation Improves the Thermal Stability of Egg White Proteins

Curcumin-Loaded Self-Assembly Constructed by Octenylsuccinate Fish (Cyprinus carpio L.) Scale Gelatin: Preparation and Characterization

Investigation into the chemical modification of α-amylase using octenyl succinic anhydride: enzyme characterisation and stability studies

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