Improved heat stability of protein solutions and O/W emulsions upon dry heat treatment of whey protein isolate in the presence of low-methoxyl pectin

Hidayat, Chusnul; Vermeir, Lien; Martins, José; Meulenaer, Bruno De; Meeren, Paul Van der

doi:10.1016/j.colsurfa.2016.05.034

Cited by 36 publications

(31 citation statements)

References 54 publications

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“…The results obtained from NMR measurements were generally in agreement with those obtained by chemical analysis. SDS‐PAGE analysis performed in a previous study showed that dry‐heat treatment of WPI–LMP mixtures resulted in the formation of high molecular weight compounds (WPI–LMP conjugates) . In the same study, the degree of interaction between WPI and LMP was determined by measuring the availability of the primary amino group of WPI in the conjugates as a function of incubation time using the TNBS method .…”

Section: Discussionmentioning

confidence: 93%

“…In order to evaluate the influence of dry‐heat treatment on WPI, freeze‐dried WPI was dry‐heat treated up to 16 days. Previously, SDS‐PAGE analysis revealed that a limited protein polymerization occurred in dry‐heat‐treated WPI . Polymerization of protein leads to the formation of aggregates with higher molecular weight that diffuse slower.…”

Section: Resultsmentioning

confidence: 99%

“…SDS‐PAGE analysis performed in a previous study showed that dry‐heat treatment of WPI–LMP mixtures resulted in the formation of high molecular weight compounds (WPI–LMP conjugates) . In the same study, the degree of interaction between WPI and LMP was determined by measuring the availability of the primary amino group of WPI in the conjugates as a function of incubation time using the TNBS method . Compared with the results obtained from TNBS measurement, the degree of interaction between WPI and LMP obtained using NMR was higher: TNBS analysis indicated that after 16 days of dry‐heat treatment, WPI–LMP conjugates with a ratio 2:1 had a degree of conjugation of approximately 15%.…”

Section: Discussionmentioning

confidence: 99%

“…In previous studies, chemical analyses using reagents such as trinitrobenzenesulfonic acid (TNBS) and o ‐phthaldialdehyde were performed to determine the degree of covalent interaction between proteins and polysaccharides by determining the residual amount of available amino groups in the conjugates. Whereas these methods are sensitive, they are also highly labor intensive and time consuming.…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, the amount of free WPI and LMP‐bound WPI in the conjugates could be determined. The outcome of this study was evaluated by comparing the results to those obtained through sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE) and TNBS analysis in a previous study …”

Section: Introductionmentioning

confidence: 99%

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Quantification of the electrostatic and covalent interaction between whey proteins and low methoxyl pectin using PFG‐NMR diffusometry

Hidayat

Vermeir

Neve

et al. 2019

Magnetic Reson in Chemistry

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As interaction between proteins and polysaccharides is expected to change the average diffusion coefficient and the distribution width, it is believed that NMR diffusometry can be a useful tool to study and quantify the interaction between whey protein isolate (WPI) and low methoxyl pectin (LMP). For this purpose, the influence of pH, dry‐heat‐treatment duration, and WPI to LMP ratio on WPI and LMP interaction was evaluated using pulsed field gradient NMR. At pH 5.0 and 5.5, approximately 40–50% of the WPI present in the mixture interacted with LMP through electrostatic interaction. Hence, it is important to measure the degree of covalent interaction at a pH where electrostatic interaction between WPI and LMP is limited. The diffusion coefficient of WPI gradually decreased as the mixtures of WPI and LMP were incubated for 1, 2, 8, and 16 days, which was accompanied by an increase in the distribution width. With regard to the LMP concentration, the higher the LMP concentration, the higher the amount of WPI bound to LMP and the smaller the diffusion coefficient of WPI. Overall, the results indicate that NMR diffusometry enables the quantification of the interaction in biopolymer mixtures. Whereas the results showed a similar trend as that obtained via chemical analysis, pulsed field gradient NMR does not require any sample pretreatment.

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Section: Discussionmentioning

confidence: 93%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Quantification of the electrostatic and covalent interaction between whey proteins and low methoxyl pectin using PFG‐NMR diffusometry

Hidayat

Vermeir

Neve

et al. 2019

Magnetic Reson in Chemistry

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Functional and Engineered Colloids from Edible Materials for Emerging Applications in Designing the Food of the Future

Patel

2018

Adv Funct Materials

104

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Functional and engineered colloids fabricated from edible materials have recently gained a lot of interest for futuristic applications in the field of foods for purposes ranging from microstructure development to delivery of healthpromoting bioactives to manipulation of food-body interactions. This review tackles a very ambitious task of discussing the current understanding of functional colloids within the framework of foods. Physicochemical attributes of several novel complex colloids fabricated from natural, and often, underutilized edible materials are clearly and comprehensively reviewed in this paper. This review not only provides a scientific insight into the advances made in the field of colloid-based food structuring but also touches on the exciting future opportunities in this promising multidisciplinary field.

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Physicochemical and structural characterization of whey protein concentrate–tomato pectin conjugates

2023

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BACKGROUND Protein–pectin conjugates, obtained through a controlled Maillard reaction in blends of precursors, are studied for their contribution to improving the emulsifying and thermal properties of proteins. The objective was to obtain a conjugate between whey protein concentrate (WPC) and non‐conventional pectins extracted in acid (acid tomato pectin, ATP) and aqueous medium (water tomato pectin, WTP) from industrialized tomato residues (tomato waste, TW), characterize the conjugates and study their emulsion properties. The Maillard reaction was carried out at 60 °C and 75% relative humidity in blends with 2:1 proportions; 1:1 and 1:2 (mprotein:mpectin) for 3, 6 and 12 days. Conjugates were compared concerning treated and untreated WPC. RESULTS The WPC–ATP conjugate showed significant increases in color difference (ΔE). The electrophoresis profile of the conjugates showed diffuse bands of molecular weight between 37 and 250 kDa and a reduction in the intensity of bands characteristic of WPC (α‐lactalbumin and β‐lactoglobulin). Thermal analysis showed an increase in the peak temperature and a reduction in the enthalpy change in protein denaturation, associated with the formation of conjugates. The infrared spectroscopy of the conjugates, in the amide III zone (1300–1100 cm−1), indicated an increase in the relative peak area associated with the unfolding and exhibition of the hydrophobic zones of the WPC fraction. The emulsions formulated with the conjugates showed a significant increase in the emulsifying stability index (ESI) (P < 0.05) concerning the treated and untreated WPC emulsions. CONCLUSION The formation of conjugates increased the emulsifying properties and improved the thermal stability of WPC, showing an innovative and alternative food ingredient too. © 2023 Society of Chemical Industry.

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Improved heat stability of protein solutions and O/W emulsions upon dry heat treatment of whey protein isolate in the presence of low-methoxyl pectin

Cited by 36 publications

References 54 publications

Quantification of the electrostatic and covalent interaction between whey proteins and low methoxyl pectin using PFG‐NMR diffusometry

Quantification of the electrostatic and covalent interaction between whey proteins and low methoxyl pectin using PFG‐NMR diffusometry

Functional and Engineered Colloids from Edible Materials for Emerging Applications in Designing the Food of the Future

Physicochemical and structural characterization of whey protein concentrate–tomato pectin conjugates

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