Interaction between trypsin and alginate: An ITC and DLS approach to the formation of insoluble complexes

Braia, Mauricio; Loureiro, Dana Belén; Tubío, Gisela; Lienqueo, María Elena; Romanini, Diana

doi:10.1016/j.colsurfb.2017.04.033

Cited by 16 publications

(8 citation statements)

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“…Previously, the particle size distribution of alginate−protein complexes has been determined by DLS. 16,26,40 However, the protein alginate interactions at pH 2.65 and 4.0 led to large particles that phase-separated and sedimented rapidly. Therefore, a Master- sizer flow-through cell and laser diffraction was used for the precipitating systems, while alginates and proteins were analyzed individually by conventional DLS (Figure 4A).…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…Alginate and β-Lg have been reported to form smaller particles at pH 2.0 (200 nm) than at pH 4.0 (1000–5000 nm). , The particle size distribution was determined to elucidate if this pertains to the higher ionic strength used in the present study and if it was influenced by the M/G ratio. Previously, the particle size distribution of alginate–protein complexes has been determined by DLS. ,, However, the protein alginate interactions at pH 2.65 and 4.0 led to large particles that phase-separated and sedimented rapidly. Therefore, a Mastersizer flow-through cell and laser diffraction was used for the precipitating systems, while alginates and proteins were analyzed individually by conventional DLS (Figure A).…”

Section: Resultsmentioning

confidence: 99%

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Impact of Alginate Mannuronic-Guluronic Acid Contents and pH on Protein Binding Capacity and Complex Size

et al. 2021

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Alginates, serving as hydrocolloids in the food and pharma industries, form particles at pH < 4.5 with positively charged proteins, such as β-lactoglobulin (β-Lg). Alginates are linear anionic polysaccharides composed of 1,4-linked β-d-mannuronate (M) and α-l-guluronate (G) residues. The impact of M and G contents and pH is investigated to correlate with the formation and size of β-Lg alginate complexes under relevant ionic strength. It is concluded, using three alginates of M/G ratios 0.6, 1.1, and 1.8 and similar molecular mass, that β-Lg binding capacity is higher at pH 4.0 than at pH 2.65 and for high M content. By contrast, the largest particles are obtained at pH 2.65 and with high G content. At pH 4.0 and 2.65, the stoichiometry was 28–48 and 3–10 β-Lg molecules bound per alginate, respectively, increasing with higher M content. The findings will contribute to the design of formation of the desired alginate–protein particles in the acidic pH range.

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Section: ■ Results and Discussionmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Impact of Alginate Mannuronic-Guluronic Acid Contents and pH on Protein Binding Capacity and Complex Size

et al. 2021

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“…On the other hand, biochemical and biophysical techniques are attractive and developed dramatically to be the first choice in studying biomolecular interactions. Examples include spectroscopic techniques [13][14][15][16][17][18], surface plasma resonance (SPR) [19][20][21], isothermal titration calorimetry (ITC) [22][23][24] and microscale thermophoresis (MST) [25][26][27]. This review will discuss thermophoresis in the characterization of biomolecular interactions.…”

Section: Introductionmentioning

confidence: 99%

Thermophoresis for characterizing biomolecular interaction

Asmari

Ratih

Alhazmi

et al. 2018

Methods

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The study of biomolecular interactions is crucial to get more insight into the biological system. The interactions of protein-protein, protein-nucleic acids, protein-sugars, nucleic acid-nucleic acids and protein-small molecules are supporting therapeutics and technological developments. Recently, the development in a large number of analytical techniques for characterizing biomolecular interactions reflect the promising research investments in this field. In this review, microscale thermophoresis technology (MST) is presented as an analytical technique for characterizing biomolecular interactions. Recent years have seen much progress and several applications established. MST is a powerful technique in quantitation of binding events based on the movement of molecules in microscopic temperature gradient. Simplicity, free solutions analysis, low sample volume, short analysis time, and immobilization free are the MST advantages over other competitive techniques. A wide range of studies in biomolecular interactions have been successfully carried out using MST, which tend to the versatility of the technique to use in screening binding events in order to save time, cost and obtained high data quality.

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“…ITC is a direct and common technique for investigating biomolecular interactions, evaluating thermodynamics of ligand-protein interactions and studying the binding constant. 20,21 Here, the ITC has been used to study the combination of TGB-HSA and TGB-BSA, respectively. The calorimetric titration data at pH 7.4 and 298 K are shown in Fig.…”

Section: Characterization Of the Tgb-hsa And Tgb-bsa Bindingmentioning

confidence: 99%

Insights into the interaction mechanism between tiagabine hydrochloride and two serum albumins

2018

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Interaction between trypsin and alginate: An ITC and DLS approach to the formation of insoluble complexes

Cited by 16 publications

References 19 publications

Impact of Alginate Mannuronic-Guluronic Acid Contents and pH on Protein Binding Capacity and Complex Size

Impact of Alginate Mannuronic-Guluronic Acid Contents and pH on Protein Binding Capacity and Complex Size

Thermophoresis for characterizing biomolecular interaction

Insights into the interaction mechanism between tiagabine hydrochloride and two serum albumins

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