Spectroscopic analysis on the binding interaction between tetracycline hydrochloride and bovine proteins β-casein, α-lactalbumin

Bi, Hongna; Tang, Lin; Gao, Xin; Jia, Jingjing; Lv, Henghui

doi:10.1016/j.jlumin.2016.05.048

Cited by 78 publications

(17 citation statements)

References 36 publications

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“…Robbins and Holmes 38 reported that α-LA native is formed by 25−26% α-helix, 14− 15% β-strand by 60% random structure, which is in agreement with the results obtained in this study and shown in Table 1 for native α-LA at pH 7. Similar results were recently obtained by Bi et al 39 At pH 3 and 5, structural transitions from α-helix to random structure were observed when 16 and 18 C chains were incorporated. The opposite happened at pH 7 and 10.…”

Section: ■ Results and Discussionsupporting

confidence: 90%

Chemical Lipophilization of Bovine α-Lactalbumin with Saturated Fatty Acyl Residues: Effect on Structure and Functional Properties

Mendoza-Sánchez

Jiménez‐Fernández

Melgar‐Lalanne

et al. 2019

J. Agric. Food Chem.

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Bovine α-lactalbumin (α-LA) was chemically modified by the covalent attachment of fatty acid residues of different length (lauroyl, palmitoyl, and stearoyl) to modify its functional and antioxidant properties. Structural changes, functional properties, and antioxidant capacity in the pH interval between 3 and 10 were analyzed. Surface properties were improved. The esterification increased the hydrophobic interactions leading to a reduction in the solubility dependent on the incorporation ratio of the fatty acid residues. Improvement in emulsifying, foaming, and antioxidant properties were observed when the length of the fatty acid chains was short and mostly at a basic pH. With these results in mind, experiments could be conducted for the technological applications of these derivatives in the food, pharmaceutical, and cosmetic industries.

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Section: ■ Results and Discussionsupporting

confidence: 90%

Chemical Lipophilization of Bovine α-Lactalbumin with Saturated Fatty Acyl Residues: Effect on Structure and Functional Properties

Mendoza-Sánchez

Jiménez‐Fernández

Melgar‐Lalanne

et al. 2019

J. Agric. Food Chem.

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“…For the surface hydrophobicity study, the 8-anilino-1-naphthalenesulfonic acid (ANS) fluorescent probe was used (Bi, Tang, Gao, Jia, & Lv, 2016). For each suspension studied, increasing volumes of the probe (20 mg/L) ranging from 10 to 30 μL were added to 4.0 ml of the suspension.…”

Section: Measurement Of Surface Hydrophobicitymentioning

confidence: 99%

Spray-drying of protein/polysaccharide complexes: Dissociation of the effects of shearing and heating

et al. 2019

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“…A possible explanation for this initial decrease in S 0 would be the onset of aggregation where the non‐native protein fraction aggregated primarily due to the segregative effect of the polysaccharide, and the native fraction will be probed thereafter. Nevertheless, increasing the concentration of LMP up to the turbidity peak at 1.0 g/L (Figure ) produced an increase in S 0 , which could be associated with the exposure of the hydrophobic sites of the protein (Bi, Tang, Gao, Jia, & Lv, ). The decrease in S 0 for high concentrations of LMP from 2.0 g/L can be correlated with the masking of the hydrophobic sites of the protein, which could be associated with the increase of the size of aggregates (Benichou et al, ).…”

Section: Resultsmentioning

confidence: 99%

Influence of low methoxyl pectin on the physicochemical properties of sodium caseinate‐stabilized emulsions

Wang

Souihi

Amara

et al. 2018

J Food Process Engineering

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Two strategies of emulsion preparation, stabilization by sodium caseinate (CAS)/low methoxyl pectin (LMP) complexes formed in advance, and stabilization by the layer‐by‐layer (LBL) method, were compared. In aqueous solution, at a constant CAS concentration (5 g/L), the gradual addition of LMP resulted in an increase in turbidity of the solution caused by the increasing formation of insoluble complexes. The zeta potential change showed that the interactions are mainly due to an electrostatic mechanism. The spectrofluorometric studies as well as the spectroscopic analysis in the UV–visible region have shown that the interactions with LMP caused a change in the secondary and tertiary structures of the protein. Then, these complexes were used for stabilizing oil/water emulsions. The emulsions stabilized by complexes formed in advance and LBL method were characterized by measuring zeta potential, dynamic viscosity, serum index, and particle size distribution. The results showed that, at low LMP concentrations, complexes‐stabilized emulsions were more stable than LBL‐stabilized ones, while at high LMP concentrations, LBL‐stabilized emulsions showed better stability. Practical applications These results would be useful during the development of encapsulation systems having hybrid interfaces in order to better control the release of hydrophobic active molecules like essential oils. These molecules have various benefits like antioxidant and antimicrobial activities, which could be exploited for food biopreservation. One of the major problems for application in food preservation of these active molecules is their great sensitivity to the environmental stress (temperature, pH…), their low water‐solubility, their interactions with food components, and their pronounced odor and flavor. The encapsulation of these molecules in the developed emulsions containing the proper concentration of LMP could be a suitable solution to protect and release these lipophilic molecules in foods.

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Spectroscopic analysis on the binding interaction between tetracycline hydrochloride and bovine proteins β-casein, α-lactalbumin

Cited by 78 publications

References 36 publications

Chemical Lipophilization of Bovine α-Lactalbumin with Saturated Fatty Acyl Residues: Effect on Structure and Functional Properties

Chemical Lipophilization of Bovine α-Lactalbumin with Saturated Fatty Acyl Residues: Effect on Structure and Functional Properties

Spray-drying of protein/polysaccharide complexes: Dissociation of the effects of shearing and heating

Influence of low methoxyl pectin on the physicochemical properties of sodium caseinate‐stabilized emulsions

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