Ethyl-substituted .beta.-casein. Study of differences between esterified and reductively alkylated .beta.-casein derivatives

Chobert, J.M.; Touati, Abdelmadjid; Bertrand-Harb, C.; Dalgalarrondo, Michèle; Nicolas, Marie Georgette; Haertlé, Tomasz

doi:10.1021/jf00096a006

Cited by 13 publications

(10 citation statements)

References 19 publications

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“…The measured solubility of b-casein esters agrees well with previous results of Chobert et al [18], albeit the shift in isoelectric points was relatively more important in the present work, probably because of difference in reaction conditions used to prepare ester derivatives [20]. On the other hand, the results obtained with b-lactoglobulin partially agree with those of Mattarella and Richardson [16] and especially those concerning the decreased solubility of esterified samples in the alkaline pH-range.…”

Section: Protein Solubilitysupporting

confidence: 92%

“…The second effect is more prominent in case of derivatives with a low degree of esterification and when the grafted ester groups are more hydrophobic (e. g. propyl). This may explain well the reduced solubility reported in case of some esterified proteins at acid pHs [16,18].…”

Section: Protein Solubilitysupporting

confidence: 69%

“…Similar features were observed during esterification of b-casein [18]. The magnitude of the change in the isoionic point values depends on the degree of esterification [18][19][20]. Alternatively, methyl and ethyl esterification of b-lactoglobulin resulted in randomized protein structures [21].…”

Section: Introductionmentioning

confidence: 67%

“…The isoionic point of b-lactoglobulin was raised from 5.2 to 6.2, 8.7 and 9.8 after its esterification with butanol, ethanol and methanol, respectively [16,17]. Similar features were observed during esterification of b-casein [18]. The magnitude of the change in the isoionic point values depends on the degree of esterification [18][19][20].…”

Section: Introductionmentioning

confidence: 82%

“…Hence, esterified b-lactoglobulins were more efficient in lowering the interfacial tension at the oil/water interface as a result of increased surface hydrophobicity [17]. It was reported also that emulsifying activity of esterified b-lactoglobulins is worse than that of the native form [16,18]. This discrepancy might be due to different pH or any other limiting factors used in each study.…”

Section: Introductionmentioning

confidence: 91%

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Improvement of solubility and of emulsifying properties of milk proteins at acid pHs by esterification

Sitohy

Chobert²,

Haertlé³

2001

Nahrung

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Three milk proteins (beta-lactoglobulin, alpha-lactalbumin and beta-casein) were esterified to different extents with methanol, ethanol and propanol, then their solubility was studied in the pH-range of 3-10. Their emulsifying properties were also checked in the pH-range of 3-7 by measuring the oil-droplet size using laser light scattering. Solubility of all esterified proteins was improved in the acidic pH range (3-6). The magnitude of improvement was depending on the extent of esterification, the nature of the grafted ester group and the nature of the modified protein. Emulsifying activity and stability of esterified milk proteins in the acidic pH range of 3-5 were generally higher compared to the corresponding native proteins. This improvement was associated with the degree of solubility, the degree of esterification, the type of ester group grafted and the nature of the used protein. The highest emulsifying activity improvement was observed for methyl ester derivatives at pH 5 where the native proteins have poor emulsifying properties.

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Section: Protein Solubilitysupporting

confidence: 92%

Section: Protein Solubilitysupporting

confidence: 69%

Section: Introductionmentioning

confidence: 67%

Section: Introductionmentioning

confidence: 82%

Section: Introductionmentioning

confidence: 91%

See 3 more Smart Citations

Improvement of solubility and of emulsifying properties of milk proteins at acid pHs by esterification

Sitohy

Chobert²,

Haertlé³

2001

Nahrung

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Effect of protein‐flavour binding on flavour delivery and protein functional properties: A special emphasis on plant‐based proteins

Wang

Arntfield

2016

Flavour & Fragrance J

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As the loss of free volatile compounds in aqueous protein systems is known to greatly influence the quality, and therefore the consumer acceptability, of protein‐containing foods, examination of the ability of different proteins to react with volatile flavour compounds as well as the nature of the interaction are of great interest to flavour chemists. It is generally believed that the affinity of flavour to proteins is a multi‐factor function related to protein source, protein conformation and stereochemistry of the flavour compound. However, the nature of protein‐flavour interactions has not been explicit. Less focus has been put on plant‐based proteins in comparison to animal proteins. With an increase in the use of plant‐based proteins in food systems, this article provides a fundamental review of the impact protein‐flavour interactions on flavour retention and release with a special emphasis on plant protein materials. Flavour‐food matrix interactions have been examined with a focus on how they influence flavour perception. Current knowledge on methodologies involved in protein‐flavour binding studies, binding mechanisms and factors affecting the interaction have been discussed. The implication of protein‐flavour interaction on protein functionality specifically protein thermal gelation properties has also been considered. Copyright © 2016 John Wiley & Sons, Ltd.

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Solubility and reactivity of caseins and β-lactoglobulin in protic solvents

Touati¹,

Creuzenet²,

Chobert³

et al. 1992

J Protein Chem

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The study of the solubility of unstructured proteins (alpha s1-, beta-, and kappa-casein) and well-structured globulin (beta-lactoglobulin) in low water binary solvent systems demonstrated the crucial importance of solvent polarity and neutralization of protein polar functions on the final outcome of solubility experiments. The solubilities up to 38, 56, and 96% in CHCl3/CH3OH (1/1, v/v) acidified with HCl and up to 5, 10, and 25% in CHCl3/CH3OH (1/1, v/v) in the presence of triethylamine (TEA) were obtained for kappa-, alpha s1-, and beta-casein, respectively. The importance of protein charge neutralization was apparent when the solubilization was performed in basified CHCl3/CH3OH media, giving the optimal results when the studied proteins were brought before to their isoionic point. The maximum solubility of beta-casein at its pI in 30-70% methanol in CHCl3 was reaching 50-60% with triethylamine (TEA) added. beta-lactoglobulin could be solubilized up to 70% in CHCl3/CH3OH (7/3, v/v) acidified with HCl and up to 40% in CHCl3/CH3OH (3/7, v/v) in the presence of TEA. The observed yield of reductive alkylation of beta-lactoglobulin was much higher (98%) when performed in studied solvent system than in aqueous conditions (75%). Apparently, steric hindrance of the well-folded beta-barrel (in aqueous conditions) structure masks the portion of epsilon-NH2 groups. In the case of unstructured aqueous media beta-casein, 90% alkylation yields were obtained in organic and aqueous conditions.

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Ethyl-substituted .beta.-casein. Study of differences between esterified and reductively alkylated .beta.-casein derivatives

Cited by 13 publications

References 19 publications

Improvement of solubility and of emulsifying properties of milk proteins at acid pHs by esterification

Improvement of solubility and of emulsifying properties of milk proteins at acid pHs by esterification

Effect of protein‐flavour binding on flavour delivery and protein functional properties: A special emphasis on plant‐based proteins

Solubility and reactivity of caseins and β-lactoglobulin in protic solvents

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