Heat-induced gelation of the mixtures of α-lactalbumin and β-lactoglobulin in the presence of glutathione

Legowo, Anang Mohamad; Imade, Tamotsu; Hayakawa, Shigeru

doi:10.1016/0963-9969(93)90064-p

Cited by 25 publications

(21 citation statements)

References 15 publications

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“…GSH can react with sulfhydryl group to form disulfide bonds and reduce intramolecular disulfide bonds to sulfhydryl groups. Reduction of disulfide bonds in lysozyme and alactalbumin is involved in conformational exchanges and subsequent exposure of hydrophobic regions, which promotes the interaction of proteins and ultimately leads to gel formation (Hayakawa & Nakamura, 1986;Legowo et al, 1993). The results obtained in the present study agreed well with the suggestion that the partial cleavage of the disulfide bonds in lysozyme, bovine serum albumin and a-lactalbumin was presumably better than full cleavage for the formation of a hard gel (Hayakawa & Nakamura, 1986;Hirose et al, 1990;Legowo et al, 1993).…”

Section: Resultssupporting

confidence: 88%

“…Reduction of disulfide bonds in lysozyme and alactalbumin is involved in conformational exchanges and subsequent exposure of hydrophobic regions, which promotes the interaction of proteins and ultimately leads to gel formation (Hayakawa & Nakamura, 1986;Legowo et al, 1993). The results obtained in the present study agreed well with the suggestion that the partial cleavage of the disulfide bonds in lysozyme, bovine serum albumin and a-lactalbumin was presumably better than full cleavage for the formation of a hard gel (Hayakawa & Nakamura, 1986;Hirose et al, 1990;Legowo et al, 1993). A small amount of GSH (1-2 mM) may improve reactivity of the free sulfhydryl group in serum albumin (Cys 34) resulting in considerable improvement of gel formation.…”

Section: Resultsmentioning

confidence: 99%

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Heat-Induced Gelation of Charcoal-Treated Serum Protein.

Hayakawa

2001

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The gel strength of charcoal-treated bovine serum and porcine serum proteins at a concentration of 8% was determined with different concentrations of NaCl after heating at 80˚C for 15 min at pH 7.0. The charcoal treatment considerably enhanced the gel strength of porcine serum protein, and also improved gel strength of bovine serum protein at NaCl concentrations between 75 mM and 150 mM. The gel strength of commercial PSA and BSA and that of fractionated bovine and porcine proteins by ion-exchange chromatography were also determined at a constant NaCl concentration. With the charcoal treatment, the gel strength of fractions containing albumin increased, while that containing globulin decreased. The gel strength of charcoal-treated bovine serum and porcine serum remarkably increased by the addition of the egg white, ovalbumin and glutathione. The promotion of gel formation with glutathione and ovalbumin seemed to result from the interaction between sulfhydryl groups in glutathione and ovalbumin and intramolecular disulfide bonds in the serum protein, thereby resulting in the highly organized matrix.

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Section: Resultssupporting

confidence: 88%

Section: Resultsmentioning

confidence: 99%

Heat-Induced Gelation of Charcoal-Treated Serum Protein.

Hayakawa

2001

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“…Reducing agents with the ability to interact with disulfide bonds and/or free SH groups can sharply alter the heat‐induced gel properties of globular proteins by modifying the mechanisms governing the gelation process (Matsudomi and others ; Legowo and others ; Hoffman and van Mill ; Zhang and others ). Free‐thiol compounds like dithiothreitol (DTT), β‐mercaptoethanol, glutathione, and cysteine (Cys) are commonly used with such purpose.…”

Section: Introductionmentioning

confidence: 99%

Heat‐Induced Gelation Mechanism of Blood Plasma Modulated by Cysteine

Saguer

Álvarez

Fort

et al. 2015

Journal of Food Science

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This work aims to determine changes at molecular level of plasma proteins provoked by adding cysteine (Cys, 0.025% to 0.35% w/v) as a reducing agent and their relationship with the heat-induced gel properties obtained when subsequently the solutions were submitted to a thermal treatment. Results show that adding Cys to plasma solutions at concentrations ≥0.15% actually entails modifications in the secondary structure of their main proteins, that is, serum albumin-α-helix rich-and globulin fraction-β-sheet rich. Basically, a reduction of the intensity of the infrared (IR) bands assigned to both structures takes place concomitant to an increase of extended structures that seem to act as intermediates for the subsequent protein aggregation process through nonnative intermolecular β-sheets. Cleavage of disulfide bonds is also evidenced at Cys concentrations ≥0.15% by nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), with the effects being directly proportional to Cys concentration. However, beneficial effects on gel hardness are gradually obtained at Cys concentrations ≤0.15%, that is, when the effects at molecular level are at most just budding, while not more improvements on this textural parameter are obtained at higher Cys concentrations. By contrast, water retention capacity is gradually diminishing as Cys concentration increases, but with a significant reduction only obtained at the highest tested concentration. These results suggest a negative effect of Cys on gel microstructure at high concentrations, which probably can be attributed to protein aggregation taking place at room temperature.

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“…The particular characteristics of milk gels, in which both major protein fractions (casein and serum) play an important role, are strongly related to manufacturing processes (22,23). The variations in physical properties of simple and mixed gels have often been attributed to variations in their microstructures, and therefore many studies have focused on the relationship between structure and mechanical properties (24)(25)(26)(27). Two instrumental techniques in particular; scanning (SEM) and transmission electron microscopy (TEM), have contributed to a better knowledge of dairy gels microstructure (28,29).…”

Section: Introductionmentioning

confidence: 99%