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Coagulation of β-conglycinin, glycinin and isoflavones induced by calcium chloride in soymilk.

Hsiao YH, Yu CJ, Li WT, Hsieh JF - Sci Rep (2015)

Bottom Line: Isoflavones, including daidzein and genistein, were also coagulated into the SPF after the addition of 5 mM calcium chloride.The amounts of daidzein and genistein in the SSF decreased to 39.4 ± 1.6 and 11.8 ± 7.0%, respectively.HPLC analysis suggested that daidzein and genistein were bound with 7S and 11S proteins and then were coprecipitated into the SPF by 5 mM calcium chloride.

View Article: PubMed Central - PubMed

Affiliation: 1] Department of Food Science, Fu Jen Catholic University, Taipei 242, Taiwan [2] Ph.D. Program in Nutrition &Food Science, Fu Jen Catholic University, Taipei 242, Taiwan.

ABSTRACT
The coagulation of β-conglycinin (7S), glycinin (11S) and isoflavones induced by calcium chloride was investigated. Approximately 92.6% of the soymilk proteins were coagulated into the soymilk pellet fraction (SPF) after the addition of 5 mM calcium chloride. SDS-PAGE and two-dimensional electrophoresis analysis indicated that most of the 7S (α', α and β), 11S acidic (A1a, A1b, A2, A3 and A4) and 11S basic (B1a) proteins in the SSF were coagulated into the SPF after treatment with 5 mM calcium chloride. Isoflavones, including daidzein and genistein, were also coagulated into the SPF after the addition of 5 mM calcium chloride. The amounts of daidzein and genistein in the SSF decreased to 39.4 ± 1.6 and 11.8 ± 7.0%, respectively. HPLC analysis suggested that daidzein and genistein were bound with 7S and 11S proteins and then were coprecipitated into the SPF by 5 mM calcium chloride.

No MeSH data available.


Changes in the isoflavones contents with different amounts of calcium chloride (0, 2.5, 5, 7.5 or 10 mM) at 30 °C for 1 h.Vertical bars represent standard deviations.
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f7: Changes in the isoflavones contents with different amounts of calcium chloride (0, 2.5, 5, 7.5 or 10 mM) at 30 °C for 1 h.Vertical bars represent standard deviations.

Mentions: The effects of calcium chloride on the coagulation of isoflavones were also evaluated. The isoflavones extracted from soymilk were incubated with 0–10 mM of calcium chloride. However, no significant changes in the amounts of daidzin, daidzein, genistein, genistin and glycitin in supernatant were observed (Fig. 7). This result indicated that isoflavones were not immediately coagulated with calcium chloride. As previously mentioned, isoflavones including daidzin, daidzein and genistein were isolated from dried 7S and 11S proteins. The presence of daidzin, daidzein and genistein in the 7S and 11S proteins are evidence that daidzin, daidzein and genistein bind to the 7S and 11S proteins. The isoflavones may coprecipitate with proteins because of the surface hydrophobicity of the protein and its ability to interact with isoflavones28. Li and Hagerman29 suggested that the hydrophobic pocket between bovine serum albumin subdomains IIA and IIIA is the binding site for epigallocatechin-3-O-gallate. The interaction between flavanols and amino acids has also been reported. For example, glycine binds with the oxidized B-ring of catechin through the formation of Schiff bases30. Therefore, our results suggested that daidzein and genistein and a portion of daidzin, were bound with 7S and 11S proteins and then coprecipitated into the SPF by 5 mM calcium chloride.


Coagulation of β-conglycinin, glycinin and isoflavones induced by calcium chloride in soymilk.

Hsiao YH, Yu CJ, Li WT, Hsieh JF - Sci Rep (2015)

Changes in the isoflavones contents with different amounts of calcium chloride (0, 2.5, 5, 7.5 or 10 mM) at 30 °C for 1 h.Vertical bars represent standard deviations.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4542527&req=5

f7: Changes in the isoflavones contents with different amounts of calcium chloride (0, 2.5, 5, 7.5 or 10 mM) at 30 °C for 1 h.Vertical bars represent standard deviations.
Mentions: The effects of calcium chloride on the coagulation of isoflavones were also evaluated. The isoflavones extracted from soymilk were incubated with 0–10 mM of calcium chloride. However, no significant changes in the amounts of daidzin, daidzein, genistein, genistin and glycitin in supernatant were observed (Fig. 7). This result indicated that isoflavones were not immediately coagulated with calcium chloride. As previously mentioned, isoflavones including daidzin, daidzein and genistein were isolated from dried 7S and 11S proteins. The presence of daidzin, daidzein and genistein in the 7S and 11S proteins are evidence that daidzin, daidzein and genistein bind to the 7S and 11S proteins. The isoflavones may coprecipitate with proteins because of the surface hydrophobicity of the protein and its ability to interact with isoflavones28. Li and Hagerman29 suggested that the hydrophobic pocket between bovine serum albumin subdomains IIA and IIIA is the binding site for epigallocatechin-3-O-gallate. The interaction between flavanols and amino acids has also been reported. For example, glycine binds with the oxidized B-ring of catechin through the formation of Schiff bases30. Therefore, our results suggested that daidzein and genistein and a portion of daidzin, were bound with 7S and 11S proteins and then coprecipitated into the SPF by 5 mM calcium chloride.

Bottom Line: Isoflavones, including daidzein and genistein, were also coagulated into the SPF after the addition of 5 mM calcium chloride.The amounts of daidzein and genistein in the SSF decreased to 39.4 ± 1.6 and 11.8 ± 7.0%, respectively.HPLC analysis suggested that daidzein and genistein were bound with 7S and 11S proteins and then were coprecipitated into the SPF by 5 mM calcium chloride.

View Article: PubMed Central - PubMed

Affiliation: 1] Department of Food Science, Fu Jen Catholic University, Taipei 242, Taiwan [2] Ph.D. Program in Nutrition &Food Science, Fu Jen Catholic University, Taipei 242, Taiwan.

ABSTRACT
The coagulation of β-conglycinin (7S), glycinin (11S) and isoflavones induced by calcium chloride was investigated. Approximately 92.6% of the soymilk proteins were coagulated into the soymilk pellet fraction (SPF) after the addition of 5 mM calcium chloride. SDS-PAGE and two-dimensional electrophoresis analysis indicated that most of the 7S (α', α and β), 11S acidic (A1a, A1b, A2, A3 and A4) and 11S basic (B1a) proteins in the SSF were coagulated into the SPF after treatment with 5 mM calcium chloride. Isoflavones, including daidzein and genistein, were also coagulated into the SPF after the addition of 5 mM calcium chloride. The amounts of daidzein and genistein in the SSF decreased to 39.4 ± 1.6 and 11.8 ± 7.0%, respectively. HPLC analysis suggested that daidzein and genistein were bound with 7S and 11S proteins and then were coprecipitated into the SPF by 5 mM calcium chloride.

No MeSH data available.