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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 two-dimensional polyacrylamide gel electrophoresis profiles of soymilk proteins after treatment with different amounts of calcium chloride (0, 2.5 or 5 mM) at 30 °C for 1 h.(A) soymilk supernatant fraction (SSF); (B) soymilk pellet fraction (SPF); M: protein marker; MW: molecular weight; pI: isoelectric point.
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f4: Changes in the two-dimensional polyacrylamide gel electrophoresis profiles of soymilk proteins after treatment with different amounts of calcium chloride (0, 2.5 or 5 mM) at 30 °C for 1 h.(A) soymilk supernatant fraction (SSF); (B) soymilk pellet fraction (SPF); M: protein marker; MW: molecular weight; pI: isoelectric point.

Mentions: Soymilk samples treated with varying amounts of calcium chloride (0, 2.5 or 5 mM) were also analyzed by 2-DE gels (Fig. 4). When no calcium chloride treatment was employed, soymilk proteins were clearly observed in the SSF on the 2-DE gel, although no soymilk proteins were detected in the SPF. Some of the 7S and 11S proteins that were depleted in the SSF after 2.5 mM calcium chloride was added, including 7S α, 7S β, 11S A3, 11S A2, 11S A1b, 11S A1a, and 11S B1a, appeared in the SPF. Most of the soymilk proteins appeared in the SPF following the 5 mM calcium chloride treatment, and only a small amount of 7S α, 7S β and 11S A1a were observed in the SSF. Densitograms corresponding to the 2-DE images of the calcium chloride-treated SSF and SPF samples were also generated. As previously mentioned, most of the 7S subunits (spots 1–5) in the SSF were coagulated by the addition of 5 mM calcium chloride. The fold changes of the 7S α’ (spot 1), 7S α (spot 2), 7S β (spot 3), 7S β (spot 4) and 7S β (spot 5) subunits in the SSF were 0.04, 0.07, 0.03, 0.03 and 0.02, respectively. We observed that a portion of the 11S subunits (spots 6–14) in the SSF were also coagulated by the addition of 5 mM calcium chloride. The fold changes of 11S A3 (spot 6), 11S A3 (spot 7), 11S A4 (spot 8), 11S A2 (spot 9), 11S A1b (spot 10), 11S A1b (spot 11), 11S A1a (spot 12), 11S A1a (spot 13) and 11S B1a (spot 14) subunits in the SSF were 0.02, 0.01, 0.01, 0.02, 0.01, 0.03, 0.03, 0.01 and 0.12, respectively. These 7S and 11S proteins in spots 1–14 almost completely disappeared from the SSF and appeared in the SPF after the addition of 5 mM calcium chloride. Therefore, the coagulation of proteins, due to the addition of 5 mM calcium chloride, was demonstrated by the appearance of individual 7S and 11S proteins in the SPF.


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 two-dimensional polyacrylamide gel electrophoresis profiles of soymilk proteins after treatment with different amounts of calcium chloride (0, 2.5 or 5 mM) at 30 °C for 1 h.(A) soymilk supernatant fraction (SSF); (B) soymilk pellet fraction (SPF); M: protein marker; MW: molecular weight; pI: isoelectric point.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f4: Changes in the two-dimensional polyacrylamide gel electrophoresis profiles of soymilk proteins after treatment with different amounts of calcium chloride (0, 2.5 or 5 mM) at 30 °C for 1 h.(A) soymilk supernatant fraction (SSF); (B) soymilk pellet fraction (SPF); M: protein marker; MW: molecular weight; pI: isoelectric point.
Mentions: Soymilk samples treated with varying amounts of calcium chloride (0, 2.5 or 5 mM) were also analyzed by 2-DE gels (Fig. 4). When no calcium chloride treatment was employed, soymilk proteins were clearly observed in the SSF on the 2-DE gel, although no soymilk proteins were detected in the SPF. Some of the 7S and 11S proteins that were depleted in the SSF after 2.5 mM calcium chloride was added, including 7S α, 7S β, 11S A3, 11S A2, 11S A1b, 11S A1a, and 11S B1a, appeared in the SPF. Most of the soymilk proteins appeared in the SPF following the 5 mM calcium chloride treatment, and only a small amount of 7S α, 7S β and 11S A1a were observed in the SSF. Densitograms corresponding to the 2-DE images of the calcium chloride-treated SSF and SPF samples were also generated. As previously mentioned, most of the 7S subunits (spots 1–5) in the SSF were coagulated by the addition of 5 mM calcium chloride. The fold changes of the 7S α’ (spot 1), 7S α (spot 2), 7S β (spot 3), 7S β (spot 4) and 7S β (spot 5) subunits in the SSF were 0.04, 0.07, 0.03, 0.03 and 0.02, respectively. We observed that a portion of the 11S subunits (spots 6–14) in the SSF were also coagulated by the addition of 5 mM calcium chloride. The fold changes of 11S A3 (spot 6), 11S A3 (spot 7), 11S A4 (spot 8), 11S A2 (spot 9), 11S A1b (spot 10), 11S A1b (spot 11), 11S A1a (spot 12), 11S A1a (spot 13) and 11S B1a (spot 14) subunits in the SSF were 0.02, 0.01, 0.01, 0.02, 0.01, 0.03, 0.03, 0.01 and 0.12, respectively. These 7S and 11S proteins in spots 1–14 almost completely disappeared from the SSF and appeared in the SPF after the addition of 5 mM calcium chloride. Therefore, the coagulation of proteins, due to the addition of 5 mM calcium chloride, was demonstrated by the appearance of individual 7S and 11S proteins in the SPF.

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.