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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 SDS-PAGE profiles of soymilk with different amounts of calcium chloride (0, 2.5, or 5 mM) incubated at 30 °C for 1 h.(A) Soymilk supernatant fraction (SSF); (B) soymilk pellet fraction (SPF); M: protein marker.
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f2: Changes in the SDS-PAGE profiles of soymilk with different amounts of calcium chloride (0, 2.5, or 5 mM) incubated at 30 °C for 1 h.(A) Soymilk supernatant fraction (SSF); (B) soymilk pellet fraction (SPF); M: protein marker.

Mentions: As previously mentioned, the addition of 5 mM calcium chloride sufficiently coagulated the soymilk proteins into the SPF. Therefore, soymilk samples treated with varying amounts of calcium chloride (0, 2.5 or 5 mM) were analyzed by SDS-PAGE (Fig. 2). The intensity of the protein bands corresponding to the 7S α’, 7S α, 7S β, 11S A3, 11S acidic subunits and 11S basic proteins in the SSF significantly decreased following the addition of 5 mM calcium chloride (P < 0.05), the protein bands corresponding to the these proteins decreased to 1.8 ± 0.1, 0.9 ± 0.1, 1.1 ± 0.3, 1.6 ± 0.2, 2.1 ± 0.1 and 1.6 ± 0.1%, respectively (Fig. 2A). These proteins appeared in the SPF (Fig. 2B). The presence of 7S and 11S proteins in the SPF is evidence that calcium chloride binds to the 7S and 11S proteins and that they are both involved in soybean curd formation. The protein particles in soymilk contain a large amount of 7S β and 11S subunits and that the 11S subunit is formed by conjugation with the core of the 7S β subunit17. Teng et al.18 indicated that 10 mM and 20 mM calcium chloride can precipitate the maximum amounts of 11S and 7S, respectively. Our results suggest that 5 mM calcium chloride can precipitate soymilk proteins, including the 7S α’, 7S α, 7S β, 11S A3, 11S acidic subunits and 11S basic proteins.


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 SDS-PAGE profiles of soymilk with different amounts of calcium chloride (0, 2.5, or 5 mM) incubated at 30 °C for 1 h.(A) Soymilk supernatant fraction (SSF); (B) soymilk pellet fraction (SPF); M: protein marker.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f2: Changes in the SDS-PAGE profiles of soymilk with different amounts of calcium chloride (0, 2.5, or 5 mM) incubated at 30 °C for 1 h.(A) Soymilk supernatant fraction (SSF); (B) soymilk pellet fraction (SPF); M: protein marker.
Mentions: As previously mentioned, the addition of 5 mM calcium chloride sufficiently coagulated the soymilk proteins into the SPF. Therefore, soymilk samples treated with varying amounts of calcium chloride (0, 2.5 or 5 mM) were analyzed by SDS-PAGE (Fig. 2). The intensity of the protein bands corresponding to the 7S α’, 7S α, 7S β, 11S A3, 11S acidic subunits and 11S basic proteins in the SSF significantly decreased following the addition of 5 mM calcium chloride (P < 0.05), the protein bands corresponding to the these proteins decreased to 1.8 ± 0.1, 0.9 ± 0.1, 1.1 ± 0.3, 1.6 ± 0.2, 2.1 ± 0.1 and 1.6 ± 0.1%, respectively (Fig. 2A). These proteins appeared in the SPF (Fig. 2B). The presence of 7S and 11S proteins in the SPF is evidence that calcium chloride binds to the 7S and 11S proteins and that they are both involved in soybean curd formation. The protein particles in soymilk contain a large amount of 7S β and 11S subunits and that the 11S subunit is formed by conjugation with the core of the 7S β subunit17. Teng et al.18 indicated that 10 mM and 20 mM calcium chloride can precipitate the maximum amounts of 11S and 7S, respectively. Our results suggest that 5 mM calcium chloride can precipitate soymilk proteins, including the 7S α’, 7S α, 7S β, 11S A3, 11S acidic subunits and 11S basic proteins.

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.