Soy Protein Isolate Components and Their Interactions

Petruccelli, Silvana; Añón, Marı́a Cristina

doi:10.1021/jf00055a004

Cited by 114 publications

(77 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…A chickpea extract (C-E), B chickpea isoprecipitate, C chickpea cryoprecipitate, A s soybean isoprecipitate (Utsumi and Kinsella 1985), 20.6 and 10.0 (Sathe et al 1987) kDa. The estimated molecular weights of chickpea vicilin subunits, were 70.2, 50.7, 35.0, 33.6, 18.9 and 15.5 kDa and these subunits are comparable to 7S pea protein subunits (MW 50,35,33,19,15 and 13 kDa) reported by Gueguen (1991) and soybean 7S β-conglycinin subunits 70.6 (Sathe et al 1987), 52 (Nielsen 1985), 30.0 (Petruccelli and Anon 1995), and 18.0 (Sathe et al 1989) kDa. The chickpea extract containing the band A3 identified in Native PAGE, showed subunits of MW 54.3 kDa in SDS-PAGE; this is similar to the 55 kDa rice glutelin identified by Takaiwa et al (1999).…”

Section: Native and Sds-page Characterizationsupporting

confidence: 70%

“…Soybean globulin subunits were previously identified by SDS-PAGE as 42.0 (Moreira et al 1979), 38.0 (Utsumi andKinsella 1985), 20.6 and 10.0 (Sathe et al 1987) kDa for 11S glycinin and as 70.6 (Sathe et al 1987), 52 (Nielsen 1985), 30.0 (Petruccelli and Anon 1995), and 18.0 (Sathe et al 1989) kDa for 7S β-conglycinin; soybean albumin (2 S proteins) contains several tyrpsin inhibitors with molecular weight ranging from 8-21.5 kDa reported by Vaidehi and Kadam (1989). The available information on chickpea globulin and albumin fractions suggests that their subunit molecular characteristics are comparable to those of other legume seeds such as soybean seeds.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Isolation and Characterization of Chickpea (Cicer arietinum L.) Seed Protein Fractions

Chang

Alli

Molina

et al. 2009

Food Bioprocess Technol

View full text Add to dashboard Cite

Proteins of ground chickpea seeds were extracted with sodium hydroxide (NaOH) solution and precipitated with addition of acid (isoelectric precipitate (C-IP)) and by cryoprecipitation (cryoprecipitate (C-CP)). The protein isolates were characterized by Native PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), reversed-phase high performance liquid chromatography (RP-HPLC) and electrospray-ionization mass spectrometry (ESI/MS). Both the isoelectric precipitate and cryoprecipitate contained the globulin protein 11S legumins and 7S vicilins as the major protein fractions and 2S albumin proteins as a minor protein fraction. The major subunits of RP-HPLC protein fractions from both cryoprecipitate and isoelectric precipitate were found to contain subunits of both legumins and vicilins. SDS-PAGE identified legumin α-subunits with MW 40.6 and 39.5 kDa and legumin β-subunits with MW 23.5 and 22.5 kDa, and vicilin subunits with MW 70.2, 50.7, 35.0, 33.6, 18.9 and 15.5 kDa. ESI-MS molecular weights 35,366, 35,268 and 14,648 Da are likely vicilin subunits while the 24,894 Da is a legumin β-subunit.

show abstract

Section: Native and Sds-page Characterizationsupporting

confidence: 70%

Section: Introductionmentioning

confidence: 99%

Isolation and Characterization of Chickpea (Cicer arietinum L.) Seed Protein Fractions

Chang

Alli

Molina

et al. 2009

Food Bioprocess Technol

View full text Add to dashboard Cite

show abstract

“…From SDS-PAGE (Fig. 2), soymilk samples, which were unheated or heated at 70 and 80ºC, showed bands corresponding to glycinin subunits (Petrucceli and Añón 1995a). However, the glycinin subunits disappeared, and the aggregates formed through disulfide (S-S) binding were detected in soymilk heated to 90ºC or higher.…”

Section: Resultsmentioning

confidence: 99%

Effect of Heat Treatment on Dispersion Stability of Soymilk and Heat Denaturation of Soymilk Protein

Shimoyamada

Tsushima

Tsuzuki

et al. 2008

FSTR

View full text Add to dashboard Cite

Soymilk was prepared by non-heated squeezing and then heated at various temperatures. For one-step heating, the precipitate produced by heating soymilk increased for heating at 70 and 80ºC and was much less at 90ºC or higher temperatures, showing that the dispersion stability of soymilk was dependent on the heating temperature. In the case of two-step heating (combinations of 115ºC and a lower temperature), soymilk heated at 115ºC in the first step and 70 or 80ºC in the second step resulted in increased precipitation. Changes in protein surface hydrophobicity were considered to be related to the precipitate formation of soymilk heated at the two different temperatures, indicating the significance of heat denaturation and aggregate formation of proteins on the dispersion stability of soymilk.

show abstract

“…Preparation of SPI SPI was prepared from defatted flour manufactured by Archer Daniel Midland (USA). An alkaline extraction (pH 8.0), followed by precipitation at the isoelectric point (pI 4.5) was carried out according to Petruccelli and Añón (1995). The isoelectric precipitate was dispersed in distilled water and adjusted to pH 8.0 with 2 M NaOH.…”

Section: Methodsmentioning

confidence: 99%