Thermal and electrophoretic behavior, hydrophobicity, and some functional properties of acid-treated soy isolates
In the present work, changes in the structure and functional properties of soy protein isolates caused by mild acid treatment at room temperature were investigated. Different conditions (pH, time, neutralization procedure, and isolate concentration) of acid treatment and consequent salt increase wer...
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| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
| Publicado: |
American Chemical Society
1996
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 10315caa a22008897a 4500 | ||
|---|---|---|---|
| 001 | PAPER-18948 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518205018.0 | ||
| 008 | 190411s1996 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0001129215 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a JAFCA | ||
| 100 | 1 | |a Wagner, J.R. | |
| 245 | 1 | 0 | |a Thermal and electrophoretic behavior, hydrophobicity, and some functional properties of acid-treated soy isolates |
| 260 | |b American Chemical Society |c 1996 | ||
| 270 | 1 | 0 | |m Wagner, J.R.; Ctro. Invest. Desarrollo C.A., Facultad de Ciencias Exactas, Buenos Aires, Argentina |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a In the present work, changes in the structure and functional properties of soy protein isolates caused by mild acid treatment at room temperature were investigated. Different conditions (pH, time, neutralization procedure, and isolate concentration) of acid treatment and consequent salt increase were analyzed. The results obtained show that there is a selective denaturation of US protein, which conduces to higher surface hydrophobicity. The solubility of modified isolates decreases with extended storage period of the flour from which they were obtained and with higher isolate concentration during acid treatment. The high water imbibing capacity (WIG) of the resulted insoluble fraction does not produce significant changes in the WIG of the total isolate. The denaturation and dissociation of US protein lead to modified isolates with improved capacity to form and to stabilize foams without losing the gel formation capacity. |l eng | |
| 593 | |a Ctro. Invest. Desarrollo C.A., Facultad de Ciencias Exactas, Buenos Aires, Argentina | ||
| 593 | |a Area Quim. Biol. y Biol. Molecular, Depto. de Ciencias Biológicas, Universidad Nacional de La Plata, 1900 La Plata, Pcia, Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a ACID TREATMENT |
| 690 | 1 | 0 | |a CHEMICAL MODIFICATION |
| 690 | 1 | 0 | |a FUNCTIONAL PROPERTIES |
| 690 | 1 | 0 | |a SOY ISOLATE |
| 690 | 1 | 0 | |a SOY PROTEIN |
| 690 | 1 | 0 | |a THERMAL BEHAVIOR |
| 700 | 1 | |a Sorgentini, D.A. | |
| 700 | 1 | |a Añón, M.C. | |
| 773 | 0 | |d American Chemical Society, 1996 |g v. 44 |h pp. 1881-1889 |k n. 7 |p J. Agric. Food Chem. |x 00218561 |w (AR-BaUEN)CENRE-101 |t Journal of Agricultural and Food Chemistry | |
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| 856 | 4 | 0 | |u https://doi.org/10.1021/jf950444s |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_00218561_v44_n7_p1881_Wagner |y Handle |
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