Properties of spray‐dried and freeze‐dried faba bean protein concentrates

Abstract

A protein concentrate from faba bean seeds was prepared by isoelectric precipitation and spray-dried. Its functional properties were measured and the results obtained were compared to those from another concentrate prepared by the classical freeze-drying technique. The functional properties were found to be indistinguishable. However, the protein solubility profile was different depending on the preparation technique. Some antinutritional factors (trypsin inhibitors, tannins and phytates) were also analysed. Both protein concentrates showed lower concentrations of tannins and phytates than the seeds.Feedfood supplements, functional properties, legume seed proteins, phytate, tannin, trypsin inhibitor.

Caracterização de concentrado proteico de feijão comum preto, cultivar Iapar 44, novo e envelhecido

“…Segundo Damodaran (1997), na maioria das proteínas ocorre mínima solubilidade no pH isoelétrico (pH 4-5), onde a repulsão eletrostática e a hidratação iônica são mínimas e a interação hidrofóbica entre as superfícies não polares é máxima. Resultados semelhantes foram encontrados em concentrado proteico de feijão fava novo e concentrados proteicos de feijão carioca novo e armazenado por Otegui et al (1997) e Donadel e Prudêncio-Ferreira (1999).…”

“…Resultados semelhantes foram encontrados por Donadel e Prudêncio-Ferreira (1999) ao avaliarem as propriedades funcionais de concentrado proteico de feijão comum, variedade carioca, envelhecido. A concentração mínima de dispersão para formação de gel observada neste trabalho foi maior do que as encontradas na literatura para isolados e concentrados de feijão 'mung' (COFFMANN; GARCIA, 1977); tremoço (KING; AGUIRRE; PABLO, 1985) e feijão fava (OTEGUI et al, 1997), novos.…”

Isothermal study of nonenzymatic browning kinetics in spray-dried and freeze-dried systems at different relative vapor pressure environments

“…Consequently, the functional properties of the materials might also be affected (Chinprahast, Jantawat, & Kristavee, 1995;Otegui et al, 1997). The physical state of an amorphous matrix greatly influences stability and affects rates of both physical and chemical changes during processing and storage (Buera & Karel, 1995;Champion, Le Meste, & Simatos, 2000;Eichner, 1981;Karmas, Buera, & Karel, 1992;Kim, Saltmarch, & Labuza, 1981;Roos, Karel, & Kokini, 1996;Roudaut, Simatos, Champion, Contreras-Lopez, & Le Meste, 2004;Slade & Levine, 1991).…”

Functional, conformational and topographical changes of succinic acid deamidated wheat gluten upon freeze- and spray-drying: A comparative study

“…Those structural and morphological differences had significant effects on the functional properties of food proteins (Otegui et al, 1997;Rahman, Al-Amri, & Al-Bulushi, 2002). Changes in functional properties of globular proteins during freezedrying and spray-drying, e.g., egg albumen, whole egg and yolk (Ayadi, Khemakhem, Belgith, & Attia, 2008;Galyean & Cotterill, 1979), hen egg ovalbumin (Kitabatake, Indo, & Doi, 1989), porcine blood plasma (Agyare, Addo, & Xiong, 2009) and faba bean protein (Cepeda, Villarán, & Aranguiz, 1998;Otegui et al, 1997), have been extensively reported. As for wheat gluten protein which has a network structure, Linarès, Larré, and Popineau (2001a) found that drying process induced no significant modification of molecular size distribution, hydrophobicity, and solubility of wheat gluten protein, and the interfacial properties of soluble peptides from freeze-and spray-dried samples were equivalent.…”