Assessment of Soy Genotype and Processing Method on Quality of Soybean Tofu

Stanojević, Sladjana P.; Barać, Miroljub B.; Pešić, Mirjana B.; Vucelić-Radović, Biljana V.

doi:10.1021/jf2006672

Cited by 67 publications

(56 citation statements)

References 28 publications

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“…In addition, the specific breeding or genetic modification of wheat could be performed to minimize any potential disease- or food quality-related protein or peptide content compared to that of existing wheat cultivars, as is underway for the deletion of the conglycinin α' subunit from the soybean proteome [47,48]. …”

Section: Resultsmentioning

confidence: 99%

Seed storage proteins of the globulin family are cleaved post-translationally in wheat embryos

et al. 2012

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BackgroundThe 7S globulins are plant seed storage proteins that have been associated with the development of a number of human diseases, including peanut allergy. Immune reactivity to the wheat seed storage protein globulin-3 (Glo-3) has been associated with the development of the autoimmune disease type 1 diabetes in diabetes-prone rats and mice, as well as in a subset of human patients.FindingsThe present study characterized native wheat Glo-3 in salt-soluble wheat seed protein extracts. Glo-3-like peptides were observed primarily in the wheat embryo. Glo-3-like proteins varied significantly in their molecular masses and isoelectric points, as determined by two dimensional electrophoresis and immunoblotting with anti-Glo-3A antibodies. Five major polypeptide spots were identified by mass spectrometry and N-terminal sequencing as belonging to the Glo-3 family.ConclusionsThese results in combination with our previous findings have allowed for the development of a hypothetical model of the post-translational events contributing to the wheat 7S globulin profile in mature wheat kernels.

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Section: Resultsmentioning

confidence: 99%

Seed storage proteins of the globulin family are cleaved post-translationally in wheat embryos

et al. 2012

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“…In fact, a gradual decrease in the protein solubility was observed for all samples tested from 72 to 38 mg g Similarly, studies by Liu et al (2008) demonstrated that the protein solubility of soybeans decreased significantly after one year of storage under adverse conditions (88% relative humidity and 30 °C). Changes in these characteristics were due to molecular changes in the B-pleated structure and disulfide bonds, with protein denaturation, in addition to the possible complexation of proteins with phenolic acids during storage (CHEN et al, 2011;STANOJEVIC et al, 2011).…”

Section: Crude Protein and Protein Solubilitymentioning

confidence: 99%

Physicochemical properties and enzymatic bean grains dried at different temperatures and stored for 225 days

Elias

Ziegler

Romano

et al. 2016

SCA

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Beans are an important food in the world and are present on the tables of Brazilians almost daily. The harvest of these grains occurs seasonally during the year, and hence, steps after harvesting are essential to maintain product demand. However, the drying and storage conditions may alter the characteristics of the beans, reducing their economic value and their acceptability to consumers. The objective of this study was to evaluate the impact of storage time on the chemical, technological and enzymatic parameters of black beans dried at three temperatures (30, 45 and 60 °C) and stored for 225 days in conventional woven polypropylene bags. The results show that the increase in storage time leads to a lower protein solubility, and a decreased content of tannins, lipids and proteins; and an increased cooking time, fat acidity, and the enzymatic activity of peroxidase and polyphenol oxidase. These parameters are important in the quality control of beans for consumption and as a raw material for the food industry. The quantity of broken grains and the grain roughness index are only influenced by the drying temperature regardless of the storage time of 225 days. Key words: Conservation. Quality. Phaseolus vulgaris L. Postharvest. ResumoO feijão é um alimento importante em todo o mundo, estando presente quase que diariamente na mesa dos brasileiros. A colheita desses grãos ocorre sazonalmente durante o ano, e por isso, as etapas de pós-colheita são imprescindíveis para manter a demanda do produto, no entanto, as condições de secagem e armazenamento podem alteram suas características, reduzindo o valor econômico e a aceitabilidade dos consumidores. O objetivo do estudo foi avaliar os efeitos do tempo de armazenamento sobre parâmetros químicos, tecnológicos e enzimáticos de avaliação da qualidade de grãos de feijão preto secos em três temperaturas (30, 45 e 60°C), e armazenados por 225 dias em um sistema convencional de sacos de polipropileno trançado. Os resultados mostram que o aumento do tempo de armazenamento provoca redução da solubilidade proteica, dos níveis de taninos, do conteúdo de lipídios e de proteínas, com o aumento do tempo de cocção, da acidez lipídica e da atividade enzimática da peroxidase e polifenoloxidase à 30, 45 e 60°C. Esses parâmetros são importantes para o controle de qualidade dos grãos para o consumo e como matéria-prima para a indústria de alimentos. A quantidade de grãos quebrados e o índice de rugosidade dos grãos são alterados apenas pela temperatura de secagem, independentemente do tempo de armazenamento de 225 dias. Palavras-chave: Conservação. Qualidade. Phaseolus vulgaris L. Pós-colheita.

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“…They showed that this enzyme had no significant proteolytic activity against native form of glycinin. In contrast, Stanojevic et al [37] proved that chymosin hydrolyzed thermally-treated soy proteins. In current literature, there is no data about the effect of particular enzymes on protein composition of pea isolates or on their functional properties.…”

Section: Introductionmentioning

confidence: 99%

Functional Properties of Pea (Pisum sativum, L.) Protein Isolates Modified with Chymosin

Barać

Čabrilo²,

Pešić

et al. 2011

IJMS

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In this paper, the effects of limited hydrolysis on functional properties, as well as on protein composition of laboratory-prepared pea protein isolates, were investigated. Pea protein isolates were hydrolyzed for either 15, 30 and 60 min with recombined chymosin (Maxiren). The effect of enzymatic action on solubility, emulsifying and foaming properties at different pH values (3.0; 5.0; 7.0 and 8.0) was monitored. Chymosin can be a very useful agent for improvement of functional properties of isolates. Action of this enzyme caused a low degree of hydrolysis (3.9–4.7%), but improved significantly functional properties of pea protein isolates (PPI), especially at lower pH values (3.0–5.0). At these pH values all hydrolysates had better solubility, emulsifying activity and foaming stability, while longer-treated samples (60 min) formed more stable emulsions at higher pH values (7.0, 8.0) than initial isolates. Also, regardless of pH value, all hydrolysates showed improved foaming ability. A moderate positive correlation between solubility and emulsifying activity index (EAI) (0.74) and negative correlation between solubility and foam stability (−0.60) as well as between foam stability (FS) and EAI (−0.77) were observed. Detected enhancement in functional properties was a result of partial hydrolysis of insoluble protein complexes.

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Assessment of Soy Genotype and Processing Method on Quality of Soybean Tofu

Cited by 67 publications

References 28 publications

Seed storage proteins of the globulin family are cleaved post-translationally in wheat embryos

Seed storage proteins of the globulin family are cleaved post-translationally in wheat embryos

Physicochemical properties and enzymatic bean grains dried at different temperatures and stored for 225 days

Functional Properties of Pea (Pisum sativum, L.) Protein Isolates Modified with Chymosin

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