Application of Fourier transform infrared spectroscopy to legume seed flour analysis

Carbonaro, Marina; Maselli, P.; Dore, P.; Nucara, A.

doi:10.1016/j.foodchem.2007.10.045

Cited by 114 publications

(93 citation statements)

References 29 publications

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“…This result has also been observed by other authors (Hentges et al, 1991;Ribeiro et al, 2005). Moreover, the low protein solubility found in beans is due to a secondary structure of the beta-sheet protein found in this leguminous species, which becomes more insoluble when heat is applied (Carbonaro et al, 2008); it may also be associated with the production of insoluble aggregates during storage.…”

Section: Discussionsupporting

confidence: 86%

Physico-chemical properties of common beans under natural and accelerated storage conditions

et al. 2013

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The common bean is an important food in the human diet. Certain storage conditions, high temperatures and high humidity, cause a texture defect that reduces the acceptability of common beans. The present study aimed at evaluating the effect of storage on the physico-chemical properties of common bean grains and the relationship between accelerated aging at 40 °C and 76% RH and storage under natural conditions. Two varieties of common beans (Iapar 81 -carioca variety and Iapar 44 -black variety) were stored at 40 ºC and 76% RH for 15, 30, 45, 60 and 75 days to accelerate aging. The same varieties were stored under environmental conditions (natural aging) for 3, 6, 9 and 12 months. For both storage conditions of each variety, fresh beans stored at 5 ºC were used as a control group. In all of the samples, hardness, pH, acidity and the soluble protein percentage were analyzed. Both storage processes, in the natural and accelerated conditions, caused an increase in acidity (4.0 to 5.9 and 3.2 to 6.4 g acetic acid kg -1 ) and a decrease in cellular pH (6.65 to 6.45 and 6.65 to 6.45) and protein solubility (77 to 54 and 76 to 38%). The greatest percentage changes in the parameters of acidity, pH and soluble proteins were observed in the beans in the accelerated aging condition. Beans' hardness during storage has a negative correlation with pH, which shows that it is a good indicator of grain quality. Natural storage for one year is equivalent to accelerated aging for 45 days at 40 °C and 76% RH.

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Section: Discussionsupporting

confidence: 86%

Physico-chemical properties of common beans under natural and accelerated storage conditions

et al. 2013

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“…, which is indicative of intermolecular β-sheets of proteins and is associated with thermal protein aggregation (Allain et al, 1999;Carbonaro et al, 2008;Kato and Takagi, 1988;Militello et al, 2004). …”

Section: Ft-irmentioning

confidence: 99%

Temperature Effect on Pink Shrimp (<i>Pandalus eous</i>) Protein Adsorption onto a Stainless Steel Surface

Hagiwara

Suzuki

Hasegawa

et al. 2015

FSTR

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“…(1) the structural properties of proteins in plant foods have a major role in the resistance to denaturation (Deshpande and Damodaran 1989;Carbonaro 2008), and (2) plant proteins manifest stability upon gastrointestinal digestion (Carbonaro et al 2000;Shewry and Halford 2002).…”

Section: Introductionmentioning

confidence: 99%

Relationship between digestibility and secondary structure of raw and thermally treated legume proteins: a Fourier transform infrared (FT-IR) spectroscopic study

2011

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The secondary structure of proteins in legumes, cereals, milk products and chicken meat was studied by diffuse reflectance infrared spectroscopy in the region of the amide I band. Major secondary structure components ( β-sheets, random coil, α-helix, turns), together with the low- and high-frequency side contributions, were resolved and related to the in vitro digestibility behaviour of the different foods. A strong inverse correlation between the relative spectral weights of the β-sheet structures and in vitro protein digestibility values was measured. Structural modifications in legume proteins induced by autoclaving were monitored by the changes in the amide I spectra. The results indicate that the β-sheet structures of raw legume proteins and the intermolecular β-sheet aggregates, arising upon heating, are primary factors in adversely affecting the digestibility.

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Application of Fourier transform infrared spectroscopy to legume seed flour analysis

Cited by 114 publications

References 29 publications

Physico-chemical properties of common beans under natural and accelerated storage conditions

Physico-chemical properties of common beans under natural and accelerated storage conditions

Temperature Effect on Pink Shrimp (<i>Pandalus eous</i>) Protein Adsorption onto a Stainless Steel Surface

Relationship between digestibility and secondary structure of raw and thermally treated legume proteins: a Fourier transform infrared (FT-IR) spectroscopic study

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