Variability in phytic acid content and protein digestibility of grain legumes

Chitra, Uma; Vimala, V.; Singh, Ummed; Geervani, P.

doi:10.1007/bf01089266

Cited by 120 publications

(78 citation statements)

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“…A baixa digestibilidade da proteína de leguminosas parece resultar de diversas causas, porém, sem uma única explicação definitiva, e tem sido associada a interações proteína-tanino da semente [28], complexos proteína-fitato [10], proteína-fibra [26], inibição de enzimas digestivas [15], constrangimentos estruturais [14,32] e estrutura compacta de sua fração majoritária [1,29], as globulinas; presença de açúcares ligados à estrutura das globulinas e albuminas e possíveis impedimentos estéricos à ação das enzimas [30], além de interações proteína-proteína e proteína-carboidratos no tratamento térmico e interações proteína-outros constituintes no aquecimento. A digestibilidade in vitro da proteína total de grão-de-bico, em diferentes genótipos, mostra uma variação entre 60,4 e 74,4% [2,11], e aumento variável de 68,6 a 77,5% foi observado em diferentes cultivares após descorticação e/ou cozimento [4,7,20].…”

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“…Essa digestibilidade protéica tem sido melhorada em função de tratamentos, tais como: germinação, fermentação, aquecimento, descorticação, entre outros [9,27]. A germinação e fermentação de grão-de-bico provocaram aumento da digestibilidade in vitro em grau superior ao observado pós autoclavagem [10]. Por outro lado, o grão-de-bico apresenta baixos níveis de compostos polifenólicos [9,36], enquanto os inibidores de proteases são facilmente destruídos pelos procedimentos normais de cozimento [9], e em alguns casos, tem se verificado correlação negativa entre atividade de inibidor de tripsina e a digestibilidade in vitro, pós-aquecimento [34].…”

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Caracterização e hidrólise in vitro da globulina principal de grão-de-bico (Cicer arietinum L.), var. IAC-Marrocos

Neves¹,

Silva²,

Lourenço³

2004

Ciênc. Tecnol. Aliment.

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RESUMONo presente estudo procedeu-se ao isolamento e caracterização da fração globulina majoritária (11 S) de grão-de-bico, var. IACMarrocos. A globulina majoritária extraída foi isolada por cromatografia de filtração em gel e de troca-iônica mostrando apenas uma banda de proteína na eletroforese em gel de poliacrilamida. A globulina majoritária, após passagem em coluna de Sephadex, revelou duas bandas protéicas de 55 e 52,5kDa e três bandas menores em gel de poliacrilamida dodecilsulfato de sódio. Na presença de 2-mercaptoetanol 6 polipeptídios na faixa de 18 a 42kDa foram revelados na eletroforese. A globulina isolada foi submetida à ação da tripsina e quimotripsina onde a forma nativa mostrou-se resistente à ação enzimática enquanto o aquecimento (96 e 121°C/ 15min) não foi suficiente para aumentar a susceptibilidade à hidrólise, significativamente. Adição de NaCl 0,3M levou a um aumento da estabilidade estrutural com menor susceptibilidade à digestão proteolítica, fato em parte perdido com o aquecimento. As hidrólises foram acompanhadas por eletroforese em gel de poliacrilamida dodecilsulfato de sódio. Palavras-chave: grão-de-bico; Cicer arietinum L.; globulina majoritária; caracterização; hidrólise in vitro. SUMMARY CHARACTERIZATION AND in vitro TRYPTIC HYDROLYSIS OF THE MAJOR GLOBULIN FROM CHICKPEA (Cicer arietinum L.).The isolation and characterization of the major globulin fraction (11 S) from Chickpea, vc IAC-Marrocos, were evaluated. The major globulin was extracted, isolated by gel filtration and ion-exchange chromatography showing only one protein band on PAGE. The globulin, after Sephadex elution, revealed two protein bands of 55 and 52.5kDa and three minor bands on SDS-PAGE. In the presence of 2-mercaptoethanol six polypeptides were revealed on SDS-PAGE in the range of 18 to 42kDa. The isolated native globulin shown to be resistant to trypsin and chymotrypsin however heating at 96 and 121ºC/15min was not sufficient to increase the hydrolysis significantly. The proteolytic susceptibility of the enzymes was reduced by 0.3M NaCl addition at the assay. The salt concentration was sufficient to stabilize the native protein structure that was lost after heating as demonstrated on SDS-PAGE.

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Caracterização e hidrólise in vitro da globulina principal de grão-de-bico (Cicer arietinum L.), var. IAC-Marrocos

Neves¹,

Silva²,

Lourenço³

2004

Ciênc. Tecnol. Aliment.

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“…radiata is a rich source of protein, resistant starch and dietary fibres (Chitra et al 1995;Sandhu et al 2008), and contains higher levels of folate and iron than most other legumes (Graham and Vance 2003). Proteins and carbohydrates of V. radiata are easily digestible and create less flatulence than proteins derived from other legumes.…”

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confidence: 99%

In silico genome-wide identification and characterization of the glutathione S-transferase gene family in Vigna radiata

Vaish

Awasthi

Tiwari

et al. 2018

Genome

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Plant glutathione S-transferases are integral to normal plant metabolism, and biotic and abiotic stress tolerance. GST gene family has been characterized in diverse plant species using molecular biology and bioinformatics approaches. In the current study, in silico analysis identified 44 GSTs in Vigna radiata. Of the total 44 GSTs identified, chromosomal locations of 31 GSTs were confirmed. The pI value of GST proteins ranged from 5.10 to 9.40. The predicted molecular weights ranged from 13.12 to 50 kDa. Subcellular localization analysis revealed that all GSTs were predominantly localized in the cytoplasm. The active site amino acids were confirmed to be serine in tau, phi, theta, zeta and TCHQD; cysteine in lambda, DHAR and omega; and tyrosine in EF1G. The gene architecture conformed to the 2 exon-1 intron and 3 exon-2 intron organization in case of tau and phi classes, respectively. MEME analysis identified 10 significantly conserved motifs with the width of 8 to 50 amino acids. The motifs identified were either specific to a specific GST class, or were shared by multiple GST classes. The results of the current study will be of potential importance in the characterization of GST gene family in V. radiata, an economically important leguminous crop.

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“…Chitra et al [5] also observed positive correlation between phytate and proteins, but with lower significance compared to other legume seed. This could mean that irrespectively to relatively low oil and protein content in chickpea seed (Table 1), its nutritional quality could be increased by slight oil increase in parallel with phytate decrease.…”

Section: Resultsmentioning

confidence: 93%

“…Chickpea seeds contain less than 7% of oil, with linoleic and oleic acid as predominant [4]. According to Chitra et al [5], chickpea contains relatively low phytic acid content, compared to other legumes. Significant and negative correlation between phytic acid and in vitro digestibility made chickpea seeds necessary in human diet.…”

Section: Introductionmentioning

confidence: 99%

Variations in level of oil, protein, and some antioxidants in chickpea and peanut seeds

Dragičević

Kratovalieva

Dumanović

et al. 2015

Chem. Biol. Technol. Agric.

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Background: Chickpea and peanut are two legume species not frequently used in human diets. Chickpea is rich in starch and proteins, while peanut is mainly a source of oils and proteins and they could be successfully used as protein sources in vegetarian diets. Seeds of 19 chickpea and 13 peanut landraces were colorimetrically analyzed in respect to antioxidant content (i.e., free soluble phenolics, total glutathione, and phytate). Oil and protein contents in grain were also determined. Results: Free soluble phenolics content varied in range from 520 to1,050 mg kg −1 in peanut and from 720 to 1,370 mg kg −1 in chickpea. Total glutathione content ranged from 1,495 to 2,365 mmol kg −1 in peanut and from 955 to 1,232 mmol kg −1 in chickpea. Relatively low content of phytic phosphorus was found in grain of both species, ranging from 2.5 to 4.5 g kg −1 in peanut and from 1.4 to 3.0 g kg −1 in chickpea, respectively. Considering the lack of data for phytate variability in Macedonian chickpea and peanut local landraces up to date, the observed high variation in phytic phosphorus content could represent the great basis for further breeding programs for phytate decrease in seeds of those genotypes. This is significant, since phytate is an important antinutrient which affects availability of mineral elements. Regression analysis revealed positive and highly significant interdependence between oil content and total glutathione in chickpea seeds, as well as between oil content and phytic phosphorus in peanut seeds. In chickpea, significant and negative correlation between oil and phytic phosphorus content was also observed. Conclusions: Results obtained indicated that chickpea genotypes with higher oil content could have increased nutritional value due to higher glutathione and lower phytate content observed. However, lower level of phytate content, along with higher level of soluble phenolics and total glutathione found in peanut seeds with lower oil content, indicated higher digestibility and increased antioxidant activity of those genotypes.

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Variability in phytic acid content and protein digestibility of grain legumes

Cited by 120 publications

References 15 publications

Caracterização e hidrólise in vitro da globulina principal de grão-de-bico (Cicer arietinum L.), var. IAC-Marrocos

Caracterização e hidrólise in vitro da globulina principal de grão-de-bico (Cicer arietinum L.), var. IAC-Marrocos

In silico genome-wide identification and characterization of the glutathione S-transferase gene family in Vigna radiata

Variations in level of oil, protein, and some antioxidants in chickpea and peanut seeds

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