Determination of heat-set gelation capacity of a quinoa protein isolate (Chenopodium quinoa) by dynamic oscillatory rheological analysis

Kaspchak, Elaine; Oliveira, Marco Aurélio Schüler de; Simas, Fernanda Fogagnoli; Franco, Célia Regina C.; Silveira, Joana Léa Meira; Mafra, Marcos R.; Igarashi‐Mafra, Luciana

doi:10.1016/j.foodchem.2017.04.014

Cited by 71 publications

(40 citation statements)

References 35 publications

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“…Rape BP includes all essential amino acids, and proline is the most abundant, consistent with the findings of a previous study (Roulston & Cane, ). Pollen protein may be a promising food ingredient, as complementing proteins of other foods due to its complete essential amino acids (Kaspchak et al ., ). Except for tryptophan, other amino acid contents were increased after pollen wall breaking.…”

Section: Resultsmentioning

confidence: 97%

Analysis of improved nutritional composition of bee pollen (Brassica campestris L.) after different fermentation treatments

Yan

Xue

et al. 2019

Int J of Food Sci Tech

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Summary Microbial fermentation as an excellent food processing technology has been used for improving the flavour and nutritional feature of food material. In this study, we compared the differences in the nutrient profile of bee pollen (rape bee pollen, Brassica campestris L., BP) fermented with different species of microbes, such as lactic acid bacteria (LAB), yeast, and the two mixed. Based on the nutritional components and multivariate statistical analysis, yeast fermentation has more advantage for BP than fermentation with LAB or mixed microbes. The yeast‐fermented BP has an 83.5% reduction in fructose and 87.4% reduction in glucose, while phenolic compounds, oligopeptides and fatty acids were increased by 9.3%, 68.8% and 18.2%, respectively, compared with the BP without fermentation. The contents of riboflavin, nicotinic acid, nicotinamide and free amino acids in the pollen fermented by yeast were 2.4, 39.6, 4.6 and 4.8 times higher than those in raw BP, respectively. Additionally, in the fermentation process, wall‐breaking pollen showed more advantages in the transformation of nutrients, free amino acid increased by 11% at least, more low molecular weight peptides produced and nicotinic acid and nicotinamide increased by 7% at least, compared with fermented BP. Taken together, these results showed that BP with yeast fermentation has great potential in obtaining high available nutritional products.

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Section: Resultsmentioning

confidence: 97%

Analysis of improved nutritional composition of bee pollen (Brassica campestris L.) after different fermentation treatments

Yan

Xue

et al. 2019

Int J of Food Sci Tech

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“…The analyzed proteins had a low solubility (1.68%–4.47%) at pH 4, whereas at pH 7 were in the range of 13.03%–13.37% and pH 10 solubility increases (49.03%–71.24%). The low solubility at pH 4 is due to the fact that this pH is close to the pH of the isoelectric point (pI) of the 11S quinoa globulin (around 5) since there are no repulsive charges, which leads to protein association and precipitation (Kaspchak et al, ). In contrast, the solubility of QPI, QPI‐HD, and QPI‐FL at pH 10 was significantly higher ( p < .05) compared to the values found at pH 4 and 7, possibly due to higher pH at the isoelectric point favoring a change in the structure of the protein that produces a greater exposure of the hydrophilic proteins, increasing the surface polarity and its interaction with water (Elsohaimy et al, ; Kaspchak et al, ; Mäkinen et al, ).…”

Section: Resultsmentioning

confidence: 99%

“…The low solubility at pH 4 is due to the fact that this pH is close to the pH of the isoelectric point (pI) of the 11S quinoa globulin (around 5) since there are no repulsive charges, which leads to protein association and precipitation (Kaspchak et al, ). In contrast, the solubility of QPI, QPI‐HD, and QPI‐FL at pH 10 was significantly higher ( p < .05) compared to the values found at pH 4 and 7, possibly due to higher pH at the isoelectric point favoring a change in the structure of the protein that produces a greater exposure of the hydrophilic proteins, increasing the surface polarity and its interaction with water (Elsohaimy et al, ; Kaspchak et al, ; Mäkinen et al, ). Furthermore, it has been reported that at pH values higher than isoelectric point value, there are negative charges on the protein, causing more interaction with the solvent and increase of solubility (Ruiz, Xiao, Van Boekel, Minor, & Stieger, ).…”

Section: Resultsmentioning

confidence: 99%

“…The higher adsorption capacity of QPI‐HD and QPI‐FL is congruent with the change in microstructure (Acosta‐Dominguez et al, ; Romero‐Luna et al, ) and with a higher porosity compared to QPI. It has been reported that the microstructure of the protein quinoa isolate is associated with attributes such as flavor retention, water‐holding capacity, and rigidity (Baier & McClements, ; Kaspchak et al, ) and that a change in the conformation of the proteins modifies the hydrophilicity and its capacity of adsorption on the surface (Sharma et al, ). The monolayer values found for the different quinoa protein isolates are lower than those reported for quinoa seeds (Tolaba, Peltzer, Enriquez, & Pollio, ), which is possibly due to the other components of the quinoa seed and effect of the treatment (freezing or denaturing by heat) on the adsorption sites and/or the modification of the microstructure.…”

Section: Resultsmentioning

confidence: 99%

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Influence of heat denaturation and freezing–lyophilization on physicochemical and functional properties of quinoa protein isolate

et al. 2020

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Backgrounds and objectives Quinoa protein isolate has been shown to confer significant health benefits. However, it is necessary to evaluate the effect of processing on its properties. Therefore, the aim of this work was to evaluate the influence of heat denaturation or freezing followed by lyophilization on the physicochemical and functional properties of the quinoa protein isolate. Findings Freezing–lyophilization of quinoa protein isolate (QPI‐FL) exhibited a higher foaming capacity and emulsifying capacity at pH 10, and the oil retention capacity was ten times greater that exhibited by the unmodified quinoa protein isolate (QPI), while the particle size and water and oil retention capacity in the modified protein isolate by heat denaturation (QPI‐HD) were twice as compared to QPI. The pH had a significant effect on all physicochemical and functional properties. The flow properties and the micrograph analysis of modified protein isolates revealed greater porosity in comparison with those of the unmodified protein isolate. QPI‐FL showed higher water adsorption capacity at high water activity and a greater displacement in the thermal transitions. Conclusions In general, heating did not significantly affect the functional properties of the quinoa protein isolate, while the freezing–lyophilization improved them, which may be of interest in the processes of foods that include in their process the heating or freezing. Significance and novelty Quinoa protein isolate can be added to different food products with the purpose of improving its composition. However, heating and freezing are two frequent operations in most processes that could affect their properties.

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“…These results coincide with Kaspchak et al [20], who found polypeptides of 59 kDa, 43 kDa, 35 kDa, 26 kDa, 24 kDa, and 22 kDa in quinoa protein, which are characteristic of acidic and basic subunits of 11S quinoa globulin [21]. QW showed bands of molecular weight >66 kDa that were not observed in the QP variety, in addition to clearly defined bands of 58.4 kDa, 40.5 kDa, and three more bands close to 27 kDa, which are characteristic of this quinoa variety ( Figure 1) [22]. Characteristic bands of globulin fractions are observed for both quinoa varieties in the presence and absence of TG (Figure 1), such as 11S basic subunit (28 kDa), 11S acid (40.5 kDa), 7s (43 kDa), and the 2S fraction of albumin (<20 kDa).…”

Section: Protein Isolate Characterizationmentioning

confidence: 95%

Effect of Transglutaminase Cross-Linking in Protein Isolates from a Mixture of Two Quinoa Varieties with Chitosan on the Physicochemical Properties of Edible Films

et al. 2019

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The growing demand for minimally processed foods with a long shelf life and environmentally friendly materials has forced industry to develop new technologies for food preservation and handling. The use of edible films has emerged as an alternative solution to this problem, and mixtures of carbohydrates and proteins, may be formulated to improve their properties. The objective of this work was to evaluate the effect of protein cross-linking with transglutaminase (TG) of two varieties of quinoa protein isolate (Chenopodium quinoa) [Willd (QW), and Pasankalla (QP)] on the physicochemical and barrier properties of edible films based on chitosan (CT)-quinoa protein. The evaluated properties were water vapor permeability (WVP), solubility, adsorption, roughness determined by atomic force microscopy, and the interactions among the main film components determined by Raman spectroscopy. The results indicated that TG interacted with lysine of QW and QP. CT:QW (1:5, w/w) showed the lowest solubility (14.02 ± 2.17% w/w). WVP varied with the composition of the mixture. The WVP of CT:quinoa protein ranged from 2.85 to 9.95 × 10−11 g cm Pa−1 cm−2 s−1 without TG, whereas adding TG reduced this range to 2.42–4.69 × 10−11 g cm Pa−1 cm−2 s−1. The addition of TG to CT:QP (1:10, w/w) reduced the film surface roughness from 8.0 ± 0.5 nm to 4.4 ± 0.3 nm. According to the sorption isotherm, the addition of TG to CT-QW films improved their stability [monolayer (Xm) = 0.13 ± 0.02 %]. Films with a higher amount of cross-linking showed the highest improvement in the evaluated physical properties, but interactions among proteins that were catalyzed by TG depended on the protein source and profile.

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Determination of heat-set gelation capacity of a quinoa protein isolate (Chenopodium quinoa) by dynamic oscillatory rheological analysis

Cited by 71 publications

References 35 publications

Analysis of improved nutritional composition of bee pollen (Brassica campestris L.) after different fermentation treatments

Analysis of improved nutritional composition of bee pollen (Brassica campestris L.) after different fermentation treatments

Influence of heat denaturation and freezing–lyophilization on physicochemical and functional properties of quinoa protein isolate

Effect of Transglutaminase Cross-Linking in Protein Isolates from a Mixture of Two Quinoa Varieties with Chitosan on the Physicochemical Properties of Edible Films

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