2016
DOI: 10.1016/j.foodhyd.2016.07.013
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Functionality and digestibility of albumins and globulins from lentil and horse gram and their effect on starch rheology

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Cited by 75 publications
(55 citation statements)
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“…The globulin, prolamin, and glutelin content was considerably lower than the albumin content in all soybean samples. The literature reports that from 35% to 70% of the total soybean storage proteins is composed of globulins, mainly glycinin and β ‐conglycinin . This was not corroborated by the present results.…”
Section: Resultscontrasting
confidence: 96%
“…The globulin, prolamin, and glutelin content was considerably lower than the albumin content in all soybean samples. The literature reports that from 35% to 70% of the total soybean storage proteins is composed of globulins, mainly glycinin and β ‐conglycinin . This was not corroborated by the present results.…”
Section: Resultscontrasting
confidence: 96%
“…Barichello et al () reported that starches with higher transition temperatures have higher degree of crystallinity that provides starch granules structural stability and makes them more resistant to gelatinisation. These results are in concurrence with high apparent amylose content in horse gram as compared to lentils, as observed in our previous studies (Ghumman et al , ). However, lower transition temperature but higher ∆ H gel were observed in lentil starches as compared to horse gram starches.…”
Section: Resultssupporting
confidence: 93%
“…In the case of fermented PPEF, the surface hydrophobicity was shown to decrease over fermentation time; thus, the EA did not increase possibly due to the protein's inflexibility and low adsorption at the oil–water interface. The surface charge of fermented PPEF increased over fermentation time; however, the results were in the low range (between −30 and +30 mV), and consequently, samples would be unstable due to the lack of repulsion and have an inclination to flocculate (Ghumman et al, ).…”
Section: Resultsmentioning
confidence: 99%
“…Physicochemical properties such as surface hydrophobicity and surface charge of proteins are important factors that can influence the EA and ES properties due to their adsorption and flexibility of proteins at the interface (Ghumman, Kaur, & Singh, 2016;Shevkani, Singh, Kaur, & Rana, 2015;Xiao et al, 2018). Xiao et al (2018) hypothesized that fungal SSF of red bean protein increased EA due to increased hydrophobicity of proteins.…”
Section: Emulsifying Propertiesmentioning
confidence: 99%