2012
DOI: 10.1016/j.jcs.2012.06.008
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Characterization and In Vitro digestibility of rice protein prepared by enzyme-assisted microfluidization: Comparison to alkaline extraction

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Cited by 103 publications
(43 citation statements)
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“…The proteins are very susceptible to denaturation in alkaline solution by destabilization of the tertiary structures through elimination of the electrostatic interactions between ionized carboxylic groups and amine protonated guanidinium groups and the cleavage of hydrogen bonds between the hydroxyl group of tyrosine and carboxylic groups. Xia et al (2012) observed a similar behavior. In that study, the authors isolated the protein from broken rice, which was then mixed with 0.1% NaOH solution at room temperature for 1 h, and then left overnight before separation.…”
Section: Differential Scanning Calorimetrysupporting
confidence: 57%
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“…The proteins are very susceptible to denaturation in alkaline solution by destabilization of the tertiary structures through elimination of the electrostatic interactions between ionized carboxylic groups and amine protonated guanidinium groups and the cleavage of hydrogen bonds between the hydroxyl group of tyrosine and carboxylic groups. Xia et al (2012) observed a similar behavior. In that study, the authors isolated the protein from broken rice, which was then mixed with 0.1% NaOH solution at room temperature for 1 h, and then left overnight before separation.…”
Section: Differential Scanning Calorimetrysupporting
confidence: 57%
“…However, Ju et al (2001) observed a denaturation peak (at 82.2 o C) of the glutelin fraction of rice endosperm extracted with 0.08% NaOH at 20°C for 30 min. It is notable that these authors used a lower NaOH concentration and a lower extraction temperature than that employed by either Xia et al (2012) or this study. Thus, it is understood that the intensity of the alkaline treatment (alkali concentration, temperature and contact time) influences the preservation of protein tertiary structure during extraction.…”
Section: Differential Scanning Calorimetrymentioning
confidence: 89%
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“…It is comprised of 11-16% of hypoallergenic protein (Fabian and Ju 2011;Xia et al 2012). Rice bran is a popular byproduct that is often used as starting material.…”
Section: Introductionmentioning
confidence: 99%
“…RPIs may lose commercial value when chemical or biochemical modifications likely generate undesirable substances, such as bitter hydrolysates (Lamsal, Reitmeier, Murphy, & Johnson, 2006), with uncertain effects on the human body. Various physical approaches, such as microfluidization (Xia, Wang, Gong, et al, 2012), hydrothermal cooking , freeze-thaw, sonication, high-speed blending, and high pressure (Tang, Hettiarachchy, & Shellhammer, 2002), have been investigated. However, the effects of these treatments on the solubilization of RPIs are unsatisfactory.…”
Section: Introductionmentioning
confidence: 99%