2013
DOI: 10.1016/j.jcs.2013.05.008
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Electrophoretic analysis of malting degradability of major sorghum reserve proteins

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Cited by 8 publications
(14 citation statements)
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“…Nkama et al (2015) observed that malting resulted in a sorghum flour protein digestibility increase from 38 to 61%. Malting also enhances the nutritional quality of grains by increasing the availability of protein and starch and the level of readily absorbed N in the forms of free amino acids and soluble peptides (Afify et al, 2012;Mokhawa et al, 2013). Malting increases protein digestibility by increasing protein solubility, decreasing the amount of cross-linked kafirin, and hydrolyzing antinutrients such as phytate and polyphenol (Afify et al, 2012;Nkama et al, 2015).…”
Section: Food Processing and Sorghum Protein Digestibilitymentioning
confidence: 99%
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“…Nkama et al (2015) observed that malting resulted in a sorghum flour protein digestibility increase from 38 to 61%. Malting also enhances the nutritional quality of grains by increasing the availability of protein and starch and the level of readily absorbed N in the forms of free amino acids and soluble peptides (Afify et al, 2012;Mokhawa et al, 2013). Malting increases protein digestibility by increasing protein solubility, decreasing the amount of cross-linked kafirin, and hydrolyzing antinutrients such as phytate and polyphenol (Afify et al, 2012;Nkama et al, 2015).…”
Section: Food Processing and Sorghum Protein Digestibilitymentioning
confidence: 99%
“…Malting also enhances the nutritional quality of grains by increasing the availability of protein and starch and the level of readily absorbed N in the forms of free amino acids and soluble peptides (Afify et al, 2012;Mokhawa et al, 2013). In the electrophoric profile of malted sorghum, polymeric and monomeric kafirin fractions are substantially reduced due to germination induced proteolytic enzyme activation and subsequent kafirin deploymerization and digestion, but the digestion recalcitrant 45-kDa kafirin discussed elsewhere in this manuscript and a-kafirin monomers appear to be less affected (Mokhawa et al, 2013). During malting, kafirins undergo extensive proteolytic degradation, which explains the mechanism for improved digestibility, but the relative degradation of the different kafirin classes vary with sorghum cultivar (Mokhawa et al, 2013).…”
Section: Food Processing and Sorghum Protein Digestibilitymentioning
confidence: 99%
“…Instead, it is possible that this protein could potentially be classified as a HMW protein entity, which may be linked by hydrogen bonds. In previous studies, this protein has been identified as a HMW kafirin due to its resistance to breakdown by reducing agents (132). In the current study, a HMW protein was isolated within a similar size range (40-50kD) on 2D SDS-PAGE and identified as a homolog to 50 kD γ-prolamins from other grass species, such as sugarcane and maize, through LC-MS/MS (Chapter 3).…”
Section: High Mw (Hmw) Prolaminmentioning
confidence: 79%
“…Proteins are fractionated according to size (SDS-CE), charge density (FZCE), or isoelectric point (cIEF) (131). These methods have been useful for distinguishing between cereal genotypes and in assigning functionality to storage proteins (132). FZCE has also been used in the differentiation of wheat cultivars, identification of rye translocations in wheat flour, and to monitor seed maturation (133,134).…”
Section: High Performance Capillary Electrophoresis (Hpce)mentioning
confidence: 99%
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