Kafirin structure and functionality

Belton, Peter; Delgadillo, Ivonne; Halford, Nigel G.; Shewry, Peter R.

doi:10.1016/j.jcs.2006.05.004

Cited by 261 publications

(250 citation statements)

References 48 publications

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“…Sorghum proteins are classified as albumins, globulins, kafirins, cross-linked kafirins and glutelins. (60) Of these, kafirins are the main protein, (61) comprising 50-70% of total protein content. (27) The kafirins are prolamin storage proteins with limiting levels of some amino acids, in particular lysine, (62) a disadvantage not unique among cereal grains.…”

Section: Proteinsmentioning

confidence: 99%

Sorghum: An Underutilized Cereal Whole Grain with the Potential to Assist in the Prevention of Chronic Disease

Stefoska‐Needham

Beck

Johnson

et al. 2015

Food Reviews International

148

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Section: Proteinsmentioning

confidence: 99%

Sorghum: An Underutilized Cereal Whole Grain with the Potential to Assist in the Prevention of Chronic Disease

Stefoska‐Needham

Beck

Johnson

et al. 2015

Food Reviews International

148

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“…Kafirin-2 = protein extracted from residual whole grain flour using 60% tert-butanol plus 5% (v/v) mercaptoethanol. 3 Different letters in columns indicate significant difference (p<0.05). 29 Figure 5 …”

Section: Pepsin Digestion Of the Pp By Starch Digestionmentioning

confidence: 99%

Transgenic Sorghum with Altered Kafirin Synthesis: Kafirin Solubility, Polymerization, and Protein Digestion

Silva

Taylor

2011

J. Agric. Food Chem.

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Transgenic sorghum (TG) lines with altered kafirin synthesis, particularly suppression of gamma-kafirin synthesis, and improved protein quality have been developed. The proportion of kafirin extracted with 60% tert-butanol alone was greatly increased in the TG lines. However, the total amount of kafirin remained unchanged.Further, in the TG lines, the kafirin was much less polymerized by disulfide bonding.There was also evidence of compensatory synthesis of other kafirin proteins. Cooked protein digestibility was increased in the TG form, even after removal of interfering starch.The TG protein bodies were intermediate in appearance between the normal type and the invaginated high digestibility mutants. Hence, the increased protein digestibility of these TG lines is probably related to their lower levels of disulfide-bonded kafirin polymerization, allowing better access of proteases. This work appears to confirm that disulfide bond formation in kafirin is responsible for the reduced protein digestibility of cooked sorghum.

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“…Kafirin is very similar to zein in amino acid composition but is more hydrophobic, or more strictly speaking less hydrophilic (12) and so can be considered amphiphilic in nature. Kafirin microparticles can be made by a process that is almost opposite to that used by Wang and Padua et al (10,11).…”

Section: Introductionmentioning

confidence: 99%

“…However, there has been little research on cross-linking of prolamin protein microparticles, probably because the proteins are relatively hydrophobic (12).…”

Section: Introductionmentioning

confidence: 99%

Physicochemical Modification of Kafirin Microparticles and Their Ability To Bind Bone Morphogenetic Protein-2 (BMP-2), for Application as a Biomaterial

Anyango

Duneas²,

Taylor

2012

J. Agric. Food Chem.

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Vacuolated spherical kafirin microparticles mean diameter 5 µm, can be formed from an acidic solution with water addition. Three dimensional scaffolds for hard tissue repair require large structures with a high degree of interconnected porosity. Cross-linking the formed kafirin microparticles using wet heat or glutaraldehyde treatment resulted in larger structures (approx. 20 µm), which whilst similar in size and external morphology, were apparently formed by further assisted-assembly by two significantly different mechanisms. Heat treatment, which increased vacuole size, involved kafirin polymerization by disulfide bonding with the microparticles being formed from round, coalesced nanostructures, as shown by AFM. Kafirin polymerization of glutaraldehyde treated microparticles was not by disulfide bonding and the nanostructures, as revealed by AFM, were spindle shaped. Both treatments enhanced BMP-2 binding to the microparticles, probably due to their increased size. Thus, these modified kafirin microparticles have potential as natural, non-animal protein bio-active scaffolds.

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Kafirin structure and functionality

Cited by 261 publications

References 48 publications

Sorghum: An Underutilized Cereal Whole Grain with the Potential to Assist in the Prevention of Chronic Disease

Sorghum: An Underutilized Cereal Whole Grain with the Potential to Assist in the Prevention of Chronic Disease

Transgenic Sorghum with Altered Kafirin Synthesis: Kafirin Solubility, Polymerization, and Protein Digestion

Physicochemical Modification of Kafirin Microparticles and Their Ability To Bind Bone Morphogenetic Protein-2 (BMP-2), for Application as a Biomaterial

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