Characterisation of Sorghum Kafirins in Relation to their Cross-linking Behaviour

Nour, I. N. A. El; Peruffo, A. Dal Belin; Curioni, Andrea

doi:10.1006/jcrs.1998.0185

Cited by 80 publications

(90 citation statements)

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“…Under both non-reducing and reducing conditions at least six 8 monomeric kafirin bands with apparent molecular weights ranging from approx. 18 to 27 kDa were present, as was described by El Nour et al (15). The individual kafirin monomers are not identified as unpublished work (Dr R. Jung, Pioneer Hi-Bred, personal communication) showed that the important 27 kDa gamma-kafirin was not separated from the alpha-kafirins by SDS-PAGE in these sorghum lines.…”

Section: Resultsmentioning

confidence: 60%

“…The latter have been identified as disulfidebonded kafirins, pre-existing in the endosperm tissue (8,15,16). Of significance is that the band intensities of the monomers and the number of resolving bands for the dimers were significantly higher in the TG lines (black arrows) compared to their Cs, HD and Macia.…”

Section: Resultsmentioning

confidence: 94%

“…With regard to the nature of the kafirins in the TG lines, it is significant that extraction with 60% tert-butanol alone extracted substantially more kafirin-1 (8,15,16) from the TG lines (approx. 69% of total kafirin extracted) compared to their Cs (40-42%), HD (43%) and Macia (56%) ( Table 1).…”

Section: Resultsmentioning

confidence: 99%

“…Together, these results clearly show that the kafirin-1 in the TG lines was much less polymerized than that of their Cs, HD and Macia (Figure 3a). This can be attributed to suppression of synthesis of the cysteine-rich gamma-kafirins, which are required for polymerization through disulfide bonding (15).…”

Section: Resultsmentioning

confidence: 99%

“…Further, with SDS-PAGE under both non-reducing and reducing conditions additional high intensity low molecular weight bands (<14.4 and 6.0 kDa) were also present in kafirin-1 of the TG lines (Figure 3a, b lower black dashed arrows). These low molecular weight proteins are presumably kafirins as the extraction conditions used (60% tert-butanol extract) is specific for solubilizing prolamin proteins such as kafirin (15,18).…”

Section: Sds-page Of Kafirin-1 Under Non-reducing Conditionsmentioning

confidence: 99%

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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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Section: Resultsmentioning

confidence: 60%

Section: Resultsmentioning

confidence: 94%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Sds-page Of Kafirin-1 Under Non-reducing Conditionsmentioning

confidence: 99%

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

Silva

Taylor

2011

J. Agric. Food Chem.

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Sorghum and Millet Proteins

Bean

Ioerger

2014

Applied Food Protein Chemistry

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Do kafirin bioplastic materials have unique functional characteristics?

Taylor

2023

Cereal Chem

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Background and Objectives: There is considerable interest in kafirin, sorghum prolamin, as a bioplastic material because it apparently produces bioplastics with superior functional properties. This review evaluates the evidence, focussing on research directly comparing the properties of kafirin bioplastics (films and elastomers) with those from zein and gluten.Findings: Kafirin and zein are more hydrophobic than gluten but there is little difference in hydrophobicity between them. Kafirin and zein films have better moisture barrier properties than gluten films. Films made from total kafirin (α-, β-, and γ-kafirins) are stronger and take up less moisture than films from commercial zein (essentially α-zein). However, total kafirin-and total zein films have similar moisture uptake. Also, there is little difference in oxygen barrier properties between total kafirin-and commercial zein films. Total kafirin elastomers have better elastic recovery than commercial-and total zein elastomers and similar elastic recovery to gluten. Conclusions:The better functional properties of kafirin bioplastics compared to commercial zein bioplastics seems to be largely due to the greater disulfide bonded polymerization of kafirin polypeptides, involving the cysteine-rich βand γ-kafirin classes. Significance and Novelty: This work should stimulate research into disulfidebonded polymerization of prolamins to improve their bioplastic functionality.

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Characterisation of Sorghum Kafirins in Relation to their Cross-linking Behaviour

Cited by 80 publications

References 0 publications

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

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

Sorghum and Millet Proteins

Do kafirin bioplastic materials have unique functional characteristics?

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