2013
DOI: 10.1094/cchem-12-12-0165-ia
|View full text |Cite
|
Sign up to set email alerts
|

Developments in the Science of Zein, Kafirin, and Gluten Protein Bioplastic Materials

Abstract: Despite much research, there are very few commercial prolamin bio-plastics. The major reason, apart from their high cost, is that they have inferior functional properties compared to synthetic polymer plastics. This is because the prolamins are complex, each consisting of several classes and sub-classes and the functional properties of their bio-plastics are greatly affected by water. Prolamin bio-plastics are produced by protein aggregation from a solvent or by thermoplastic processing. Recent research indica… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

0
36
0

Year Published

2013
2013
2021
2021

Publication Types

Select...
7
2

Relationship

3
6

Authors

Journals

citations
Cited by 58 publications
(36 citation statements)
references
References 145 publications
(142 reference statements)
0
36
0
Order By: Relevance
“…Also, both zein and kafirin are considerably more hydrophobic than gluten.. Presumably as a consequence of their greater hydrophobicity and different secondary structure, zein and kafirin have a higher glass transition temperature (T g ) than gluten (Taylor et al, 2013a). The prolamins of pearl millet, pennisetin, whilst less studied, are considered to be similar to α-zein in structure (Bugs et al, 2004).…”
Section: Composition and Structure Of The Storage Proteins Of Non-whementioning
confidence: 99%
“…Also, both zein and kafirin are considerably more hydrophobic than gluten.. Presumably as a consequence of their greater hydrophobicity and different secondary structure, zein and kafirin have a higher glass transition temperature (T g ) than gluten (Taylor et al, 2013a). The prolamins of pearl millet, pennisetin, whilst less studied, are considered to be similar to α-zein in structure (Bugs et al, 2004).…”
Section: Composition and Structure Of The Storage Proteins Of Non-whementioning
confidence: 99%
“…Without this, the structure of the microparticles would be destabilized, as demonstrated. This suggestion is based on a model for kafirin microparticles formation 17 using an analogy of protein body formation but in an isolated and non-cellular system. The model describes that the microparticles form by precipitation of α-and β-kafirin around small particles of undissolved kafirin and then the γ-kafirin forms a stabilizing layer on the surface of the partially formed microparticle.…”
Section: Effect Of γ-Kafirin On the Morphology Of Kafirin "Micropartimentioning
confidence: 99%
“…All prolamins are recognized water insoluble in their native conformation in protein bodies within endoplasmic reticulum originated vacuoles, and they are extractable in water/alcohol mixtures. 39) Despite predominant content of hydrophobic amino acid residues, prolamins from different cereal seeds have different hydrophilic characteristic. 39,40) It was evident that a number of prolamins in wheat, barley, and rye could be directly extracted in water or 0.5 M NaCl at room temperature.…”
Section: Discussionmentioning
confidence: 99%
“…39) Despite predominant content of hydrophobic amino acid residues, prolamins from different cereal seeds have different hydrophilic characteristic. 39,40) It was evident that a number of prolamins in wheat, barley, and rye could be directly extracted in water or 0.5 M NaCl at room temperature. 41) These prolamins probably exhibit their water solubility once vacuolar free.…”
Section: Discussionmentioning
confidence: 99%