Prak, K;
Naka, M;
Tandang-Silvas, MR;
Kriston-Vizi, J;
Maruyama, N;
Utsumi, S;
(2015)
Polypeptide modification: an improved proglycinin design to stabilise oil-in-water emulsions.
Protein Engineering Design & Selection
, 28
(9)
pp. 281-291.
10.1093/protein/gzv031.
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Abstract
β-Conglycinin and glycinin are soybean major seed storage proteins. Previous studies have shown that adding the extension region of β-conglycinin α subunit improves the emulsifying properties of proglycinin and confers more favourable characteristics than fusing the extension region of β-conglycinin α' subunit or the hypervariable regions (A4IV) of glycinin A1aB1b subunit. To evaluate the polypeptide properties, we designed mutants of A1aB1b subunits fused with truncated versions of A4IV (A4IVcut), α (αcut) or α' (α'cut) extension regions lacking the C-terminus 25 or 31 residues (A4IVC25, αC25 or α'C31), and also A4IVcut and α'cut with αC25 residues added (A4IVcut-αC25 and α'cut-αC25). All the modified proteins displayed conformations similar to the wild type. With good solubilities, the emulsion properties of the modified proteins were much better at ionic strength μ = 0.08 than at μ = 0.5. The modified A1aB1bαcut and A1aB1bα'cut showed poorer emulsion properties than those of A1aB1bα and A1aB1bα'. Replacing the hydrophobic A4IVC25 region of A1aB1bA4IV with hydrophilic αC25 created A1aB1bA4IVcut-αC25, which had the best emulsion stability among these proglycinin mutants. We found that addition of αC25 improves the emulsifying properties of two C-terminally truncated proglycinin variants, thereby illustrating its potential general utility. Our investigation showed that in order to improve the emulsifying ability and emulsion stability of a globular protein, the introduced polypeptide should (i) be highly hydrophilic, (ii) consist of multiple hydrophobic-strong hydrophilic regions comprising at least two alpha helixes, (iii) harbour a terminal α-helix at the end of the C-terminus and (iv) have properties similar to those of αC25.
| Type: | Article |
|---|---|
| Title: | Polypeptide modification: an improved proglycinin design to stabilise oil-in-water emulsions |
| Location: | England |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1093/protein/gzv031 |
| Publisher version: | http://dx.doi.org/10.1093/protein/gzv031 |
| Language: | English |
| Additional information: | This is a pre-copyedited, author-produced PDF of an article accepted for publication in Protein Engineering Design & Selection following peer review. The version of record Protein Engineering, Design and Selection (2015) 28 (9): 281-291. doi: 10.1093/protein/gzv031 is available online at: http://dx.doi.org/10.1093/protein/gzv031 |
| Keywords: | emulsion, glycinin, polypeptide properties, protein engineering, protein interface |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Lab for Molecular Cell Bio MRC-UCL |
| URI: | https://discovery.ucl.ac.uk/id/eprint/1470060 |
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