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Stability of artificial oil bodies constituted with recombinant caleosins.
J Agric Food Chem. 2009 Mar 25; 57(6):2308-13.JA

Abstract

Caleosin is a unique calcium binding protein anchoring to the surface of seed oil bodies by its central hydrophobic domain composed of an amphiphatic alpha-helix and a proline-knot subdomain. Stable artificial oil bodies were successfully constituted with recombinant caleosin overexpressed in Escherichia coli. The stability of artificial oil bodies was slightly or severely reduced when the amphiphatic alpha-helix or proline-knot subdomain in the hydrophobic domain of caleosin was truncated. Deletion of the entire central hydrophobic domain substantially increased the solubility of the recombinant caleosin, leading to a complete loss of its capability to stabilize these oil bodies. A recombinant protein engineered with the hydrophobic domain of caleosin replaced by that of oleosin, the abundant structural protein of seed oil bodies, could stabilize the artificial oil bodies, in terms of thermo- and structural stability, as effectively as caleosin or oleosin.

Authors+Show Affiliations

Graduate Institute of Biotechnology, National Chung-Hsing University, Taichung, TaiwanNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19216529

Citation

Liu, Ting-hang, et al. "Stability of Artificial Oil Bodies Constituted With Recombinant Caleosins." Journal of Agricultural and Food Chemistry, vol. 57, no. 6, 2009, pp. 2308-13.
Liu TH, Chyan CL, Li FY, et al. Stability of artificial oil bodies constituted with recombinant caleosins. J Agric Food Chem. 2009;57(6):2308-13.
Liu, T. H., Chyan, C. L., Li, F. Y., & Tzen, J. T. (2009). Stability of artificial oil bodies constituted with recombinant caleosins. Journal of Agricultural and Food Chemistry, 57(6), 2308-13. https://doi.org/10.1021/jf803566w
Liu TH, et al. Stability of Artificial Oil Bodies Constituted With Recombinant Caleosins. J Agric Food Chem. 2009 Mar 25;57(6):2308-13. PubMed PMID: 19216529.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Stability of artificial oil bodies constituted with recombinant caleosins. AU - Liu,Ting-hang, AU - Chyan,Chia-lin, AU - Li,Feng-yin, AU - Tzen,Jason T C, PY - 2009/2/17/entrez PY - 2009/2/17/pubmed PY - 2009/5/7/medline SP - 2308 EP - 13 JF - Journal of agricultural and food chemistry JO - J Agric Food Chem VL - 57 IS - 6 N2 - Caleosin is a unique calcium binding protein anchoring to the surface of seed oil bodies by its central hydrophobic domain composed of an amphiphatic alpha-helix and a proline-knot subdomain. Stable artificial oil bodies were successfully constituted with recombinant caleosin overexpressed in Escherichia coli. The stability of artificial oil bodies was slightly or severely reduced when the amphiphatic alpha-helix or proline-knot subdomain in the hydrophobic domain of caleosin was truncated. Deletion of the entire central hydrophobic domain substantially increased the solubility of the recombinant caleosin, leading to a complete loss of its capability to stabilize these oil bodies. A recombinant protein engineered with the hydrophobic domain of caleosin replaced by that of oleosin, the abundant structural protein of seed oil bodies, could stabilize the artificial oil bodies, in terms of thermo- and structural stability, as effectively as caleosin or oleosin. SN - 1520-5118 UR - https://www.unboundmedicine.com/medline/citation/19216529/Stability_of_artificial_oil_bodies_constituted_with_recombinant_caleosins_ L2 - https://doi.org/10.1021/jf803566w DB - PRIME DP - Unbound Medicine ER -