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Minimizing the central hydrophobic domain in oleosin for the constitution of artificial oil bodies.
J Agric Food Chem. 2007 Jul 11; 55(14):5604-10.JA

Abstract

Oleosin, a unique structural protein anchoring onto the surface of seed oil bodies by its central hydrophobic domain, stabilizes these lipid-storage organelles as discrete entities. Stable artificial oil bodies have been successfully constituted with native or recombinant oleosins. In this study, recombinant sesame oleosin with 12 residues stepwise truncated from its central hydrophobic domain of 72 residues was overexpressed in Escherichia coli, was purified to homogeneity, and was used for the constitution. Artificial oil bodies constituted by truncated oleosins with the central hydrophobic domain longer than 36 residues were as stable as native sesame oil bodies, and those constituted by truncated oleosins lacking more than half of the original central hydrophobic domain inclined to coalesce upon collision or aggregation.

Authors+Show Affiliations

Department of Biotechnology, National Formosa University, Yunlin, Taiwan.No affiliation info availableNo 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

17567149

Citation

Peng, Chi-Chung, et al. "Minimizing the Central Hydrophobic Domain in Oleosin for the Constitution of Artificial Oil Bodies." Journal of Agricultural and Food Chemistry, vol. 55, no. 14, 2007, pp. 5604-10.
Peng CC, Lee VS, Lin MY, et al. Minimizing the central hydrophobic domain in oleosin for the constitution of artificial oil bodies. J Agric Food Chem. 2007;55(14):5604-10.
Peng, C. C., Lee, V. S., Lin, M. Y., Huang, H. Y., & Tzen, J. T. (2007). Minimizing the central hydrophobic domain in oleosin for the constitution of artificial oil bodies. Journal of Agricultural and Food Chemistry, 55(14), 5604-10.
Peng CC, et al. Minimizing the Central Hydrophobic Domain in Oleosin for the Constitution of Artificial Oil Bodies. J Agric Food Chem. 2007 Jul 11;55(14):5604-10. PubMed PMID: 17567149.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Minimizing the central hydrophobic domain in oleosin for the constitution of artificial oil bodies. AU - Peng,Chi-Chung, AU - Lee,Viola S Y, AU - Lin,Meei-Yn, AU - Huang,Hsin-Yi, AU - Tzen,Jason T C, Y1 - 2007/06/14/ PY - 2007/6/15/pubmed PY - 2007/9/20/medline PY - 2007/6/15/entrez SP - 5604 EP - 10 JF - Journal of agricultural and food chemistry JO - J Agric Food Chem VL - 55 IS - 14 N2 - Oleosin, a unique structural protein anchoring onto the surface of seed oil bodies by its central hydrophobic domain, stabilizes these lipid-storage organelles as discrete entities. Stable artificial oil bodies have been successfully constituted with native or recombinant oleosins. In this study, recombinant sesame oleosin with 12 residues stepwise truncated from its central hydrophobic domain of 72 residues was overexpressed in Escherichia coli, was purified to homogeneity, and was used for the constitution. Artificial oil bodies constituted by truncated oleosins with the central hydrophobic domain longer than 36 residues were as stable as native sesame oil bodies, and those constituted by truncated oleosins lacking more than half of the original central hydrophobic domain inclined to coalesce upon collision or aggregation. SN - 0021-8561 UR - https://www.unboundmedicine.com/medline/citation/17567149/Minimizing_the_central_hydrophobic_domain_in_oleosin_for_the_constitution_of_artificial_oil_bodies_ L2 - https://doi.org/10.1021/jf070977o DB - PRIME DP - Unbound Medicine ER -