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Plants 2016, 5(3), 36; doi:10.3390/plants5030036

Structural Properties of Cruciferin and Napin of Brassica napus (Canola) Show Distinct Responses to Changes in pH and Temperature

1
Saskatoon Research and Development Centre, Agriculture and Agri-Food Canada, 107 Science Place, Saskatoon, SK S7N 0X2, Canada
2
Department of Food and Bioproduct Sciences, University of Saskatchewan, Saskatoon, SK S7N 5A8, Canada
*
Author to whom correspondence should be addressed.
Academic Editor: Milan S. Stankovic
Received: 15 March 2016 / Revised: 22 August 2016 / Accepted: 25 August 2016 / Published: 7 September 2016
(This article belongs to the Special Issue Selected/Extended Full Papers of 14th International Rapeseed Congress)
View Full-Text   |   Download PDF [5991 KB, uploaded 7 September 2016]   |  

Abstract

The two major storage proteins identified in Brassica napus (canola) were isolated and studied for their molecular composition, structural characteristics and the responses of structural features to the changes in pH and temperature. Cruciferin, a complex of six monomers, has a predominantly β-sheet-containing secondary structure. This protein showed low pH unstable tertiary structure, and distinctly different solubility behaviour with pH when intact in the seed cellular matrix. Cruciferin structure unfolds at pH 3 even at ambient temperature. Temperature-induced structure unfolding was observed above the maximum denaturation temperature of cruciferin. Napin was soluble in a wider pH range than cruciferin and has α-helices dominating secondary structure. Structural features of napin showed less sensitivity to the changes in medium pH and temperature. The surface hydrophobicity (S0) and intrinsic fluorescence of tryptophan residue appear to be good indicators of cruciferin unfolding, however they were not the best to demonstrate structural changes of napin. These two storage proteins of B. napus have distinct molecular characteristics, therefore properties and functionalities they provide are contrasting rather than complementary. View Full-Text
Keywords: canola/rapeseed; cruciferin; napin; protein; solubility; secondary structure; tertiary structure; surface hydrophobicity; intrinsic fluorescence; denaturation canola/rapeseed; cruciferin; napin; protein; solubility; secondary structure; tertiary structure; surface hydrophobicity; intrinsic fluorescence; denaturation
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Perera, S.P.; McIntosh, T.C.; Wanasundara, J.P.D. Structural Properties of Cruciferin and Napin of Brassica napus (Canola) Show Distinct Responses to Changes in pH and Temperature. Plants 2016, 5, 36.

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