Comparison of the N-glycosylation on recombinant miraculin expressed in tomato plants with native miraculin.

ABSTRACT: Miraculin is a promising protein with taste-modifying properties. Focusing on the unique function and potential of miraculin, recombinant miraculin production has been explored with the use of heterologous expression systems, but the activities of recombinant miraculins were much lower than those of native miraculin, probably due to the difference in post-translational modification, especially N-glycosylation. For practical use therefore, the differences between N-glycan of recombinant miraculin compared to that of native miraculin should be minimized. Here, to establish the platform for functional miraculin production, we expressed miraculin in tomato plants with the same taste-modifying activity as native miraculin purified from miracle fruit, and we compared the N-g

SUBMITTER: Kajiura H 

PROVIDER: S-EPMC6905219 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature