Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 432519
Title Expression of an engineered granule-bound Escherichia coli glycogen branching enzyme in potato results in severe morphological changes in starch granules
Author(s) Huang, X.; Nazarian Firouzabadi, F.; Vincken, J.P.; Ji, Q.; Suurs, L.C.J.M.; Visser, R.G.F.; Trindade, L.M.
Source Plant Biotechnology Journal 11 (2013)4. - ISSN 1467-7644 - p. 470 - 479.
DOI https://doi.org/10.1111/pbi.12033
Department(s) Plant Breeding
Food Chemistry
Plant Breeding
EPS
Publication type Refereed Article in a scientific journal
Publication year 2013
Keyword(s) binding domain - gene-expression - beta-amylase - freeze-thaw - amylose - biosynthesis - amylopectin - arabidopsis - synthase - protein
Abstract The Escherichia coli glycogen branching enzyme (GLGB) was fused to either the C- or N-terminus of a starch-binding domain (SBD) and expressed in two potato genetic backgrounds: the amylose-free mutant (amf) and an amylose-containing line (Kardal). Regardless of background or construct used, a large amount of GLGB/SBD fusion protein was accumulated inside the starch granules, however, without an increase in branching. The presence of GLGB/SBD fusion proteins resulted in altered morphology of the starch granules in both genetic backgrounds. In the amf genetic background, the starch granules showed both amalgamated granules and porous starch granules, whereas in Kardal background, the starch granules showed an irregular rough surface. The altered starch granules in both amf and Kardal backgrounds were visible from the initial stage of potato tuber development. High-throughput transcriptomic analysis showed that expression of GLGB/SBD fusion protein in potato tubers did not affect the expression level of most genes directly involved in the starch biosynthesis except for the up-regulation of a beta-amylase gene in Kardal background. The beta-amylase protein could be responsible for the degradation of the extra branches potentially introduced by GLGB.
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