Production of dextran in transgenic potato plants

Kok‐Jacon, Géraldine A.; Vincken, Jean‐Paul; Suurs, L.C.J.M.; Wang, Guoyin; Liu, Shaoyi; Visser, Richard G. F.

doi:10.1007/s11248-005-0439-0

Cited by 18 publications

(19 citation statements)

References 33 publications

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“…Similar observations were made for Kardal and amf potato transformants expressing the Leuconostoc mesenteroides DSRS gene (Kok-Jacon et al 2005b). With this study, we provide a second example that the amf background might be less suitable for the production of carbohydrate polymers or oligomers from sucrose.…”

Section: Granule Targeting Of Gtficat Without Covalent Attachment Of supporting

confidence: 82%

“…Internodal stem segments from the tetraploid (cv. Kardal (KD)) and diploid mutant (amf) potato genotypes were used for Agrobacterium-mediated transformation, which was performed as described by Kok-Jacon et al (2005b).…”

Section: Preparation Of Constructs Containingmentioning

confidence: 99%

“…Semi-quantitative RT-PCR was performed as described by Kok-Jacon et al (2005b). GtfIRT primers, 5¢-CCGTGCTTACAGTACCTCAGC-3¢ and 5¢-GGTCGTTAGCATTGTAGGTGAAA-3¢ (Tm = 59°C, 35 cycles) were based on the GtfI gene sequence (Ferretti et al 1987).…”

Section: Starch Isolationmentioning

confidence: 99%

“…Mutan polymers were visualized with LM, and the exo-mutanase treatment was performed as described by Kok-Jacon et al (2005a). Median values of the granule size distribution (d 50 ), gelatinization behaviour, amylose content, starch content, and chain length distri- butions (HPSEC, HPAEC) were determined as described by Kok-Jacon et al (2005b).…”

Section: Starch Isolationmentioning

confidence: 99%

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Fusion proteins comprising the catalytic domain of mutansucrase and a starch-binding domain can alter the morphology of amylose-free potato starch granules during biosynthesis

et al. 2006

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It has been shown previously that mutan can be co-synthesized with starch when a truncated mutansucrase (GtfICAT) is directed to potato tuber amyloplasts. The mutan seemed to adhere to the isolated starch granules, but it was not incorporated in the starch granules. In this study, GtfICAT was fused to the N-or C-terminus of a starch-binding domain (SBD). These constructs were introduced into two genetically different potato backgrounds (cv. Kardal and amf), in order to bring GtfICAT in more intimate contact with growing starch granules, and to facilitate the incorporation of mutan polymers in starch. Fusion proteins of the appropriate size were evidenced in starch granules, particularly in the amf background. The starches from the various GtfICAT/ SBD transformants seemed to contain less mutan than those from transformants with GtfICAT alone, suggesting that the appended SBD might inhibit the activity of GtfICAT in the engineered fusion proteins. Scanning electron microscopy showed that expression of SBD-GtfICAT resulted in alterations of granule morphology in both genetic backgrounds. Surprisingly, the amf starches containing SBD-GtfICAT had a spongeous appearance, i.e., the granule surface contained many small holes and grooves, suggesting that this fusion protein can interfere with the lateral interactions

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Section: Granule Targeting Of Gtficat Without Covalent Attachment Of supporting

confidence: 82%

Section: Preparation Of Constructs Containingmentioning

confidence: 99%

Section: Starch Isolationmentioning

confidence: 99%

Section: Starch Isolationmentioning

confidence: 99%

See 2 more Smart Citations

Fusion proteins comprising the catalytic domain of mutansucrase and a starch-binding domain can alter the morphology of amylose-free potato starch granules during biosynthesis

et al. 2006

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“…Its high molecular weight and heterogeneity made it impossible to resolve on a HPLC column which provides a more direct assay to measure polymers with a low degree of polymerization (Sevenier et al 1998; this study). Kok-Jason et al (2005) reported a method to detect dextrans in transgenic corn seeds with ELISA (enzyme-linked immunosorbent assay) using a monoclonal anti-a-(1fi6) dextran antibody that recognizes the terminal non-reducing end of the polysaccharide. Our glucan quantification method took the advantage of the high percentage of a-(1fi6) and the low percentage of a-(1fi4) linkages present in the GTF-D glucan.…”

Section: Discussionmentioning

confidence: 99%

High level accumulation of α-glucan in maize kernels by expressing the gtfD gene from Streptococcus mutans

et al. 2006

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Glucosyltransferases (GTFs, EC.2.4.1.5) are bacterial enzymes that catalyze the polymerization of glucose residues from sucrose, leading to the production of high molecular weight glucan with a-1,3 /a-1,6 linkages. Such glucans, with many potential food and industrial applications, do not normally exist in higher plants. We fused a mutant form of the gtfD gene from Sreptococcus mutans with the maize (Zea mays L.) chloroplastic Brittle 1 transit peptide for amyloplast targeting. This construct, driven by the ubiquitin promoter, was introduced into maize by Agrobacterium-mediated transformation. We developed a novel HPLC-based method that enabled us differentially to distinguish transgene glucan from other endogenous polysaccharides in maize kernels. Using this method, we screened over 100 transgenic plants for the presence of GTF-produced glucan whose content varied between 0.8 and 14% of dry weight in the mature transgenic seeds. The mature transgenic plants were indistinguishable from wildtype plants in growth rate and morphology. Furthermore, starch granule size in the transgenic maize kernel was unaffected by the accumulation of the foreign polysaccharide. Mutation in Sh2, which encodes a subunit of ADP-glucose pyrophosphorylase, had no effect on glucan accumulation caused by gtfD expression. Our results indicated that high levels of novel carbohydrate polymer can be accumulated in crop plants through transgene technology.

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Transgenic Vegetable Crops: Progress, Potentials, and Prospects

Dias

Ortíz

2011

Plant Breeding Reviews

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Production of dextran in transgenic potato plants

Cited by 18 publications

References 33 publications

Fusion proteins comprising the catalytic domain of mutansucrase and a starch-binding domain can alter the morphology of amylose-free potato starch granules during biosynthesis

Fusion proteins comprising the catalytic domain of mutansucrase and a starch-binding domain can alter the morphology of amylose-free potato starch granules during biosynthesis

High level accumulation of α-glucan in maize kernels by expressing the gtfD gene from Streptococcus mutans

Transgenic Vegetable Crops: Progress, Potentials, and Prospects

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