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An examination of methods used to assay potato tuber invertase and its naturally occurring inhibitor.

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Confirming an earlier report, it was shown that the endogenous inhibitor of potato tuber invertase forms an essentially undissociable complex with the enzyme. Consequently, several previous analyses of potato tuber invertase which were based on equations derived for highly dissociable

[Cloning of potato invertase inhibitor St-inh cDNA and its expression in E. coli and functional analysis].

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A full length cDNA clone encoding invertase inhibitor was isolated by RT-PCR combined with 5' RACE from potato (S. tuberosum) tubers of cv. JH and designated as St-inh. The encoding region of St-inh is of 663bp encoding a protein of 221 amino acids. The DNA fragment including St-inh cDNA was cloned

Tapping natural variation at functional level reveals allele specific molecular characteristics of potato invertase Pain-1.

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Biochemical, molecular and genetic studies emphasize the role of the potato vacuolar invertase Pain-1 in the accumulation of reducing sugars in potato tubers upon cold storage, and thereby its influence on the quality of potato chips and French fries. Previous studies showed that natural Pain-1 cDNA

Silencing of vacuolar invertase and asparagine synthetase genes and its impact on acrylamide formation of fried potato products.

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Acrylamide is produced in a wide variety of carbohydrate-rich foods during high-temperature cooking. Dietary acrylamide is a suspected human carcinogen, and health concerns related to dietary acrylamide have been raised worldwide. French fries and potato chips contribute a significant proportion to

Tuber-specific silencing of the acid invertase gene substantially lowers the acrylamide-forming potential of potato.

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Some popular processed foods including French fries contain small amounts of toxic acrylamide. Efforts to lower the accumulation of this reactive compound by modifying the production process have a negative effect on sensory characteristics and are not broadly applicable. This study optimized a

Inhibition of Potato Tuber Invertase by an Endogenous Inhibitor: EFFECTS OF SALTS, pH, TEMPERATURE, AND SUGARS ON BINDING .

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Binding between potato tuber invertase and its endogenous inhibitor followed second-order reaction kinetics. Binding rates were diminished by the presence of various inorganic salts, MgCl(2) being especially effective. This effect of MgCl(2) was used in binding rate studies by adding the salt with

Changes in sugar content and activity of vacuolar acid invertase during low-temperature storage of potato tubers from six Japanese cultivars.

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The storage of potato tubers at low temperatures leads to the accumulation of sugars in a process called "low-temperature sweetening." To understand this phenomenon, we measured the sugar contents and the activity of acid invertase over several months in tubers of six Japanese cultivars stored at 4

Combined expression of glucokinase and invertase in potato tubers leads to a dramatic reduction in starch accumulation and a stimulation of glycolysis.

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The original aim of this work was to increase starch accumulation in potato tubers by enhancing their capacity to metabolise sucrose.We previously reported that specific expression of a yeast invertase in the cytosol of tubers led to a 95% reduction in sucrose content, but that this was accompanied

Vacuolar invertases in sweet potato: molecular cloning, characterization, and analysis of gene expression.

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Two cDNAs (Ib beta fruct2 and Ib beta fruct3) encoding vacuolar invertases were cloned from sweet potato leaves, expressed in Pichia pastoris, and the recombinant proteins were purified by ammonium sulfate fractionation and chromatography on Ni-NTA agarose. The deduced amino acid sequences encoded

Invertase inhibitors from sweet potato (Ipomoea batatas): purification and biochemical characterization.

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Two proteinaceous invertase inhibitors, designated ITI-L and ITI-R, were purified to electrophoretic homogeneity. ITI-L was purified from acetone powder of sweet potato leaves through sequential steps entailing buffer extraction, acid treatment, DEAE-Sephacel ion-exchange chromatography, and

Invertase inhibitors from red beet, sugar beet, and sweet potato roots.

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Invertase inhibitors have been isolated and partially purified from red beets, sugar beets, and sweet potatoes. These inhibitors are thermolabile proteins with molecular weights of 18,000 to 23,000. They do not inhibit yeast and Neurospora invertases, but they are reactive with potato tuber

Expression and characterization of sweet potato invertase in Pichia pastoris.

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An invertase cDNA (Ibbetafruct1) was cloned from sweet potato leaves and characterized. The deduced amino acid sequence of the Ibbetafruct1-encoded protein was closely related to vacuolar invertases and included the WECVD catalytic domain characteristic of them. An expression plasmid containing the

Synthesis and apparent turnover of Acid invertase in relation to invertase inhibitor in wounded sweet potato root tissue.

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Previously we showed that acid invertase activity increased and then decreased rapidly in wounded sweet potato (Ipomoea batatas Liam.) root tissue, and that the tissue contained a heat-stable, proteinaceous inhibitor with a molecular weight of about 19,500 daltons.In response to wounding of sweet

Change in invertase activity of sweet potato in response to wounding and purification and properties of its invertases.

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When root tissue of sweet potato (Ipomoea batatas Lam.) was sliced, acid invertase activity, initially absent in freshly sliced tissue, appeared after a 3- to 6-hour lag phase, rapidly reached a maximum in 18 hours, and thereafter decreased. The increase in invertase activity was accompanied by a

Isolation and characterization of acid invertase inhibitor from sweet potato.

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An inhibitor of sweet potato acid invertase [EC 3.2.1.26] was found in fresh sweet potato root tissue, and partially purified. The inhibitor is possibly a thermostable protein with a molecular weight of about 19,500. The inhibitory activity is highly specific to acid invertase. The inhibitor binds

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