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Compositional and enzymatic changes associated with the sugar-end defect in Russet Burbank potatoes

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Abstract

This study was initiated to determine the starchsugar composition and the activities of relevant enzymes of carbohydrate metabolism in Russet Burbank (cv.) potatoes exhibiting the sugar-end defect. The frequency of sugar-end tubers was increased by applying a single, transient, moisture-deficit stress period following tuberization. The following properties were unique to sugar-end tubers compared to normal tuber tissue. (1) Starch and total solids decreased markedly while glucose content increased 15-fold, (2) The concentration of Suc was markedly lower, (3) Pi was slightly but significantly increased, (4) The activities of UGPase and Susy decreased nearly 3 and 2-fold, respectively, (5) The activity of AGPase decreased 50%, (6) The ratio of STPLase to AGPase shifted over 3-fold in favor of starch mobilization, (7) Basal AcInv activity (assayed in the presence of inhibitor) increased 7-fold during storage, (8) Tuber Glc concentration showed a better correlation to basal Aclnv activity than to total Aclnv activity (inhibitor destroyed), (9) Kinetic analysis suggested that the level and/or effectiveness of the Aclnv inhibitor was decreased in the sugar-end tuber tissue. These results are discussed in relation to metabolic changes which occur in converting a starch storing tuber to one primarily involved with starch mobilization.

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Abbreviations

Aclnv:

acid invertase

AGPase:

ADP-Glc pyrophosphorylase

EDTA:

ethylenediaminetetraacetic acid

Fru:

fructose

Glc:

glucose

Glc-l-P:

glucose 1-phosphate

GSH:

glutathione

HEPES:

4-(2-hydroxyethyl)-l-piperazineethane-sulfonic acid

NADH:

reduced form of nicotinamide aderdne dinucleotide

NAD+:

oxidized form of nicotinamide adenine dinucleotide

Pi:

inorganic phosphate

PPi:

inorganic pyrophosphate

PVP:

polyvinylpyrrolidone

Sue:

sucrose

SPS:

sucrose phosphate synthase

STPLase:

starch phosphorylase

Susy:

sucrose synthase

TCA:

trichloroacetic acid

UGPase:

UDP-Glc pyrophosphorylase

YSI:

Yellow Springs Instrument

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Author notes

  1. J. R. Sowokinos

    Present address: Department of Horticultural Science, University of Minnesota, 55108, St. Paul, MN

Authors and Affiliations

  1. Stationed at the USDA/ARS Potato Research Worksite, 311 5th Avenue NE, 56721, East Grand Forks, MN

    J. R. Sowokinos

  2. Malheur Experiment Station, Oregon State University, 595 Onion Avenue, 97914, Ontario, OR

    C. C. Shock & E. P. Eldredge

  3. Yamhill SWCD, 2200 SW 2nd St, 97128, McMinnville, OR

    T. D. Stieber

Authors
  1. J. R. Sowokinos
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  2. C. C. Shock
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  3. T. D. Stieber
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  4. E. P. Eldredge
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Additional information

Agricultural Experiment Station, University of Minnesota Scientific Journal Series No. 981210038.

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Sowokinos, J.R., Shock, C.C., Stieber, T.D. et al. Compositional and enzymatic changes associated with the sugar-end defect in Russet Burbank potatoes. Am. J. Pot Res 77, 47–56 (2000). https://doi.org/10.1007/BF02853661

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