Effect of Potato Tuber Exposure to UV-C Radiation and Semi-Product Soaking in Water on Acrylamide Content in French Fries Dry Matter

This study aims to determine the effect of raw potato tubers’ exposure to UV-C radiation and semi-products soaking in water on the content of acrylamide in the dry matter of French fries. The French fries were prepared from tubers of the Innovator variety of potato (Solanum tuberosum L.). Acrylamide contents were determined by HPLC-UV/Vis on a C-18 column after extraction of fried potatoes with acetonitrile. Potato tubers exposure to UV-C radiation caused an increase in acrylamide content and the soaking of semi-products in water caused a decrease in acrylamide content in the dry matter of French fries.

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PPemberian Rizobakteri dan Coumarin pada Pertumbuhan dan Pembentukan Umbi Tanaman Kentang (Solanum tuberosum L)

10.31227/osf.io/bh8d7 ◽

2019 ◽

Cited By ~ 1

Author(s):

hennypuspitasari ◽

Warnita

Keyword(s):

Solanum Tuberosum ◽

Potato Tuber ◽

Solanum Tuberosum L ◽

Growth And Yield ◽

Growth Inhibitors ◽

Potato Tubers ◽

Potato Plants ◽

Randomized Design ◽

Potato Crops

Research on the growth and formation of potato tubers was conducted to determine the effect of rhizobacteria isolates and coumarin applications growth inhibitors. Bacteria are isolated from the roots of potato plants that grow in the healthy roots of potato plants.The study used a two-factor complete randomized design with three replications. The first factor was rhizobacterial isolates BT.4.1 isolates, BT.4.2 isolates, BT.4.3 isolates. The second factor was the concentration of coumarin 0, 50, 100 and 150 mg L-1. Thus from the results of this study obtained of rhizobacteria BT.4.1, BT.4.3 and coumarin 100 - 150 mg L-1 increases the growth and yield of potato crops. Based on the results of potato tuber produced, the combination of BT.4.1 rhizobacteria, and coumarin 150 mg L-1 can increase growth and yield.

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The influence of light upon glycoalkaloid and chlorophyll accumulation in potato tubers (Solanum tuberosum L.)

Plant Science ◽

10.1016/s0168-9452(99)00081-3 ◽

1999 ◽

Vol 145 (2) ◽

pp. 99-107 ◽

Cited By ~ 21

Author(s):

G.C Percival

Keyword(s):

Solanum Tuberosum ◽

Solanum Tuberosum L ◽

Potato Tubers ◽

Chlorophyll Accumulation

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Cathepsin D Inhibitor from Potato Tubers (Solanum tuberosum L.)

Advances in Experimental Medicine and Biology - Structure and Function of the Aspartic Proteinases ◽

10.1007/978-1-4684-6012-4_42 ◽

1991 ◽

pp. 349-353 ◽

Cited By ~ 2

Author(s):

M. Mareš ◽

M. Fusek ◽

V. Kostka ◽

M. Baudyš

Keyword(s):

Solanum Tuberosum ◽

Cathepsin D ◽

Solanum Tuberosum L ◽

Potato Tubers

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Polyacrylamid-Elektrophorese zur Beurteilung von Proteinen der Kartoffel (Solanum tuberosum L.)

Zeitschrift für Naturforschung B ◽

10.1515/znb-1966-0914 ◽

1966 ◽

Vol 21 (9) ◽

pp. 879-888 ◽

Cited By ~ 10

Author(s):

Volkmar Loeschcke ◽

Hermann Stegemann

Keyword(s):

Ascorbic Acid ◽

Solanum Tuberosum ◽

Pore Size ◽

Plant Material ◽

Solanum Tuberosum L ◽

Protein Pattern ◽

Potato Tubers ◽

Active Inhibitor ◽

Electrophoretic Behavior ◽

Acidic Proteins

Up to 25 proteins have been found in the sap of potato tubers by polyacrylamid electrophoresis. The mode of preparation and concentration of the plant material was investigated as well as the pretreatment of the polyacrylamid gel to avoid undue retardation of the migrating bands.Sulfite was the most active inhibitor of sap-browning compared with ascorbic acid and cysteine. which did not influence the protein pattern except for one line. The juice had to be dialyzed or filtered through Sephadex G 25 to remove an unkown acidic material which interferes with the more acidic proteins and causes spreading and diffusing of bands. Proteins were concentrated by means of Carbowax MW 20000. For best results ionic contaminations inherent in the gels was removed by electrophoresis before applying the proteins or dyes. Very few proteins were affected by decreasing the pore size of the gel. Ammonium sulfate (40% saturation) precipitated mainly those proteins which are similar in electrophoretic behavior to the albumin- and transferrinregion of human plasma.

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