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- W2186364320 abstract "The enzyme invertase (β-D-fructofuranoside fructohydrolase; E.C. 3.2.1.26) was isolated and partially purifi ed from healthy tomato juice. The purifi cation involved buffer extraction, DEAE- cellulose and Sephadex G-75 chromatography. The purity of the enzyme preparation was determined by SDS-PAGE. The enzyme was purifi ed 29.9 fold with 23.19% yield, giving a fi nal specifi c activity 87.62 U/mg. The molecular weights of the purifi ed enzymes measured by gel fi ltration chromatogra- phy and SDS-PAGE were found to be 54 kDa and 49 kDa, respectively. The purifi ed invertase was a glycoprotein with 17.5% sugar. The optimum pH of the purifi ed enzyme was 5.5 and the activity was stable at pH 3.5-7.5. The enzyme showed maximum activity at 35oC and was found to be stable at the temperature ranged from 10oC to 35oC. The K m value of this enzyme for sucrose was 4.5 mM at pH 5. Tris, glucose and fructose reduced invertase activities poorly while urea, EDTA, acetic acid, Zn 2+ and Cd 2 + decreased moderately. Ag+ and Al 3 + produced a slight inhibitory effect on invertase activity. Ca 2+ had almost no effect on tomato invertase activity. Mn 2+ , Mg 2+ , K+, Na+ and Ba 2+ increased invertase activity slightly, while Cu 2+ accelerate invertase action moderately. Hg 2+ almost completely ceased the" @default.
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- W2186364320 date "2007-01-01" @default.
- W2186364320 modified "2023-09-27" @default.
- W2186364320 title "EXTRACTION, PARTIAL PURIFICATION AND CHARACTERIZATION OF TOMATO INVERTASE" @default.
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