Enzymatic Properties of Pectin Esterase from Aspergillus sp.
Hyung-Ik Song, Tae-Shick Yu, Ki-Taek Chung
Abstract
Hyung-Ik Song, Tae-Shick Yu, Ki-Taek Chung
Abstract
The enzymatic properties of pectin esterase from Aspergillus sp. were studied. The optimum conditions for the enzyme reaction were pH 4.2 and temperature of . The crude enzyme was very stable at pH range of , but about 20 percent of activity was lost at the range of pH . The crude enzyme was very stable at for one hour, however almost 100 percent of enzyme activity was lost at for 30 minutes. The pectin esterase activity of crude enzyme was greatly inhibited by addition of sodium chloride at lower pH range. That is, the inhibition rates of enzyme activity at pH 3.0 and 4.0 were 47% and 28% in concentration of 1M sodium chloride, respectively. The enzyme activity was not affected by sodium chloride at pH 7.0 at different concentration of sodium chloride. Although the enzyme activity was not affected by addition of sucrose, it was slightly inhibited at higher concentration of sucrose.
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The enzymatic properties of pectin esterase from Aspergillus sp. were studied. The optimum conditions for the enzyme reaction were pH 4.2 and temperature of . The crude enzyme was very stable at pH range of , but about 20 percent of activity was lost at the range of pH . The crude enzyme was very stable at for one hour, however almost 100 percent of enzyme activity was lost at for 30 minutes. The pectin esterase activity of crude enzyme was greatly inhibited by addition of sodium chloride at lower pH range. That is, the inhibition rates of enzyme activity at pH 3.0 and 4.0 were 47% and 28% in concentration of 1M sodium chloride, respectively. The enzyme activity was not affected by sodium chloride at pH 7.0 at different concentration of sodium chloride. Although the enzyme activity was not affected by addition of sucrose, it was slightly inhibited at higher concentration of sucrose.
Key concepts: Chemistry, Pectin, Esterase, Sodium, Enzyme, Enzyme assay, Sucrose, Pectinase