PEMEKATAN ENZIM SELULASE Penicillium sp. LBKURCC20 DENGAN PENGENDAPAN AMONIUM SULFAT 80% JENUH
Abstract
Cellulase enzyme activity of Penicillium sp. LBKURCC20 Isolate of Riau can be
increased by concentrating the enzyme using 80% saturated solid ammonium sulfate
(NH 4 ) 2 SO 4 anhydrous. Precipitated enzyme was redissolved by the addition of acetate
buffer solution pH 5.5 to 1/70 times its original volume. Cellulase enzyme activity was
determined using substrates CMC and avicel. CMCase and avicelase enzyme activity of
the crude enzyme was (0.0164 ± 0.0036) U/mL and (0.003 ± 0.0025) U/mL,
respectively. CMCase and avicelase enzyme activity after concentration was (0.219 ±
0.0579) U/mL and (0.03 ± 0.03) U/mL, respectively. The test results showed that the
activity of concentrated CMCase increased 13.5 times and avicelase enzyme activity
increased 10 times after concentrating.
increased by concentrating the enzyme using 80% saturated solid ammonium sulfate
(NH 4 ) 2 SO 4 anhydrous. Precipitated enzyme was redissolved by the addition of acetate
buffer solution pH 5.5 to 1/70 times its original volume. Cellulase enzyme activity was
determined using substrates CMC and avicel. CMCase and avicelase enzyme activity of
the crude enzyme was (0.0164 ± 0.0036) U/mL and (0.003 ± 0.0025) U/mL,
respectively. CMCase and avicelase enzyme activity after concentration was (0.219 ±
0.0579) U/mL and (0.03 ± 0.03) U/mL, respectively. The test results showed that the
activity of concentrated CMCase increased 13.5 times and avicelase enzyme activity
increased 10 times after concentrating.
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