OPTIMASI AKTIVITAS ENZIM SELULASE YANG DIHASILKAN OLEH BAKTERI SELULOLITIK Y
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Institusion
Universitas Sriwijaya
Author
ZAHIRA, CIK RAHMA
Yanuriati, Anny
Yanuriati, Anny
Subject
S530-559 Agricultural education
Datestamp
2023-05-24 03:47:38
Abstract :
Cellulase enzymes break ?-1,4 glycosidic bonds in cellulose, cellodextrin, cellobiose and other cellulose derivatives. This research aimed to determine the highest cellulase enzyme activity of several bacterial isolates using the DNS method and to study the optimum conditions of pH, temperature, substrate and metal ion concentrations of the cellulase enzyme activity. This research used a non-factorial Completely Randomized Design (CRD) with four treatment factors repeated three times. The parameter observed was the amount of reducing sugar released in cellulase enzyme activity. The results showed cellulase enzyme activity was measured using the DNS method for 20 isolates of cellulolytic bacteria. Two bacterial isolates had the highest enzyme activity, sample code D 10-6 (39) of 10.20 U/mL and D 10-6 (44) of 8.86 U/mL. This study used the second-highest bacterial isolate, sample D(10-6) 44. The optimum conditions for cellulase activity from bacterial isolate D (10-6) 44 were at pH 7 with an activity value of 7.03 U/mL, temperature 30oC with Enzyme activity was 6.05 U/mL, substrate concentration was 0.5% with an enzyme activity value of 85.03 U/mL and the addition of FeCl2 metal ion with an enzyme activity value of 100.45 U/mL, FeCl2 metal ion acts as an activator in cellulase activity, while the addition of metal ions MgCl2, CaCl2, ZnCl2, and CuCl2 acts as an inhibitor in cellulase activity.
Cellulase enzymes break ?-1,4 glycosidic bonds in cellulose, cellodextrin, cellobiose and other cellulose derivatives. This research aimed to determine the highest cellulase enzyme activity of several bacterial isolates using the DNS method and to study the optimum conditions of pH, temperature, substrate and metal ion concentrations of the cellulase enzyme activity. This research used a non-factorial Completely Randomized Design (CRD) with four treatment factors repeated three times. The parameter observed was the amount of reducing sugar released in cellulase enzyme activity. The results showed cellulase enzyme activity was measured using the DNS method for 20 isolates of cellulolytic bacteria. Two bacterial isolates had the highest enzyme activity, sample code D 10-6 (39) of 10.20 U/mL and D 10-6 (44) of 8.86 U/mL. This study used the second-highest bacterial isolate, sample D(10-6) 44. The optimum conditions for cellulase activity from bacterial isolate D (10-6) 44 were at pH 7 with an activity value of 7.03 U/mL, temperature 30oC with Enzyme activity was 6.05 U/mL, substrate concentration was 0.5% with an enzyme activity value of 85.03 U/mL and the addition of FeCl2 metal ion with an enzyme activity value of 100.45 U/mL, FeCl2 metal ion acts as an activator in cellulase activity, while the addition of metal ions MgCl2, CaCl2, ZnCl2, and CuCl2 acts as an inhibitor in cellulase activity.
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RAMA_41231_05031281924034.pdf
RAMA_41231_05031281924034_TURNITIN.pdf
RAMA_41231_05031281924034_0030016801_01_front_ref.pdf
RAMA_41231_05031281924034_0030016801_02.pdf
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RAMA_41231_05031281924034_0030016801_04.pdf
RAMA_41231_05031281924034_0030016801_05.pdf
RAMA_41231_05031281924034_0030016801_06_ref.pdf
RAMA_41231_05031281924034_0030016801_07_Lamp.pdf
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