Pemurnian Parsial dan Karakterisasi Amilase dari Bakteri Laut Arthrobacter arilaitensis LBF-003

Dianti Rahmasari, Wijanarka Wijanarka, Sri Pujiyanto, Nanik Rahmani, Yopi Yopi
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Abstract

Starch is an abundant carbon source in nature, and ?-amylase (1, 4-?-D-glucanohydrolase; EC 3.2.1.1), which hydrolyzes ?
-1, 4-glucosidic linkage in starch-related molecules. Microbe ?-amylase production is a hydrolytic enzyme and one of
interest in its microbial production has increased dramatically due to its wide spread use in food, textile, baking and
detergent industries in recent years. Here we report ?-amylase from marine bacterium which was purified and
characterized, as well as analyzed its hydrolysis product on starch. The enzyme of Arthrobacter arilaitensis partially
purified by acetone precipitation with 90% and ion exchange chromatography produced specific activity 0.25 U/mg and
0.38 U/mg, and it’s purity rate increased until 1.14 fold compared with former crude extract. Purifed extracelluler amilase
had an optimum activity at temperature 50°C and pH 9.0. An apparent molecular mass was between 50-75 kDa, as
estimated by zimogram electrophoresis. Hydrolysis products of this enzyme on starch were maltose, maltotriose and
maltoheptaose.
Keywords: alfa amylase, marine bacterium, Arthrobacter arilaitensis, purification, charaterization

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