Purifikasi dan Karakterisasi α-amilase Termostabil dari Bacillus stearothermophilus TII-12

Puji Lestari, Nur Richana, Abdul Aziz Darwis, Khaswar Syamsu, Untung Murdiyatmo

Abstract


Purification and Characterization of Thermostable
α-amylase from Bacillus stearothermophilus TII-12. Puji
Lestari, Nur Richana, Abdul A. Darwis, Khaswar Syamsu,
and Untung Murdiyatmo. Thermostable α-amylase is a
potential enzyme employed in the starch processing and
widely used in food industries, but this enzyme is still
imported. The local enzyme production would be more
economist and useful for its broad applications. Here we
report α-amylase from indigenous bacteria TII-12 which was
purified and characterized, as well as analyzed its hydrolysis
product on cassava starch. The enzyme of Bacillus
stearothermophilus TII-12 partially purified by ultrafiltration,
acetone precipitation and gel filtration (Sephadex G-100)
showed the reduced total activity, total protein and yield, but
increased the specific activity. The enzyme had a Km of 1,06
mg/ml and Vmax of 1,21 mol/min, with optimal activity at pH 7
and 90oC. An apparent molecular mass was of 192.932,8
Dalton, as estimated by Native-Polyacrylamide Agarose Gel
electrophoresis. Its activity was inhibited by the divalent
cation chelator such as EDTA and CuSO4 but activated by
calcium ion. Hydrolysis products of this enzyme on cassava
starch were glucose, dextrin, maltose and oligosaccharides.
After 24 hours of hydrolysis, the concentration of glucose
and maltose reached 51.970 and 10.090 ppm, respectively.
The thermostable α-amylase of TII-12 is an endo-α-amylase
and prospective to be applied on starch liquefaction with
high temperature process.


Keywords


Bacillus stearothermophilus; characterization; purification; thermostable α-amylase

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DOI: http://dx.doi.org/10.21082/jbio.v7n1.2011.p56-62

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P-ISSN : 1907-1094
E-ISSN : 2549-1547


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