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Enzymatic Properties of an Alkaline and Chelator Resistant alpha-amylase from the Alkaliphilic Bacillus sp. Isolate L1711An alkaliphilic amylase producing bacterium, Bacillus sp. strain L 711, was selected among 13 soda lakes isolates. When grown at pH 10.5 and 37 C, strain L711 produced multiple forms of amylases in the culture broth. One of these, BAA, was purified from the culture supernatant by QAE column chromatography and preparative native gel electrophoresis. The molecular weight of BAA was determined to be 51 kDa by denaturing gel electrophoresis. The pH optima for activity below and above 40 C were 9.5 - 10.0 and 7.0 - 7.5 respectively. BAA was stable in the pH range 6-11 and was completely inactivated at 55 C. The thermostability was not increased in the presence of Ca(2+). The enzyme was strongly inhibited by Ca(2+), Zn(2+), Mg(2+), Mn(2+), Ba(2+) and Cu(2+), whereas the presence of Na(+), Co(2+) and EDTA (10 mM) enhanced enzymatic activity. The K(sub m), and specific activity of BAA on soluble starch were 1.9 mg/ml and 18.5 U/mg respectively. The main end products of hydrolysis were maltotetraose, maltose and glucose.
Document ID
20040050234
Acquisition Source
Marshall Space Flight Center
Document Type
Preprint (Draft being sent to journal)
Authors
Bernhardsdotter, Eva C. M. J.
(Alabama Univ. Huntsville, AL, United States)
Pusey, Marc L.
(NASA Marshall Space Flight Center Huntsville, AL, United States)
Ng, Joseph D.
(Alabama Univ. Huntsville, AL, United States)
Garriott, Owen K.
(Alabama Univ. Huntsville, AL, United States)
Date Acquired
August 21, 2013
Publication Date
January 1, 2004
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Work of the US Gov. Public Use Permitted.

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