New Thermostable Amylase from Bacillus cohnii US147 with a Broad pH Applicability

A new thermophilic bacterial strain identified as Bacillus cohnii US147 was isolated from the southern Tunisian soil. The identification was based on physiological tests and molecular techniques related to the 16S ribosomal ribonucleic acid. The isolated strain produced amylase, which was purified....

Full description

Saved in:

Bibliographic Details
Published in:	Applied biochemistry and biotechnology Vol. 157; no. 1; pp. 50 - 60
Main Authors:	Ghorbel, Raoudha Ellouz, Maktouf, Sameh, Massoud, Ezedine Ben, Bejar, Samir, Chaabouni, Semia Ellouz
Format:	Journal Article
Language:	English
Published:	New York New York : Humana Press Inc 01-04-2009 Humana Press Inc Springer Springer Nature B.V
Subjects:	amylases Amylases - chemistry Amylases - isolation & purification Amylases - metabolism Bacillus Bacillus - enzymology Bacillus - growth & development Bacillus - isolation & purification Bacillus - metabolism Bacillus cohnii Bacteria Biochemistry Biological and medical sciences Biotechnology calcium Chemistry Chemistry and Materials Science EDTA (chelating agent) enzyme activity enzyme inhibition Enzyme Stability Enzymes Fundamental and applied biological sciences. Psychology Hydrogen peroxide Hydrogen-Ion Concentration Kinetics molecular weight polyacrylamide gel electrophoresis Polymers purification saccharification soil bacteria Starch Substrate Specificity Substrates Temperature thermal stability thermophilic bacteria zinc Tunisia Characterization Purification Amylase Acid and basic pH activity Bacillus cohnii . Amylase Enzyme Bacillaceae Thermal stability Bacillales Bacillus pH Bacteria Purification . Characterization
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	A new thermophilic bacterial strain identified as Bacillus cohnii US147 was isolated from the southern Tunisian soil. The identification was based on physiological tests and molecular techniques related to the 16S ribosomal ribonucleic acid. The isolated strain produced amylase, which was purified. This amylase had an apparent molecular mass of 30 kDa as estimated by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. Amylase US147 showed K m and V max values of 0.7 mg/ml and 2.2 U/ml, respectively, with starch as the substrate. The enzyme was active in acid and basic pH and had a maximal activity on starch at pH 9 and 70 °C. The enzyme was stable at pH 9 for 72 h and retained half of its activity after incubation at 70 °C for 150 min. A partially inhibition (15%, 25%, 23%, 20%, and 22%) was obtained with 1 mM SDS, 1 mM NaBO₃, 1 mM H₂O₂, 1 mM Zn⁺², and 5 mM ethylenediamine tetraacetic acid (EDTA), respectively. The amylase recovered its original activity by the addition of 10 mM Ca ²⁺ to the 5 mM EDTA. These properties indicated a possible use of this amylase in starch saccharification, in detergent, and in other industrial applications.
Bibliography:	http://dx.doi.org/10.1007/s12010-008-8278-0 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0273-2289 1559-0291
DOI:	10.1007/s12010-008-8278-0