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Cloning and characterization of a maltotriose-producing α-amylase gene from Thermobifida fusca

Cloning and characterization of a maltotriose-producing α-amylase gene from Thermobifida fusca The gene (tfa), encoding a maltotriose-producing α-amylase from Thermobifida fusca NTU22, was cloned, sequenced and expressed in Escherichia coli. The gene consists of 1,815 base pairs and encodes a protein of 605 amino acids. The base composition of the tfa coding sequence is 69% G+C and the protein has a predicted pI value of 5.5. The deduced amino acid sequence of the tfa amylase exhibited a high degree of similarity with amylases from Thermomonospora curvata and Streptomyces amylases. The purified amylase could be detected as a single band of about 65 kDa by SDS-polyacrylamide gel electrophoresis and this agrees with the predicted size based on the nucleotide sequence. The optimal pH and temperature of the purified amylase were 7.0 and 60°C, respectively. The properties of purified amylase from the E. coli transformant are similar to that of an amylase purified from the original T. fusca NTU22. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Industrial Microbiology Biotechnology Springer Journals

Cloning and characterization of a maltotriose-producing α-amylase gene from Thermobifida fusca

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References (41)

Publisher
Springer Journals
Copyright
Copyright © 2006 by Society for Industrial Microbiology
Subject
Chemistry; Microbial Genetics and Genomics; Microbiology ; Bioinformatics; Biochemistry, general; Genetic Engineering; Biotechnology
ISSN
1367-5435
eISSN
1476-5535
DOI
10.1007/s10295-006-0200-6
pmid
17211634
Publisher site
See Article on Publisher Site

Abstract

The gene (tfa), encoding a maltotriose-producing α-amylase from Thermobifida fusca NTU22, was cloned, sequenced and expressed in Escherichia coli. The gene consists of 1,815 base pairs and encodes a protein of 605 amino acids. The base composition of the tfa coding sequence is 69% G+C and the protein has a predicted pI value of 5.5. The deduced amino acid sequence of the tfa amylase exhibited a high degree of similarity with amylases from Thermomonospora curvata and Streptomyces amylases. The purified amylase could be detected as a single band of about 65 kDa by SDS-polyacrylamide gel electrophoresis and this agrees with the predicted size based on the nucleotide sequence. The optimal pH and temperature of the purified amylase were 7.0 and 60°C, respectively. The properties of purified amylase from the E. coli transformant are similar to that of an amylase purified from the original T. fusca NTU22.

Journal

Journal of Industrial Microbiology BiotechnologySpringer Journals

Published: Jan 9, 2007

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