Characterization of a thermostable recombinant beta-galactosidase from Thermotoga maritima
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چکیده
منابع مشابه
Thermostable chemotaxis proteins from the hyperthermophilic bacterium Thermotoga maritima.
An expressed sequence tag homologous to cheA was previously isolated by random sequencing of Thermotoga maritima cDNA clones (C. W. Kim, P. Markiewicz, J. J. Lee, C. F. Schierle, and J. H. Miller, J. Mol. Biol. 231: 960-981, 1993). Oligonucleotides complementary to this sequence tag were synthesized and used to identify a clone from a T. maritima lambda library by using PCR. Two partially overl...
متن کاملMolecular Cloning and Characterization of a Gene Encoding Thermostable Pectinase from Thermotoga maritima
A gene encoding thermostable pectinase (TmPec) was isolated from hyperthermophilic microorganism, Thermotoga maritima. The open reading frame (ORF) of TmPec gene is 1,104 bp long and encodes 367 amino acid residues with a molecular weight of 40,605 Da. To analyze the enzymatic activity and biochemical properties, the ORF of TmPec gene excluding putative signal sequence of 27 amino acids was int...
متن کاملPartial characterization of the Streptomyces lividans xlnB promoter and its use for expression of a thermostable xylanase from Thermotoga maritima.
Xylanase activity assays were used to screen a Streptomyces coelicolor genomic library in Escherichia coli, and a xylanase gene that is 99% identical to the xylanase B gene (xlnB) of S. lividans (GenBank accession no. M64552) was identified. The promoter region of this gene was identified by using a transcriptional fusion between the upstream region of the S. coelicolor xlnB gene and the xylE r...
متن کاملCharacterization of acetohydroxyacid synthase from the hyperthermophilic bacterium Thermotoga maritima
Acetohydroxyacid synthase (AHAS) is the key enzyme in branched chain amino acid biosynthesis pathway. The enzyme activity and properties of a highly thermostable AHAS from the hyperthermophilic bacterium Thermotoga maritima is being reported. The catalytic and regulatory subunits of AHAS from T. maritima were over-expressed in Escherichia coli. The recombinant subunits were purified using a sim...
متن کاملPurification and characterization of two extremely thermostable enzymes, phosphate acetyltransferase and acetate kinase, from the hyperthermophilic eubacterium Thermotoga maritima.
Phosphate acetyltransferase (PTA) and acetate kinase (AK) of the hyperthermophilic eubacterium Thermotoga maritima have been purified 1,500- and 250-fold, respectively, to apparent homogeneity. PTA had an apparent molecular mass of 170 kDa and was composed of one subunit with a molecular mass of 34 kDa, suggesting a homotetramer (alpha4) structure. The N-terminal amino acid sequence showed sign...
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ژورنال
عنوان ژورنال: Journal of Applied Microbiology
سال: 2004
ISSN: 1364-5072,1365-2672
DOI: 10.1111/j.1365-2672.2004.02377.x