BIOMAT Database Logo BIOMAT Database Logo

[A new thermostable proteinase from Thermoactinomyces SP.27a. Cloning and gene expression]. 2001

M V Zabolotskaia, and E A Nosovskaia, and M A Kaplun, and I A Tsaplina, and T V Akimkina
Institute of Molecular Genetics, Russian Academy of Sciences, Moscow.

A library of Thermoactinomyces sp. 27a, producer of thermostable proteases of different groups, has been created. Gene coding for thermostable neutral proteinase was cloned and expressed in Bac. subtilis cells. Restriction map for cloned DNA fragment was created and physicochemical parameters of recombinant proteinase were characterized. The thermostability and optimum of proteolytic activity of the enzyme was lower than in the natural Thermoactinomyces sp. strain, which can be due to heterologous expression of the gene coding for thermostable protein in the mesophilic host.

UI MeSH Term Description Entries
D008848 Micromonosporaceae A family of gram-positive, saprophytic bacteria occurring in soil and aquatic environments.
D010450 Endopeptidases A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS. Endopeptidase,Peptide Peptidohydrolases
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D004795 Enzyme Stability The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat. Enzyme Stabilities,Stabilities, Enzyme,Stability, Enzyme
D006863 Hydrogen-Ion Concentration The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D006868 Hydrolysis The process of cleaving a chemical compound by the addition of a molecule of water.
D015183 Restriction Mapping Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA. Endonuclease Mapping, Restriction,Enzyme Mapping, Restriction,Site Mapping, Restriction,Analysis, Restriction Enzyme,Enzyme Analysis, Restriction,Restriction Enzyme Analysis,Analyses, Restriction Enzyme,Endonuclease Mappings, Restriction,Enzyme Analyses, Restriction,Enzyme Mappings, Restriction,Mapping, Restriction,Mapping, Restriction Endonuclease,Mapping, Restriction Enzyme,Mapping, Restriction Site,Mappings, Restriction,Mappings, Restriction Endonuclease,Mappings, Restriction Enzyme,Mappings, Restriction Site,Restriction Endonuclease Mapping,Restriction Endonuclease Mappings,Restriction Enzyme Analyses,Restriction Enzyme Mapping,Restriction Enzyme Mappings,Restriction Mappings,Restriction Site Mapping,Restriction Site Mappings,Site Mappings, Restriction

Related Publications

M V Zabolotskaia, and E A Nosovskaia, and M A Kaplun, and I A Tsaplina, and T V Akimkina
[Cloning and expression of a serine proteinase gene from Thermoactinomyces sp. in Bacillus subtilis cells].
January 1999, Molekuliarnaia genetika, mikrobiologiia i virusologiia,
M V Zabolotskaia, and E A Nosovskaia, and M A Kaplun, and I A Tsaplina, and T V Akimkina
Cloning and expression of a thermostable keratinase gene from Thermoactinomyces sp. YT06 in Escherichia coli and characterization of purified recombinant enzymes.
August 2019, World journal of microbiology & biotechnology,
M V Zabolotskaia, and E A Nosovskaia, and M A Kaplun, and I A Tsaplina, and T V Akimkina
Thermostable phenylalanine dehydrogenase of Thermoactinomyces intermedius: cloning, expression, and sequencing of its gene.
March 1991, Journal of biochemistry,
M V Zabolotskaia, and E A Nosovskaia, and M A Kaplun, and I A Tsaplina, and T V Akimkina
Cloning and expression of an intracellular alkaline protease gene from alkalophilic Thermoactinomyces sp. HS682.
February 1997, Bioscience, biotechnology, and biochemistry,
M V Zabolotskaia, and E A Nosovskaia, and M A Kaplun, and I A Tsaplina, and T V Akimkina
Cloning and expression of the ccpA gene encoding catabolite control protein from Thermoactinomyces sp. E79.
October 2000, Bioscience, biotechnology, and biochemistry,
M V Zabolotskaia, and E A Nosovskaia, and M A Kaplun, and I A Tsaplina, and T V Akimkina
Purification and characterization of a thermostable alkaline protease from alkalophilic Thermoactinomyces sp. HS682.
February 1992, Bioscience, biotechnology, and biochemistry,
M V Zabolotskaia, and E A Nosovskaia, and M A Kaplun, and I A Tsaplina, and T V Akimkina
Novel thermostable serine collagenase from Thermoactinomyces sp. 21E: purification and some properties.
January 2006, Journal of basic microbiology,
M V Zabolotskaia, and E A Nosovskaia, and M A Kaplun, and I A Tsaplina, and T V Akimkina
The purification, characterization, cloning and sequencing of the gene for a halostable and thermostable leucine dehydrogenase from Thermoactinomyces intermedius.
June 1994, European journal of biochemistry,
M V Zabolotskaia, and E A Nosovskaia, and M A Kaplun, and I A Tsaplina, and T V Akimkina
[Thermostable alkaline phosphatase from Thermus sp. FD3041: cloning of the gene and expression in Escherichia coli].
January 1998, Yi chuan xue bao = Acta genetica Sinica,
M V Zabolotskaia, and E A Nosovskaia, and M A Kaplun, and I A Tsaplina, and T V Akimkina
Purification and characterization of a thermostable alkaline protease from Thermoactinomyces sp. E79 and the DNA sequence of the encoding gene.
May 1996, Bioscience, biotechnology, and biochemistry,
Copied contents to your clipboard!