3P108 Creation of cold-adapted subtilisin by directed evolution
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چکیده
منابع مشابه
Directed evolution on the cold adapted properties of TAB5 alkaline phosphatase.
Psychrophilic alkaline phosphatase (AP) from the Antarctic strain TAB5 was subjected to directed evolution in order to identify the key residues steering the enzyme's cold-adapted activity and stability. A round of random mutagenesis and further recombination yielded three thermostable and six thermolabile variants of the TAB5 AP. All of the isolated variants were characterised by their residua...
متن کاملCold adaptation of a mesophilic subtilisin-like protease by laboratory evolution.
Enzymes isolated from organisms native to cold environments generally exhibit higher catalytic efficiency at low temperatures and greater thermosensitivity than their mesophilic counterparts. In an effort to understand the evolutionary process and the molecular basis of cold adaptation, we have used directed evolution to convert a mesophilic subtilisin-like protease from Bacillus sphaericus, SS...
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Pubfic reporting burden for this collection of infon gathering and maintaining the data needed, and ct collection of information, including suggestions for reducing L... ~....^--, n.~-~~ tn-in* mo Da" is Highway, Suite 1204. Arlington, VA 22202-4302. and to the Office of Management and Budget, Paperwork Reduct.on Project (0704-018 Washington, DC 20503. 1. AGENCY USE ONLY (Leave blank) 2. REPORT...
متن کاملDirected evolution of subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide.
Sequential rounds of error-prone PCR to introduce random mutations and screening of the resultant mutant libraries have been used to enhance the total catalytic activity of subtilisin E significantly in a non-natural environment, aqueous dimethylformamide (DMF). Seven DNA substitutions coding for three new amino acid substitutions were identified in a mutant isolated after two additional genera...
متن کاملCreation of GPCR-based chemical sensors by directed evolution in yeast.
G protein-coupled receptors (GPCRs) form a class of biological chemical sensors with an enormous diversity in ligand binding and sensitivity. To explore structural aspects of ligand recognition, we subjected the human UDP-glucose receptor (P2Y14) functionally expressed in the yeast Saccharomyces to directed evolution. We sought to generate new receptor subtypes with ligand-binding properties th...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2004
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.44.s216_4