novel Ca2+-activated, thermostabilized polyesterase capable of hydrolyzing polyethylene terephthalate from Saccharomonospora viridis AHK190

Only two polyethylene glycol terephthalate (PET)-degrading enzymes have been reported, and their mechanism for the biochemical degradation of PET remains unclear. To identify a novel PET-degrading enzyme, a putative cutinase gene (cut190) was cloned from the thermophile Saccharomonospora viridis AHK...

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Veröffentlicht in:	Applied microbiology and biotechnology 2014-12, Vol.98 (24), p.10053-10064
Hauptverfasser:	Kawai, Fusako, Oda, Masayuki, Tamashiro, Tomonari, Waku, Tomonori, Tanaka, Naoki, Yamamoto, Masaki, Mizushima, Hiroki, Miyakawa, Takuya, Tanokura, Masaru
Format:	Artikel
Sprache:	eng
Schlagworte:	Actinobacteria - enzymology Actinobacteria - genetics Biomedical and Life Sciences Biotechnologically Relevant Enzymes and Proteins Biotechnology Calcium - metabolism Cations, Divalent - metabolism Circular Dichroism Cloning, Molecular cutinase DNA Mutational Analysis Enzyme Activators - metabolism enzyme activity Enzyme Stability Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Gene Expression genes glycerol Hydrogen-Ion Concentration Hydrolases - chemistry Hydrolases - genetics Hydrolases - isolation & purification Hydrolases - metabolism industrial applications Life Sciences Microbial Genetics and Genomics Microbiology Mutant Proteins - chemistry Mutant Proteins - genetics Mutant Proteins - isolation & purification Mutant Proteins - metabolism mutants polyethylene glycol polyethylene terephthalates Polyethylene Terephthalates - metabolism Protein Conformation - drug effects Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism recycling Saccharomonospora viridis Temperature thermal stability thermophilic microorganisms
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