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341393 occurrences (No.55 in the rank) during 5 years in the PubMed. [no cache] 500 found
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341393 occurrences (No.55 in the rank) during 5 years in the PubMed. [no cache] 500 found
| 110) For example, 1 h-preincubation at 37 °C resulted in 100% loss of enzyme activity, while a counterpart from mesophilic Pseudomonas putida mt-2 did not show any negative effect on the initial enzyme activity. |
| PMID:23720227 DOI:10.1002/jobm.201300079 |
| 2015 Journal of basic microbiology |
| * Anthranilate degradation by a cold-adapted Pseudomonas sp. |
| - An alpine soil bacterium Pseudomonas sp. strain PAMC 25931 was characterized as eurypsychrophilic (both psychrophilic and mesotolerant) with a broad temperature range of 5-30 °C both for anthranilate (2-aminobenzoate) degradation and concomitant cell growth. Two degradative gene clusters (antABC and catBCA) were detected from a fosmid clone in the PAMC 25931 genomic library; each cluster was confirmed to be specifically induced by anthranilate. When expressed in Escherichia coli, the recombinant AntABC (anthranilate 1,2-dioxygenase, AntDO) converted anthranilate into catechol, exhibiting strict specificity toward anthranilate. Recombinant CatA (catechol 1,2-dioxygenase, C12O) from the organism was active over a broad temperature range (5-37 °C). However, CatA rapidly lost the enzyme activity when incubated at above 25 °C. For example, 1 h-preincubation at 37 °C resulted in 100% loss of enzyme activity, while a counterpart from mesophilic Pseudomonas putida mt-2 did not show any negative effect on the initial enzyme activity. These results suggest that CatA is a new cold-adapted thermolabile enzyme, which might be a product through the adaptation process of PAMC 25931 to naturally cold environments and contribute to its ability to grow on anthranilate there. |
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--- WordNet output for while ---