| martelella mediterranea gen. nov., sp. nov., a novel alpha-proteobacterium isolated from a subterranean saline lake. | a bacterial strain was isolated from the water of lake martel in mallorca (spain). the isolate, designated macl11(t), was halotolerant and strictly aerobic. the cells were non-motile, non-spore-forming, gram-negative short rods. comparative 16s rrna gene sequence analysis revealed that macl11(t) represents a separate line of descent within the order 'rhizobiales' of the class 'alphaproteobacteria'. strain macl11(t) was most closely related to the genera rhizobium (93.3 % sequence similarity to r ... | 2005 | 15774691 |
| gene diversity of cyp153a and alkb alkane hydroxylases in oil-degrading bacteria isolated from the atlantic ocean. | alkane hydroxylases, including the integral-membrane non-haem iron monooxygenase (alkb) and cytochrome p450 cyp153 family, are key enzymes in bacterial alkane oxidation. although both genes have been detected in a number of bacteria and environments, knowledge about the diversity of these genes in marine alkane-degrading bacteria is still limited, especially in pelagic areas. in this report, 177 bacterial isolates, comprising 43 genera, were obtained from 18 oil-degrading consortia enriched from ... | 2010 | 20148932 |
| a novel cold-active and alkali-stable β-glucosidase gene isolated from the marine bacterium martelella mediterranea. | a β-glucosidase gene designated gluc3m was cloned through construction of a genomic library of martelella mediterranea 2928. the gluc3m consisted of 2,496 bp and encoded a peptide of 832 amino acids that shared the greatest amino acid similarity (59%) with a β-glucosidase of family 3 glycoside hydrolase from agrobacterium radiobacter k84. the optimum reaction temperature and ph of gluc3m were 45 °c and 8.0, respectively. the k (m) and v (max) for p-nitrophenyl-β-d: -glucopyranoside were 0.18 mg/ ... | 2010 | 20503105 |
| molecular cloning, purification, and characterization of a novel, acidic, ph-stable endoglucanase from martelella mediterranea. | a novel gene encoding an endoglucanase designated cel5d was cloned from a marine bacterium martelella mediterranea by genomic library. the gene had a 1,113 bp opening reading frame encoding a 371-amino-acid protein with a molecular mass of 40,508 da and containing a putative signal peptide (41 amino acids). cel5d had low similarity (48-51% identity) with other known endoglucanases and consisted of one single catalytic domain, which belonged to the glycosyl hydrolase family 5. the maximum activit ... | 2010 | 20571959 |