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Results 1 - 4 of 4
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.39environmental protection bacteria containing the genes encoding for biphenyl 2,3-dioxygenase (bphA) or 2,3-dihydroxybiphenyl 1,2-dioxygenase (bphC) are detected in 29 of the 32 samples of Dehalobacter, Dehalogenimonas and Dehalococcoides from bioretention cell media as well as surface stormwater sediment samples from seven urban areas. In some samples, both the putative OHR and functional genes encoding enzymes for biphenyl degradation are found, indicating the potential of the cooccurrence of simultaneous aerobic and anaerobic polychlorinated biphenyls respiration 764680
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.39more construction of a multistep conversion system of para-substituted phenols by recombinant phenol hydroxylase and 2,3-dihydroxybiphenyl 1,2-dioxygenase using substrates 4-fluorophenol, 4-chlorophenol, 4-bromophenol, 4-nitrophenol, and 4-cresol, mass spectrometric product analysis, overview -, 723977
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.39more immobilization of the enzyme BphC on mesoporous silica SBA-15 in order to improve its stability with relatively high retaining activities. By Fourier transformed infrared spectroscopy (FTIR) and N2 adsorption/desorption isotherms, BphC is confirmed to be successfully adsorbed and captured on SBA-15. Under the experimental conditions, the maximum loading amount reaches 124.6 mg protein/g support at pH 6.0. The immobilized BphC is more stable at 4°C than the free enzyme and the thermostability of BphC is significantly improved by immobilization compared to the wild-type enzyme, while the catalytic efficiency with biphenyl-2,3-diol is reduced. The activity and stability alteration occur due to the changes of secondary structure of BphC. Mechanism of immobilization -, 743118
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.39more usage of the enzyme for construction of a catechol biosensor, method development involving Plackett–Burman design and response surface methodology, overview. Maximal specific activity of BphC_LA-4 is about 0.58 U/mg with catechol as substrate. the BphC_LA-4 enzyme electrode prepared by SiO2 sol–gel shows good response to all these three catecholic compounds -, 724567
Results 1 - 4 of 4