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321.
Ingrid Hauser Aslak Einbu Kjetill Østgaard Hallvard F. Svendsen Francisco J. Cervantes 《Biotechnology letters》2013,35(2):219-224
Nitrogen and organic matter removal from reclaimer waste of a monoethanolamine (MEA) based CO2-capture plant was demonstrated in a pre-denitrification biofilm system. The reclaimer waste was generated from a 30 % (w/w) MEA solvent used for capturing CO2 from flue gas from a coal-fired power plant. MEA, N-(2-hydroxylethyl)glycine (HEGly) and 2-hydroxyethylformamide (HEF) were the major contaminants treated. Hydrolysis of MEA to ammonia and further oxidation of organic intermediates readily occurred in the pre-denitrification system with a hydraulic retention time of 7 h. The biofilm system achieved 98 ± 1 % removal of MEA and 72 ± 16 % removal of total nitrogen. This is the first demonstration of efficient biodegradation of real amine waste from a post-combustion CO2 capture facility by pre-denitrification without external electron donor. 相似文献
322.
Mats Holmquist Ib Groth Clausen Shamkant Patkar Allan Svendsen Karl Hult 《Journal of Protein Chemistry》1995,14(4):217-224
To reveal the functional role of Glu87 and Trp89 in the lid ofHumicola lanuginosa lipase, site-directed mutagenesis at Glu87 and Trp89 was carried out. The catalytic performance of wild-type and mutated lipases was studied in transesterification reactions in cyclohexane at a controlled water activity. Two different acyl donors were used in the investigation: tributyrin, a natural substrate for a lipase, and vinyl butyrate, an activated ester suitable for fast and efficient lipase-catalyzed transformations in preparative organic synthesis. As acyl acceptor 1-heptanol was used. The Glu87Ala mutation decreased theV
max,app value with tributyrin and vinyl butyrate by a factor of 1.5 and 2, respectively. TheK
m,app for tributyrin was not affected by the Glu87Ala mutation, but theK
m,app for vinyl butyrate increased twofold compared to the wild-type lipase. Changing Trp89 into a Phe residue afforded an enzyme with a 2.7- and 2-fold decreasedV
max,app with the substrates tributyrin and vinyl butyrate, respectively, compared to the wild-type lipase. No significant effects on theK
m,app values for tributyrin or vinyl butyrate were seen as a result of the Trp89Phe mutation. However, the introduction of a Glu residue at position 89 in the lid increased theK
m,app for tributyrin and vinyl butyrate by a factor of >5 and 2, respectively. The Trp89Glu mutated lipase could not be saturated with tributyrin within the experimental conditions (0–680 mM) studied here. With vinyl butyrate as a substrate theV
max,app was only 6% of that obtained with wild-type enzyme. 相似文献