Surface-film microheterotrophs: amino acid metabolism and solar radiation effects on their activities
β Scribed by A. F. Carlucci; D. B. Craven; S. M. Henrichs
- Publisher
- Springer-Verlag
- Year
- 1985
- Tongue
- English
- Weight
- 926 KB
- Volume
- 85
- Category
- Article
- ISSN
- 0025-3162
No coin nor oath required. For personal study only.
β¦ Synopsis
Rates of microheterotrophic utilization (incorporation+ respiration) of ~H-leucine and 3H-glutamic acid were measured in seawater surface films from oligotrophic, eutrophic and mesotrophic waters incubated in situ off Baja California in July 1981 and off Southern California in November 1982. Neither visible nor ultraviolet radiation had a marked detrimental effect on microbial heterotrophy, although solar radiation sometimes appeared to be stimulatory. Film microheterotrophs utilized glutamic acid at rates between 0.07 and 0.13 nMh -1 for oligotrophic waters and between 0.43 and 2.1 nMh -1 for eutrophic waters; the respective turnover times ranged between 101 and 313 h and between 8.6 and 21.5 h. Film microheterotrophs from oligotrophic waters utilized leucine at rates comparable to those observed for glutamic acid, but turnover times were shorter. Leucine metabolism rates of film microheterotrophs in eutrophic waters were slower than glutamic acid rates, but turnover times were similar. Naturally varying amino acid concentrations accounted, in part, for differences in turnover times. In oligotrophic waters, higher utilization rates were observed for surfacefilm microheterotrophs than for subsurface (10 cm) microheterotrophs, whereas in eutrophic waters, utilization rates were similar for surface-film microheterotrophs and subsurface microheterotrophs. Surface-film microheterotrophs, in most cases, had an average of 63% amino acid carbon assimilation efficiency, similar to euphotic-zone heterotrophs. Surface-film microheterotrophs are actively involved in the metabolism and turnover of amino acids.
π SIMILAR VOLUMES
## Abstract Covalent modification of purified __Trigonopsis variabilis__ Dβamino acid oxidase using maleimideβactivated poly(ethylene glycol) 5000 yielded a stable bioconjugate in which three surfaceβexposed cysteine side chains were selectively derivatized. Compared with the native enzyme, the PEG