caa a22 4500 477101666 CHVBK 20180405111543.0 cr unu---uuuuu 170330e19960701xx s 000 0 eng 10.1007/BF00195736 doi (NATIONALLICENCE)springer-10.1007/BF00195736 Dimethylsulfoniopropionate lyase from the marine macroalga Ulva curvata [Elektronische Daten] purification and characterization of the enzyme [M. de Souza, Y. Chen, D. Yoch] This is a report on the purification and characterization of an algal dimethylsulfoniopropionate (DMSP) lyase. This enzyme, also found in bacteria, is responsible for producing most of the dimethylsulfide (DMS) in marine environments. It was purified from the green macroalga, Ulva curvata (Kützing) De Toni. Initial in-vivo experiments showed that DMSP lyase activity from endogenous DMSP in Ulva increased for 24 h and then decreased as the culture aged and endogenous DMSP levels were depleted. When amended with exogenous DMSP, rates of DMSP lyase activity remained high even when the culture was 5 d old. Following disruption of the DMSP-depleted U. curvata cells by grinding, a soluble DMSP lyase was purified. This enzyme is a monomer of 78 kDa which has a K m for DMSP of 0.52 mM. Soluble DMSP lyase had an optimum pH of 8 and an optimum osmotic strength of 75 mM NaCl. Following disruption of the algae by either grinding with sand or blending, and washing out the soluble enzyme, the green tissue, when treated with the non-ionic detergent, Triton X-100, solubilized additional DMSP lyase activity. Three hydrophobic variant forms of Ulva DMSP lyase were isolated and partially characterized from the detergent-solubilized activity. While the molecular and kinetic properties of the algal enzyme are different from the bacterial enzymes we purified earlier, both the soluble and membrane-bound forms did, nevertheless, cross-react with antibodies raised against the bacterial (Alcaligenes strain M3A) DMSP lyase. Springer-Verlag, 1996 Dimethylsulfide nationallicence DMSP nationallicence DMS nationallicence Sulfur cycling nationallicence DMS : dimethylsulfide nationallicence DMSP : dimethylsulfoniopropionate nationallicence de Souza M. Department of Biological Sciences, University of South Carolina, 29208, Columbia, SC, USA aut Chen Y. Department of Biological Sciences, University of South Carolina, 29208, Columbia, SC, USA aut Yoch D. Department of Biological Sciences, University of South Carolina, 29208, Columbia, SC, USA aut Planta Springer-Verlag 199/3(1996-07-01), 433-438 0032-0935 199:3<433 1996 199 425 https://doi.org/10.1007/BF00195736 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00195736 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- de Souza M. Department of Biological Sciences, University of South Carolina, 29208, Columbia, SC, USA aut NATIONALLICENCE 700 1- Chen Y. Department of Biological Sciences, University of South Carolina, 29208, Columbia, SC, USA aut NATIONALLICENCE 700 1- Yoch D. Department of Biological Sciences, University of South Carolina, 29208, Columbia, SC, USA aut NATIONALLICENCE 773 0- Planta Springer-Verlag 199/3(1996-07-01), 433-438 0032-0935 199:3<433 1996 199 425 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer