We assayed proteolytic enzymes in coastal surface seawater using 16 types of fluorogenic substrates, including those for aminopeptidase, trypsin, elastase, and chymotrypsin. Hydrolysis rates were similar or higher for substrates of trypsin and chymotrypsin than for those of aminopeptidase. Substrates for elastase were hardly hydrolyzed. The results strongly suggest trypsin‐type and chymotrypsin‐type endopeptidases and aminopeptidases were present in the seawater. In most previous studies of proteolytic enzymes in aquatic environments, leucine‐aminopeptidase activity measured using a fluorogenic substrate has been used as a model of proteolytic activity. From the results of this study using various peptide analog fluorogenic substrates, the significance of endopeptidases, which could play a key role in downsizing of dissolved proteins and polypeptides to oligopeptides prior to microbial respiration, was confirmed
We tested the stability and reaction of several amino acids using hydrothermal system simulators: an autoclave and two kinds of flow reactors at 200-250 °C. This study generally showed that there is a variation in the individual amino acids survivability in the simulators. This is mainly attributed to the following factors; heat time, cold quenching exposure, metal ions and also silica. We observed that, in a rapid heating flow reactor, high aggregation and/or condensation of amino acids could occur even during a heat exposure of 2 min. We also monitored their stability in a reflow-type of simulator for 120 min at 20 min intervals. The non-hydrolyzed and hydrolyzed samples for this system showed a similar degradation only in the absence of metal ions.
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