Biomolecules are unstable under "black smoker" conditions

The effects of high hydrostatic pressure on hydrolysis and hydrothermal degrdn. of amino acids, polyglycine, and thermophilic bacteria were studied. Most amino acids, after 6 h incubation on 250 Deg and 260 bar, pH 2 and 7.6, were transformed or decompd. Glycine, alanine, and NH3 increased drastically, suggesting that they are degrdn. products. To det. the stability of the peptide bond, polyglycine was subjected for 6 h to 253 Deg, 260 bar pressure at pH 7.0. Complete hydrolysis was found at 6 h. Similarly, Pyrodictium occultum cells incubated at 260 Deg, 260 bar for 6 h suffered pronounced hydrolysis and amino acid degrdn. The ability of thermophiles to survive at these high temps. is discussed