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Enzyme‐Catalyzed Reactions as Influenced by Inert Gases at High Pressures
Author(s) -
BEHNKE J. R.,
FENNEMAand O.,
POWRIE W. D.
Publication year - 1969
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1969.tb10368.x
Subject(s) - chemistry , invertase , tyrosinase , inert , trypsin , enzyme , inert gas , oxygen , nitrogen , chymotrypsin , catalysis , biochemistry , organic chemistry
SUMMARY — The activities of tyrosinase, invertase, trypsin and chymotrypsin were studied after exposure to one or more of the following high‐pressure inert gases: N 2 O at 600 psig or N 2 or Ar each at 5000 psig. Exposure to high‐pressure nitrogen or argon failed to significantly inhibit the rate of tyrosinase activity in fluid systems. However, the rates of tyrosinase‐catalyzed reactions in shell‐cast gelatin gels were significantly depressed by exposure to high‐pressure nitrogen, and even more so by high‐pressure nitrous oxide. This inhibition proved to be oxygen dependent and reversible. Pressurization experiments with invertase, trypsin and chymotrypsin indicated that high‐pressure N 2 O did not significantly inhibit these enzymes. This lends support to the hypothesis that high‐pressure inert gases inhibited tyrosinase activity in nonfluid systems by decreasing the availability of oxygen, rather than by physically altering the enzyme. It must be concluded that there is little hope that the enzymes in food systems can be effectively inhibited by brief exposure to inert gases at pressures of 5000 psig or less.