• Title/Summary/Keyword: acitivity of L-aspartylphenyl-alanine methyl ester ammonia lyase

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Microbial Aspartase and Its Activity on Deamination of L-Aspartyl-L-Phenylalanine Methyl Eester

  • Chang, Wonyoon;Goo, Yang-Mo
    • Archives of Pharmacal Research
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    • v.11 no.2
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    • pp.139-144
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    • 1988
  • Examination of many microorganisms and soil isolated for the activity of aspartase proved that R, rubra, G, suboxydans, A. versicolor, P. purpurogenum, E. coli, Ps. aeruginosa, A. gigantus, A, unguis, A. parasiticus and a soil isolate (S-90) had high activity of aspartase. Comparison of the activity of the aspartase by cell free extracts of these microorganisms with the activity of the enzyme catalyzing the deamination of aspartame by the same cell free extracts showed similar kinetic characteristics. The aspartase existing in the cell free extracts seemed to catalyze the deamination of aspartame, too.

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