pH-Dependent Inactivation of Enzymes by Microbubbling of Supercritical Carbon Dioxide

Hiroya Ishikawa, Takashi Yoshimura, Miwa Kajihara, Mitsuya Shimoda, Kiyoshi Matsumoto, Yutaka Osajima

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10 Citations (Scopus)

Abstract

The effect of pH on the inactivation of some enzymes (acid protease, alkaline protease, papain, and glucoamylase) dissolved in McIlvaine buffer by microbubble supercritical (SC) CO2 treatment was investigated in the range of pH 3 to pH 6. Remarkable inactivation was observed with this treatment at pH less than 4, whereas with gaseous and liquid CO2 treatments little or no important inactivation occurred. Microbubbling of SC-CO2 at lower pH was effective at 40-50°C. Microbubbling of SC-CO2 at pH 3 inactivated completely enzymes at temperatures 25 ° lower than that of the thermal treatment (65-75°C). The degree of inactivation in acid protease increased with increasing ethanol concentration.

Original languageEnglish
Pages (from-to)212-215
Number of pages4
JournalFood Science and Technology Research
Volume6
Issue number3
DOIs
Publication statusPublished - Aug 2000

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Food Science
  • Chemical Engineering(all)
  • Industrial and Manufacturing Engineering
  • Marketing

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    Ishikawa, H., Yoshimura, T., Kajihara, M., Shimoda, M., Matsumoto, K., & Osajima, Y. (2000). pH-Dependent Inactivation of Enzymes by Microbubbling of Supercritical Carbon Dioxide. Food Science and Technology Research, 6(3), 212-215. https://doi.org/10.3136/fstr.6.212