Further Stabilization of Earthworm Serine Protease by Chemical Modification and Immobilization.

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  • NAKAJIMA Nobuyoshi
    <i>Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University</i>
  • ISHIHARA Kohji
    <i>Department of Chemistry, Kyoto University of Education</i>
  • SUGIMOTO Manabu
    <i>Research Institute for Bioresources, Okayama University</i>
  • NAKAHARA Takashi
    <i>Graduate School of Health and Welfare Science, Okayama Prefectural University</i>
  • TSUJI Hideaki
    <i>Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University</i>

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  Earthworm serine protease is more stable and is less affected by organic solvents and detergent than other proteases. However, it is inactivated, probably by autolysis, at 60°C or above under alkaline conditions. Further stabilization was managed by chemical modification of the enzyme with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide and phenylglyoxal to protect the activity from the autolytic inactivation. Stabilization was possible also under acidic conditions, in which the stability of the enzyme was rather low, by immobilization with folded sheet mesoporous material. Thus, further stabilization of the enzyme has been achieved by chemical modification or immobilization.<br>

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