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Some properties of a protease (subtilisin BPN') immobilized to porous glass

Biotechnology and Bioengineering

Dec 1, 1975

Jeff D Chapman, Herbert O Hultin

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Abstract

Subtilisin BPN' was immobilized to porous glass via isothiocyanate coupling. The pH optimum of the enzyme was shifted to the alkaline side on binding. This effect was more pronounced with ethyl lactate than with N-tosyl arginine methyl ester (TAME). Presumably, the shift is a reflection...read more

Mentioned in this Paper

Lactates
Subtilisin 72
Hydrogen-Ion Concentration
Glass (Substance)
Tosylarginine Methyl Ester
Surface Properties
Paper Details
References
    • References10
    • Citations4
    • References10
    • Citations4
  • Some properties of a protease (subtilisin BPN') immobilized to porous glass

    Biotechnology and Bioengineering

    Dec 1, 1975

    Jeff D Chapman, Herbert O Hultin

    PMID: 1122

    DOI: 10.1002/bit.260171208

    Abstract

    Subtilisin BPN' was immobilized to porous glass via isothiocyanate coupling. The pH optimum of the enzyme was shifted to the alkaline side on binding. This effect was more pronounced with ethyl lactate than with N-tosyl arginine methyl ester (TAME). Presumably, the shift is a reflection...read more

    Mentioned in this Paper

    Lactates
    Subtilisin 72
    Hydrogen-Ion Concentration
    Glass (Substance)
    Tosylarginine Methyl Ester

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    Paper Details
    References
    • References10
    • Citations4
    • References10
    • Citations4
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