Ion exchange of β-galactosidase: The effect of the immobilization pH on enzyme stability
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- 作者：Tiago L. de Albuquerquea ; b ; 1 ; Sara Peircea ; c ; 1 ; Nazzoly Ruedad ; Antonio Marzocchellac ; Luciana R.B. Gonç ; alvesb ; Maria Valderez Ponte Rochab ; Roberto Fernandez-Lafuentea ; rfl@icp.csic.es" class="auth_mail" title="E-mail the corresponding author ; rfernandezlafuente@hotmail.com" class="auth_mail" title="E-mail the corresponding author
- 关键词：Ionic exchange ; Enzyme-support orientation ; Enzyme stability ; β-Galactosidase ; Biocatalyst design
- 刊名：Process Biochemistry
- 出版年：2016
- 出版时间：July 2016
- 年：2016
- 卷：51
- 期：7
- 页码：875-880
- 全文大小：786 K
文摘
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The enzyme β-galactosidase could be adsorbed on MANAE support at pH 5–9.
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Activity was almost fully preserved.
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The enzyme remained immobilized at 25 mM of buffers.
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The stability strongly depended on the immobilization pH value.
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Under certain conditions, some preparations were more stable than free enzyme.